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        <title>Developmental and Comparative Immunology via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Developmental and Comparative Immunology' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Developmental+and+Comparative+Immunology&t=Developmental+and+Comparative+Immunology&s=Search&f=source]]></link>
        <lastBuildDate>Sat, 21 Nov 2009 13:38:53 +0100</lastBuildDate>
        <item>
            <title>Caenopore-5: The tHREE-DIMENSIONAL structure of an antimicrobial protein from Caenorhabditis elegans.</title>
            <link>http://www.medworm.com/index.php?rid=3004330&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19917307%26dopt%3DAbstract</link>
            <description>Authors: Mysliwy J, Dingley AJ, Stanisak M, Jung S, Lorenzen I, Roeder T, Leippe M, Gr&amp;#xF6;tzinger J
    The caenopore-5 protein encoded by the spp-5 gene is one of 33 caenopores identified in Caenorhabditis elegans and is a pore-forming peptide which plays an important role in the elimination of Escherichia coli ingested by the worm. Thus, caenopore-5 appears to contribute to the nutrition of the worm while simultaneously protecting the organism against pathogens. Here, three-dimensional heteronuclear NMR spectroscopy was used to solve the solution structure of caenopore-5. The NMR data revealed that two conformers of caenopore-5 exist in solution which differ by the isomerisation of the peptide bond of Pro-81. The overall structure of the two caenopore-5 conformers consists of five amph...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3004330</comments>
            <pubDate>Fri, 13 Nov 2009 00:00:00 +0100</pubDate>
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        <item>
            <title>Variation in the ovine C-type lectin dectin-1 gene (CLEC7A).</title>
            <link>http://www.medworm.com/index.php?rid=3004331&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19914281%26dopt%3DAbstract</link>
            <description>In this study, variation in exons 4-6 of the ovine dectin-1 gene (CLEC7A) was investigated. These exons encode the putative domain for beta-glucan recognition. Three, three and four unique PCR-single strand conformational polymorphism (PCR-SSCP) patterns were detected in exons 4, 5 and 6, respectively. DNA sequencing also revealed three, three and four different nucleotide sequences for the respective exons. All of these sequences were unique, but shared high sequence homology with the CLEC7A cDNA sequences from sheep, cattle and pigs. Either one, or a combination of two sequences was found for each exon in each sheep. This suggests that these sequences represent allelic variants of the ovine CLEC7A gene, although only defined within the exons investigated. The sequence data confirmed four...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3004331</comments>
            <pubDate>Thu, 12 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3004331</guid>        </item>
        <item>
            <title>Detection of antimicrobial peptides related to piscidin 4 in important aquacultured fish.</title>
            <link>http://www.medworm.com/index.php?rid=3004333&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913049%26dopt%3DAbstract</link>
            <description>In this study, we detected the presence of the recently discovered piscidin 4 via bug blot, Western blot, ELISA and/or immunohistochemistry in striped bass (Morone saxatilis), white bass (M. chrysops), European seabass (Dicentrarchus labrax), gilthead seabream (Sparus aurata), red drum (Sciaenops ocellatus), and barramundi (Lates calcarifer). Via bug blot, gill extracts from all species had antibacterial activity corresponding to the migration rate of piscidin 4. Western blotting showed that piscidin 4 immunoreactivity was greatest in striped bass gill extract. The concentrations of piscidin 4 detected by the ELISA in striped bass gill ( approximately 20mug/ml) were well within the levels that are inhibitory to important fish bacterial pathogens. Piscidin 4 was also detected via immunohist...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3004333</comments>
            <pubDate>Tue, 10 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3004333</guid>        </item>
        <item>
            <title>Trypanosoma carassii calreticulin binds host complement component C1q and inhibits classical complement pathway-mediated lysis.</title>
            <link>http://www.medworm.com/index.php?rid=3004332&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19913050%26dopt%3DAbstract</link>
            <description>Authors: Oladiran A, Belosevic M
    Trypanosoma carassii is an extracellular parasite of economically important fish species that has evolved several strategies to circumvent host immune responses. Proteomic analysis of the excreted/secreted (ES) and surface molecules of the parasite has revealed a number of proteins that may be involved in host-parasite interactions. Among the parasite molecules identified in the ES of T. carassii was calreticulin. We cloned and produced T. carassii calreticulin (rTcaCRT), and generated a rabbit polyclonal antibody to the recombinant protein. The incubation of parasites with rabbit anti-rTcaCRT affinity purified IgG antibody indicated substantial CRT levels on the surface of trypanosomes, as well as internal structures of permeabilized organisms. Recombi...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3004332</comments>
            <pubDate>Tue, 10 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3004332</guid>        </item>
        <item>
            <title>Binding properties of the regulatory domains in Manduca sexta hemolymph proteinase-14, an initiation enzyme of the prophenoloxidase activation system.</title>
            <link>http://www.medworm.com/index.php?rid=2985720&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19900472%26dopt%3DAbstract</link>
            <description>Authors: Wang Y, Jiang H
    Pathogen recognition and rapid initiation of defense responses are essential for the survival of host insects. In Manduca sexta, hemolymph proteinase-14 precursor (proHP14) senses non-self presence and triggers a branched serine proteinase pathway which leads to prophenoloxidase activation and melanin formation around the invading organisms. To understand functions of individual domains in HP14, we have produced a series of HP14 domains and truncation mutants and studied their interactions with microbial polysaccharides and beta-1,3-glucan recognition protein-1 (betaGRP1)-a biosensor for fungal and bacterial infection. These include: the low-density lipoprotein receptor class A repeats 1-5 (LDL(1-5)), Sushi domain, Wonton domain, and proteinase catalytic domain...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2985720</comments>
            <pubDate>Fri, 06 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2985720</guid>        </item>
        <item>
            <title>The amphibians Xenopuslaevis and Silurana tropicalis possess a family of activating KIR-related Immunoglobulin-like receptors.</title>
            <link>http://www.medworm.com/index.php?rid=2978307&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19896971%26dopt%3DAbstract</link>
            <description>In this study, we searched the amphibian species Xenopus laevis and Silurana (Xenopus) tropicalis for the presence of genes homologous to mammalian KIRs and avian CHIRs (KRIR family). By experimental and computational procedures, we identified four related ILR (Ig-like receptors) genes in S. tropicalis and three in X. laevis. ILRs encode type I transmembrane receptors with 3-4 Ig-like extracellular domains. All predicted ILR proteins appear to be activating receptors. ILRs have a broad expression pattern, the gene transcripts were found in both lymphoid and non-lymphoid tissues. Phylogenetic analysis shows that the amphibian KRIR family receptors evolved independently from their mammalian and avian counterparts. The only conserved structural element of tetrapod KRIRs is the NxxR motif-cont...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2978307</comments>
            <pubDate>Thu, 05 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2978307</guid>        </item>
        <item>
            <title>Molecular cloning and functional characterization of caspase 9 in large yellow croaker (Pseudosciaena crocea).</title>
            <link>http://www.medworm.com/index.php?rid=2970479&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19887081%26dopt%3DAbstract</link>
            <description>Authors: Mu Y, Xiao X, Zhang J, Ao J, Chen X
    The genomic and cDNA sequences of a caspase-9 homologue were cloned from large yellow croaker (Pseudosciaena crocea). The large yellow croaker caspase 9 gene (Lyccasp9) consists of ten exons and nine introns, spanning 3836 nucleotides. The full- length cDNA of Lyccasp9 is 2595bp with an open reading frame of 1314bp encoding a polypeptide of 437 amino acids (aa), which includes a 90-aa caspase recruitment domain (CARD, residues 1-90), a 133-aa p20 domain (residues 171-303) with two putative caspase family histidine and cysteine active sites, as well as an 87-aa p10 domain (residues 348-435). Recombinant Lyccasp9 (rLyccasp9) demonstrated obvious proteolytic activity. However, when histidine(249) in the histidine active site was replaced by asp...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2970479</comments>
            <pubDate>Sat, 31 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2970479</guid>        </item>
        <item>
            <title>Sp185/333: A novel family of genes and proteins involved in the purple sea urchin immune response.</title>
            <link>http://www.medworm.com/index.php?rid=2970478&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19887082%26dopt%3DAbstract</link>
            <description>Authors: Ghosh J, Buckley KM, Nair SV, Raftos DA, Miller C, Majeske AJ, Hibino T, Rast JP, Roth M, Smith LC
    The Sp185/333 system of genes, messages and proteins are expressed in the coelomocytes of the purple sea urchin, Strongylocentrotus purpuratus, and is an extraordinary example of diversification of a putative innate immune response system in an invertebrate. Reviewed here, is the current understanding of this complex system as illustrated by sequence comparisons of the genes, message and deduced proteins with descriptions of diversity, including preliminary results on genomic organization and descriptions of 185/333 in other echinoids. Sp185/333 gene expression in adults and embryos occurs in response to immune challenge and includes changes in the frequencies of Sp185/333-positi...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2970478</comments>
            <pubDate>Sat, 31 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2970478</guid>        </item>
        <item>
            <title>Two recombinant peptides, SpStrongylocin 1 and 2, from Strongylocentrotus purpuratus, show antimicrobial activity against Gram positive and Gram negative bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=2929692&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19852980%26dopt%3DAbstract</link>
            <description>Authors: Li C, Blencke HM, Smith LC, Karp MT, Stensv&amp;#xE5;g K
    The cysteine-rich strongylocins were the first antimicrobial peptides (AMPs) discovered from the sea urchin species, Strongylocentrotus droebachiensis. Homologous putative proteins (called SpStrongylocin) were found in the sister species, S. purpuratus. To demonstrate that they exhibit the same antibacterial activity as strongylocins, cDNAs encoding the 'mature' peptides (SpStrongylocin 1 and 2) were cloned into a direct expression system fusing a protease cleavage site and two purification tags to the recombinant peptide. Both recombinant fusion peptides were expressed in a soluble form in an Escherichia coli strain tolerant to toxic proteins. Enterokinase was used to remove the fusion tags and purified recombinant SpStrong...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2929692</comments>
            <pubDate>Tue, 20 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2929692</guid>        </item>
        <item>
            <title>Molecular cloning and functional characterization of porcine DNA-dependent activator of IFN-regulatory factors (DAI).</title>
            <link>http://www.medworm.com/index.php?rid=2925006&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19850075%26dopt%3DAbstract</link>
            <description>Authors: Xie L, Fang L, Wang D, Luo R, Cai K, Chen H, Xiao S
    The DNA-dependent activator of IFN-regulatory factors (DAI) is a recently identified DNA sensor for intracellular DNA that triggers a signal for the production of type I IFN. Here we report the cloning and characterization of porcine DAI (poDAI). The full-length of poDAI encodes 439 amino acids, contains two N-terminal DNA-binding domains and shows similarity to mouse, rat, dog, monkey, human, horse and cattle counterparts ranging from 44% to 67%. poDAI mRNA expression was mainly detected in spleen, lung, kidney and small intestine. Over-expression of poDAI activated transcription factors IRF3 and NF-kappaB and induced IFN-beta in different porcine cell lines, but to varying degrees. Deletion mutant analysis revealed that bot...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2925006</comments>
            <pubDate>Mon, 19 Oct 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">2925006</guid>        </item>
        <item>
            <title>Hovering between death and life: natural apoptosis and phagocytes in the blastogenetic cycle of the colonial ascidian Botryllus schlosseri.</title>
            <link>http://www.medworm.com/index.php?rid=2913032&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19837108%26dopt%3DAbstract</link>
            <description>Authors: Cima F, Manni L, Menin A, Basso G, Fortunato E, Accordi B, Schiavon F, Ballarin L
    Colonies of the compound ascidian Botryllus schlosseri undergo recurrent generation changes during which massive, natural apoptosis occurs in zooid tissues: for this reason the species is emerging as an interesting model of invertebrate chordate, phylogenetically related to vertebrates, for studies of apoptosis during development. In the present work, we carried out a series of morphological, cytofluorimetrical and biochemical analyses, useful for a better characterization of Botryllus apoptosis. Results are consistent with the following vewpoints: i) both intrinsic and extrinsic pathways, probably connected by the BH3-only protein Bid, are involved in cell death induction; ii) phagocytes, once l...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2913032</comments>
            <pubDate>Wed, 14 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2913032</guid>        </item>
        <item>
            <title>The Role of Lysozyme in the Prophenoloxidase Activation System of Manduca sexta: An in vitro approach.</title>
            <link>http://www.medworm.com/index.php?rid=2913033&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19835909%26dopt%3DAbstract</link>
            <description>In this study, we used in vitro assays to investigate the role of lysozyme in proPO activation in the tobacco hornworm Manduca sexta. We showed that lysozymes from M. sexta, human milk and hen egg white did not inhibit PO activity in the pre-activated na&amp;#xEF;ve plasma of M. sexta larvae, but significantly inhibited proPO activation in the na&amp;#xEF;ve plasma. Western blot analysis showed that direct incubation of M. sexta lysozyme with the na&amp;#xEF;ve plasma prevented conversion of proPO to PO, but stimulated degradation of precursor proteins for serine proteinase homolog-2 (SPH2) and proPO-activating proteinase-1 (PAP1), two key components required for proPO activation. Far-western blot analysis showed that M. sexta lysozyme and proPO interacted with each other. Altogether, our results sugg...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2913033</comments>
            <pubDate>Mon, 12 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2913033</guid>        </item>
        <item>
            <title>Identification, characterization and genetic mapping of TLR7, TLR8a1 and TLR8a2 genes in rainbow trout (Oncorhynchus mykiss).</title>
            <link>http://www.medworm.com/index.php?rid=2896190&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19825389%26dopt%3DAbstract</link>
            <description>Authors: Palti Y, Gahr SA, Purcell MK, Hadidi S, Rexroad CE, Wiens GD
    Induction of the innate immune pathways is critical for early antiviral defense but there is limited understanding of how teleost fish recognize viral molecules and activate these pathways. In mammals, Toll-like receptors (TLR) 7 and 8 bind single-stranded RNA of viral origin and are activated by synthetic antiviral imidazoquinoline compounds. Herein, we identify and describe the rainbow trout (Oncorhynchus mykiss) TLR7 and TLR8 gene orthologs and their mRNA expression. Two TLR7/8 loci were identified from a rainbow trout bacterial artificial chromosome (BAC) library using DNA fingerprinting and genetic linkage analyses. Direct sequencing of two representative BACs revealed intact omTLR7 and omTLR8a1 open reading fra...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2896190</comments>
            <pubDate>Fri, 09 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2896190</guid>        </item>
        <item>
            <title>INFLUENCE OF BREAST MILK polyamines on suckling rat IMMUNE SYSTEM MATURATION.</title>
            <link>http://www.medworm.com/index.php?rid=2896186&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19825390%26dopt%3DAbstract</link>
            <description>Authors: P&amp;#xE9;rez-Cano FJ, Gonz&amp;#xE1;lez-Castro A, Castellote C, Franch A, Castell M
    The aim of this study was to ascertain whether the supplementation of polyamines present in breast milk, i.e. spermine (SPM) and spermidine (SPD), influenced the post-natal maturation of the systemic and intestinal immune system in rats. From birth, pups daily received SPM or SPD. At 5, 11 and 18 days old, small intestine intraepithelial lymphocytes (IEL), lamina propria lymphocytes (LPL) and splenocytes were phenotypically characterized. SPM and, less evidently, SPD accelerated the maturation of CD8+ IEL, and enhanced the presence of intraepithelial NK cells and IEL related with specific immune responses on the proximal and distal small intestine, respectively. Polyamines increased the percentage of...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2896186</comments>
            <pubDate>Fri, 09 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2896186</guid>        </item>
        <item>
            <title>Identification of the functional Interleukin-2 binding domain of the chicken common cytokine receptor gamma chain.</title>
            <link>http://www.medworm.com/index.php?rid=2891083&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19819255%26dopt%3DAbstract</link>
            <description>Authors: Gu J, Teng Q, Huang Z, Ruan X, Zhou J
    CD132 is the common gamma chain to a number of cytokine receptor complexes including that for IL-2. To identify the functional domain of chicken CD132 (chCD132), the cDNA of chCD132 was cloned, and a neutralizing monoclonal antibody, raised against a recombinant chCD132 protein, was identified by inhibition of IL-2-dependent proliferation of T cells. Flow cytometry analysis revealed that chCD132 molecules are expressed on the surface of splenic mononuclear cells. The functional domain of chCD132 that binds to chicken interleukin 2, Q(84)E(94)L(95)Q(96)N(97)L(98), was found through phage display and peptide-competitive ELISA, and its critical residue Q(96) was further identified. A tertiary structure model shows that the functional domain i...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2891083</comments>
            <pubDate>Thu, 08 Oct 2009 23:00:00 +0100</pubDate>
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        <item>
            <title>Caenopores are antimicrobial peptides in the nematode caenorhabditis elegans instrumental in nutrition and immunity.</title>
            <link>http://www.medworm.com/index.php?rid=2891084&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19818806%26dopt%3DAbstract</link>
            <description>Authors: Roeder T, Stanisak M, Gelhaus C, Bruchhaus I, Gr&amp;#xF6;tzinger J, Leippe M
    For the soil nematode Caenorhabditis elegans, microbes are both food source and potential pathogens. Intrinsic antibiotic agents such as antimicrobial peptides (AMP) are important to protect the worm against infection. Here, we show that among potential antimicrobial peptides of C. elegans, with respect to gene number, the majority belongs to the SPP-protein family which we named caenopores as they resemble structurally and functionally amoebapores. SPP-5 kills bacteria by permeabilizing their cytoplasmic membrane and displays pore-forming activity as judged by liposome depolarization. The antimicrobial polypeptide is required to cope with Escherichia coli, the regular food source of C. elegans in the la...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2891084</comments>
            <pubDate>Tue, 06 Oct 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2891084</guid>        </item>
        <item>
            <title>Role of CRTAM during mouse early T lymphocytes development.</title>
            <link>http://www.medworm.com/index.php?rid=2866221&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19799932%26dopt%3DAbstract</link>
            <description>Authors: Medina-Contreras O, Soldevila G, Pati&amp;#xF1;o-Lopez G, Canche-Pool E, Valle-Rios R, Ortiz-Navarrete V
    CRTAM was reported as a novel receptor expressed in activated NKT and CD8 T lymphocytes. However, we have recently shown that is also expressed in several non-immune tissues. In opposition to what has been stated for lymphoid cells, CRTAM expression is constitutive in epithelia, suggesting a role in cell-cell interactions. Given the importance of cell interactions during T lymphocyte development, we evaluated CRTAM during T lymphocyte ontogeny. Here we show that CRTAM has an unexpected constitutive expression in adult thymocytes and, remarkably, it is sustained during all stages of thymocyte development. CRTAM expression is restricted to CD8 and all DN subpopulations, with a co...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2866221</comments>
            <pubDate>Mon, 28 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2866221</guid>        </item>
        <item>
            <title>Swine leukocyte antigen (SLA) diversity in Sinclair and Hanford swine.</title>
            <link>http://www.medworm.com/index.php?rid=2842246&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19782700%26dopt%3DAbstract</link>
            <description>This study furthers our understanding of the allelic architecture and polymorphism of the SLA system and will facilitate the mapping of loci associated with the expression of SSCM.
    PMID: 19782700 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2842246</comments>
            <pubDate>Wed, 23 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2842246</guid>        </item>
        <item>
            <title>Cloning and characterisation of the chicken orthologue of dendritic cell-lysosomal associated membrane protein (DC-LAMP).</title>
            <link>http://www.medworm.com/index.php?rid=2842245&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19782701%26dopt%3DAbstract</link>
            <description>Authors: Wu Z, Hu T, Butter C, Kaiser P
    A cDNA encoding the chicken orthologue of dendritic cell-lysosomal associated membrane protein (DC-LAMP)/CD208 was cloned by RT-PCR from RNA isolated from mature chicken bone marrow-derived dendritic cells (chBM-DC). The cloned chicken DC-LAMP (chDC-LAMP) cDNA consists of 1281 nucleotides encoding an open reading frame of 426 amino acids (aa). Comparison of the deduced aa sequence of DC-LAMP with orthologous proteins from human and mouse revealed 27% and 24% identity, respectively. The predicted chDC-LAMP protein shares the characteristic features of LAMP family members. ChDC-LAMP mRNA, unlike its mammalian orthologues, was expressed in a wide range of tissues, at highest levels in the lung. Lymphoid tissues including thymus, spleen, bursa, ceaca...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2842245</comments>
            <pubDate>Wed, 23 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2842245</guid>        </item>
        <item>
            <title>Characterization of arrangement and expression of the beta-2 microglobulin locus in the sandbar and nurse shark.</title>
            <link>http://www.medworm.com/index.php?rid=2842248&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19782101%26dopt%3DAbstract</link>
            <description>In this report, beta2m cDNAs were identified and sequenced from sandbar shark spleen cDNA library. Sandbar shark beta2m gene encodes one amino acid less than most teleost beta2m genes, and 3 amino acids less than mammal beta2m genes. Although sandbar shark beta2m protein contains one beta sheet less than that of human in the predicted protein structure, the overall structure of beta2m proteins is conserved during evolution. Germline gene for the beta2m in sandbar and nurse shark is present as a single locus. It contains 3 three exons and two introns. CpG sites are evenly distributed in the shark beta2m loci. Several DNA repeat elements were also identified in the shark beta2m loci. Sequence analysis suggests that the beta2m locus is not linked to the MHC I loci in the shark genome.
    PMI...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2842248</comments>
            <pubDate>Tue, 22 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2842248</guid>        </item>
        <item>
            <title>CD62L defines a subset of pathogen-specific bovine CD4 with central memory cell characteristics.</title>
            <link>http://www.medworm.com/index.php?rid=2825047&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19766669%26dopt%3DAbstract</link>
            <description>Authors: Tott&amp;#xE9; P, Duperray C, Dedieu L
    Central memory T cells (Tcm) have not previously been characterized in cattle and any other ruminant species. Here we described two phenotypically and functionally different subsets of pathogen-specific memory CD4(+) T cells in cattle that survived infection with Mycoplasma mycoides subsp. mycoides small colony (MmmSC). The first subset is CD45RO(+)CD45R(-)CD62L(-) and comprises two thirds of IFN-gamma producing CD4(+) T cells after MmmSC recall stimulation. The second is CD45RO(+)CD45R(-)CD62L(+) and represents the majority of proliferating CD4(+) T cells after 7 days of stimulation. Cell sorting experiments confirmed that both CD4(+)CD62L(+) and CD4(+)CD62L(-) subsets are present in vivo and proliferate independently in recall responses to ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2825047</comments>
            <pubDate>Wed, 16 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2825047</guid>        </item>
        <item>
            <title>Cloning of a novel interleukin (IL)-20 like gene in rainbow trout Oncorhynchus mykiss gives an insight into the evolution of the IL-10 family.</title>
            <link>http://www.medworm.com/index.php?rid=2807147&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19755128%26dopt%3DAbstract</link>
            <description>Authors: Wang T, D&amp;#xED;az-Rosales P, Martin SA, Secombes CJ
    A novel IL-20-like (IL-20L) gene has been analyzed in rainbow trout. It has a six exon/five intron gene organisation and is translated into 181 amino acids (aa) with a signal peptide of 25 aa and a mature peptide of 156 aa. The trout IL-20L translation shares highest identities to other IL-20L molecules from fish and to IL-20 in mammals. Phylogenetic analysis showed that the fish IL-20L molecules form an independent clade but cluster with the group containing the IL-19, IL-20 and IL-24 molecules from higher vertebrates with a high bootstrap value (89%). The fish IL-20L genes are syntenically in the same location as mammalian IL-19/IL-20/IL-24. Gene organisation and multiple alignment also showed a close relationship of fish I...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2807147</comments>
            <pubDate>Fri, 11 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2807147</guid>        </item>
        <item>
            <title>A clip domain serine proteinase plays a role in antibacterial defense but is not required for prophenoloxidase activation in shrimp.</title>
            <link>http://www.medworm.com/index.php?rid=2800842&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19751760%26dopt%3DAbstract</link>
            <description>Authors: Amparyup P, Wiriyaukaradecha K, Charoensapsri W, Tassanakajon A
    The clip domain serine proteinases (clip-SPs) play critical roles in the signaling processes during embryonic development and in the innate immunity of invertebrates. In the present study, we identified a homolog of the clip-SP, designated as PmClipSP1, by searching the Penaeus monodon EST database (http://pmonodon.biotec.or.th), and using RACE-PCR to obtain the complete gene which contained a 1095bp open reading frame encoding 364 amino acids with a 25 amino acid signal peptide. The deduced PmClipSP1 protein sequence, which shares a predicted structural similarity to the clip-SPs of other arthropod species, appears to possess a clip domain at the N-terminus and an enzymatically active serine proteinase domain at ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2800842</comments>
            <pubDate>Thu, 10 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2800842</guid>        </item>
        <item>
            <title>Differences in transcriptomic profile and IgA repertoire between jejunal and ileal Peyer's patches.</title>
            <link>http://www.medworm.com/index.php?rid=2800844&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19747939%26dopt%3DAbstract</link>
            <description>We examined, by quantitative real-time PCR, the expression of 36 transcripts of antimicrobial peptides, chemokines, cytokines, toll-like receptors and transcription factors from both PP and we highlighted the differences by a principal component analysis. Ileal PP was characterized by a higher mRNA expression of CCL28, IL5, IL10, TLR2 and TLR4 while jejunal PP showed higher mRNA expression of antimicrobial peptides, CCL25, FOXP3, IL4, T-Bet, TSLP and SOCS2. Then, we analyzed some VDJ rearrangements to assess immunoglobulin repertoire diversity in jejunal and ileal PP from weaned piglets. The IgA and IgM repertoires were more diverse in ileal than in jejunal piglet PP. All these results could be related to the rarefaction of interfolicullar T-cell zone and the presence in ileal versus jejun...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2800844</comments>
            <pubDate>Tue, 08 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2800844</guid>        </item>
        <item>
            <title>Identification and characterization of the first reptilian CD9, and its expression analysis in response to bacterial infection.</title>
            <link>http://www.medworm.com/index.php?rid=2800843&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19747940%26dopt%3DAbstract</link>
            <description>In this study, a CD9 homologue in a reptile, Chinese soft-shelled turtle, has been cloned and identified for the first time. The full-length cDNA of turtle CD9 was 1146bp and contained a 672bp open reading frame (ORF) coding for a protein of 224 amino acids. Four transmembrane domains (TMs) divided the turtle CD9 into several parts: short N, C-termini, an intracellular loop and two (small and large) extracellular loops (SEL and LEL). A CCG motif, a potential N-linked glycosylation site and ten cysteine residues were well conserved. The deduced amino acid sequence analysis showed that the turtle CD9 shared 82% identity to duck CD9. Most of the differences were found in the LEL. Phylogenetic analysis showed that the turtle CD9 sequence clustered together with bird CD9 sequence. RT-PCR analys...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2800843</comments>
            <pubDate>Tue, 08 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2800843</guid>        </item>
        <item>
            <title>Conservation of CD1 protein expression patterns in the chicken.</title>
            <link>http://www.medworm.com/index.php?rid=2775608&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19735672%26dopt%3DAbstract</link>
            <description>Authors: Ly N, Danzl NM, Wang J, Zajonc DM, Dascher CC
    The CD1 molecules are cell surface proteins that bind and present foreign lipids and glycolipids to T cells in a manner similar to the MHC system. While the mammalian CD1 antigen presentation pathway is well characterized, little is known about CD1 in non-mammalian vertebrates. Previous studies have identified two CD1 homologues in the chicken. We developed a monoclonal antibody designated NL1-1.A1 specific for the chCD1-1 isoform and have used this to characterize CD1 expression in tissues and cells of normal adult and embryonic chickens. The chCD1-1 isoform is expressed on a high proportion of cells in the spleen and bursa. Cells in the spleen that stain for CD1 are also positive for IgM and consistent with identification of thes...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2775608</comments>
            <pubDate>Thu, 03 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2775608</guid>        </item>
        <item>
            <title>Mutations in an Avian IgY-Fc Fragment Reveal the Locations of Monocyte Fc Receptor Binding Sites.</title>
            <link>http://www.medworm.com/index.php?rid=2775612&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19733585%26dopt%3DAbstract</link>
            <description>Authors: Taylor AI, Sutton BJ, Calvert RA
    The avian IgY antibody isotype shares a common ancestor with both mammalian IgG and IgE and so provides a means to study the evolution of their structural and functional specialisations. Although both IgG and IgE bind to their leukocyte Fc receptors with 1:1 stoichiometry, IgY binds to CHIR-AB1, a receptor expressed in avian monocytes, with 2:1 stoichiometry. The mutagenesis data reported here explain the structural basis for this difference, mapping the CHIR-AB1 binding site to the Cupsilon3/Cupsilon4 interface and not the N-terminal region of Cupsilon3 where, at equivalent locations, the IgG and IgE leukocyte Fc receptor binding sites lie. This finding, together with the phylogenetic relationship of the antibodies and their receptors, indicat...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2775612</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2775612</guid>        </item>
        <item>
            <title>BCG vaccine confers adaptive immunity against Mycobacterium sp. infection in fish.</title>
            <link>http://www.medworm.com/index.php?rid=2775611&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19733586%26dopt%3DAbstract</link>
            <description>In this study, the effects of two vaccine candidates, Bacillus Calmette and Gu&amp;#xE8;rin (BCG, an attenuated strain of Mycobacterium bovis) and formalin-killed cells of Mycobacterium sp. were evaluated in Japanese flounder, Paralichthys olivaceus. In the immediate response and tuberculin response, BCG vaccinated fish showed higher gene expression levels of inflammatory cytokines such as IL-1beta, IL-6, IFN-gamma and TNFalpha. Furthermore, BCG vaccination conferred protective efficacy against Mycobacterium sp. infection in Japanese flounder. Transcriptome analysis using a Japanese flounder cDNA microarray revealed that BCG vaccination induced not only adaptive immunity against Mycobacterium sp. antigen but also the expression of non-specific bactericidal proteins such as lysozyme. These data...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2775611</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2775611</guid>        </item>
        <item>
            <title>Presence of an unique IgT on the IGH locus in G. aculeatus and the very recent generation of a repertoire of VH genes.</title>
            <link>http://www.medworm.com/index.php?rid=2775610&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19733587%26dopt%3DAbstract</link>
            <description>This study describes the IGH locus in Gasterosteus aculeatus, with 10 genes encoding three immunoglobulin classes: IgT, IgM and IgD. These genes are organized into a structure with three repeats of IGHT-IGHM-IGHD separated by segments including the VH segments. There was also a fourth IGHT gene. IGHT encodes an antibody with three immunoglobulin domains. Comparative studies indicate it is related to IgT and IgZ and other antibodies located upstream of the IGHM in teleost fish. The IGHM and IGHD are similar to the ones described in teleost. The IGHM has four immunoglobulin domains while the IGHD seven and none is duplicated. The IGH locus of G. aculeatus has 49 VH segments located in four regions. They belonged to four families, whose members show a greater than 92% amino acid identity, ind...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2775610</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2775610</guid>        </item>
        <item>
            <title>Nitric oxide is an essential component of the hemocyte-mediated mosquito immune response against bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=2775609&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19733588%26dopt%3DAbstract</link>
            <description>Authors: Hillyer JF, Est&amp;#xE9;vez-Lao TY
    Nitric oxide is a signaling and immune effector molecule synthesized by the enzyme nitric oxide synthase. In mosquitoes, nitric oxide functions as a parasite antagonist in the midgut but little is known about its function in the hemocoel. Here, we characterized the temporal and spatial expression of the Anopheles gambiae nitric oxide synthase gene and explored the role nitric oxide plays in the antibacterial response in the mosquito hemocoel. Quantitative PCR and Western blot analyses showed that nitric oxide synthase is expressed in hemocytes and fat body, and is upregulated in response to systemic infection with Escherichia coli and Micrococcus luteus. Diaphorase staining and immunofluorescence showed that nitric oxide synthase is abundant in ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2775609</comments>
            <pubDate>Wed, 02 Sep 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2775609</guid>        </item>
        <item>
            <title>Influence of temperature, salinity and E. coli tissue content on immune gene expression in mussel: results from a 2005-2008 survey.</title>
            <link>http://www.medworm.com/index.php?rid=2529023&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19409926%26dopt%3DAbstract</link>
            <description>Authors: Li H, Toubiana M, Monfort P, Roch P
    Several bivalves, including mussels, suffered from mortalities particularly in summer. To look for the possible effect of environmental parameters on immune capacities, Mytilus galloprovincialis were collected monthly from August 2005 to July 2008 from the Palavas Laguna, French Mediterranean coast. Q-PCR was used to quantify the expression of three antimicrobial peptide genes (defensin, mytilin B and myticin B), in addition to lysozyme and HSP70. House keeping gene was 28S rRNA. Defensin, myticin B and lysozyme appeared more expressed in spring-summer than in winter. In contrast, HSP70 expression was higher in winter. Statistical studies using principal component analysis (PCA) and multiple regression models revealed positive influence of t...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529023</comments>
            <pubDate>Sat, 27 Jun 2009 13:04:08 +0100</pubDate>
            <guid isPermaLink="false">2529023</guid>        </item>
        <item>
            <title>Gene cloning of a sigma class glutathione S-transferase from abalone (Haliotis diversicolor) and expression analysis upon bacterial challenge.</title>
            <link>http://www.medworm.com/index.php?rid=2529022&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19414031%26dopt%3DAbstract</link>
            <description>In this study, a full-length cDNA of a sigma class GST (abGSTsigma) (GenBank accession number EF546619) from variously colored abalone (Haliotis diversicolor) was identified. It was 1328bp containing an open reading frame of 624bp, encoding 208 amino acid residues with a predicted protein molecular weight of 23.67kDa and an estimated pI of 5.67. Sequence analysis showed that the predicted protein sequence of abGSTsigma cDNA contained the conserved domain of the GST_N_Sigma_like (PSSM: cd03039) and GST_C_Sigma_like (PSSM: cd03192). Alignment analysis demonstrated that the abGSTsigma of H. diversicolor was in a branch position with other known class sigma GSTs from different organisms. The abGSTsigma mRNA was distributed in multiple tissues tested and was highly demonstrated in the gill and ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529022</comments>
            <pubDate>Sat, 27 Jun 2009 13:04:04 +0100</pubDate>
            <guid isPermaLink="false">2529022</guid>        </item>
        <item>
            <title>NOD-like subfamily of the nucleotide-binding domain and leucine-rich repeat containing family receptors and their expression in channel catfish.</title>
            <link>http://www.medworm.com/index.php?rid=2529021&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19414032%26dopt%3DAbstract</link>
            <description>Authors: Sha Z, Abernathy JW, Wang S, Li P, Kucuktas H, Liu H, Peatman E, Liu Z
    The NLRs (nucleotide-binding domain and leucine-rich repeat containing family receptors) are a recently identified family of pattern recognition receptors in vertebrates. Several subfamilies of NLRs have been characterized in human, mouse, and zebrafish, but studies of NLRs in other species, especially teleost species, have been lacking. Here we report characterization of five NLRs from channel catfish: NOD1, NOD2, NLRC3, NLRC5, and NLRX1. Structural analysis indicated that the genes were organized in a similar fashion as in the mammals and in zebrafish. Phylogenetic analysis suggested that they were orthologous to the NOD-like subfamily of NLRs. All five NOD-like genes exist as a single copy gene in the ca...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529021</comments>
            <pubDate>Sat, 27 Jun 2009 13:04:01 +0100</pubDate>
            <guid isPermaLink="false">2529021</guid>        </item>
        <item>
            <title>An ancient immunity gene duplication in Daphnia magna: RNA expression and sequence analysis of two nitric oxide synthase genes.</title>
            <link>http://www.medworm.com/index.php?rid=2529019&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19416737%26dopt%3DAbstract</link>
            <description>Authors: Labb&amp;#xE9; P, McTaggart SJ, Little TJ
    NO (nitric oxide) is a highly reactive free radical gas thought to play a major role in the invertebrate immune response by harming pathogens and limiting their growth. Here we report on studies of nitric oxide synthase (NOS) genes in the crustacean Daphnia, one of the few non-insect arthropod models used to study host-pathogen interactions. While the NOS gene is found as a single copy in other invertebrates, we found two copies (NOS1 and NOS2), which a phylogenetic reconstruction showed to be the result of an ancient duplication event. Both genes bear features commonly found in invertebrate NOS, however, the two genes differ in their rate of evolution, intraspecific polymorphism and expression level. We tested whether the more rapid evolu...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529019</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:55 +0100</pubDate>
            <guid isPermaLink="false">2529019</guid>        </item>
        <item>
            <title>Identification and characterization of TLR8 and MyD88 homologs in Atlantic salmon (Salmo salar).</title>
            <link>http://www.medworm.com/index.php?rid=2529018&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19422846%26dopt%3DAbstract</link>
            <description>Authors: Skjaeveland I, Iliev DB, Strandskog G, J&amp;#xF8;rgensen JB
    Toll-like receptor 8 (TLR 8) belongs to a subgroup of the TLR family that recognizes nucleic acids and that is involved in the protection against viruses. In mammals, TLR7 and 8 have been characterized as receptors for viral and synthetic single-stranded RNA. Here we describe the cloning of a TLR8 homolog in Atlantic salmon (Salmo salar) and its proximal adaptor protein MyD88. The mRNA expression of SsTLR8 was tissue-restricted and its highest level was detected in the spleen while SsMyD88 was expressed in all of the tested organs. SsTLR8 and SsMyD88 mRNAs were up-regulated in TO cells treated with recombinant IFN alpha1 and IFN gamma. In vivo, the expression of SsTLR8 was not significantly affected following challenge w...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529018</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:52 +0100</pubDate>
            <guid isPermaLink="false">2529018</guid>        </item>
        <item>
            <title>Characterisation of a carp cell line for analysis of apoptosis.</title>
            <link>http://www.medworm.com/index.php?rid=2529017&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428480%26dopt%3DAbstract</link>
            <description>This study was designed as a first step towards a better knowledge of fish macrophages and their fate after different types of apoptotic insults.
    PMID: 19428480 [PubMed - in process] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529017</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:49 +0100</pubDate>
            <guid isPermaLink="false">2529017</guid>        </item>
        <item>
            <title>Lack of evidence for Litopenaeus vannamei Toll receptor (lToll) involvement in activation of sequence-independent antiviral immunity in shrimp.</title>
            <link>http://www.medworm.com/index.php?rid=2529016&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428481%26dopt%3DAbstract</link>
            <description>Authors: Labreuche Y, O'Leary NA, de la Vega E, Veloso A, Gross PS, Chapman RW, Browdy CL, Warr GW
    Injection of non-specific dsRNA initiates a broad-spectrum innate antiviral immune response in the Pacific white shrimp, Litopenaeus vannamei, however, the receptor involved in recognition of this by-product of viral infections remains unknown. In vertebrates, dsRNA sensing is mediated by a class of Toll-like receptors (TLRs) and results in activation of the interferon system. Because a TLR (lToll) was recently characterized in L. vannamei, we investigated its potential role in dsRNA recognition. We showed that injection of non-specific RNA duplexes did not modify lToll gene expression. A reverse genetic approach was therefore implemented to study its role in vivo. Silencing of lToll did ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529016</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:46 +0100</pubDate>
            <guid isPermaLink="false">2529016</guid>        </item>
        <item>
            <title>Gene silencing of a prophenoloxidase activating enzyme in the shrimp, Penaeus monodon, increases susceptibility to Vibrio harveyi infection.</title>
            <link>http://www.medworm.com/index.php?rid=2529015&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428482%26dopt%3DAbstract</link>
            <description>In this study, a cDNA encoding a proPO activating enzyme (PPAE) from the black tiger shrimp, Penaeus monodon, designated as PmPPAE1, was cloned and characterized. The full-length cDNA contains an open reading frame (ORF) of 1392bp encoding a predicted protein of 463 amino acids including an 18 amino acid signal peptide. The PmPPAE1 protein exhibits a characteristic sequence structure of clip-SPs consisting of the clip domain at the N-terminus and a SP domain at the C-terminus. Sequence analysis showed that PmPPAE1 exhibited the highest amino acid sequence similarity (70%) to a PPAE of the crayfish, Pacifastacus leniusculus. PmPPAE1 mRNA is abundantly expressed in hemocytes, and this is regulated after systemic Vibrio harveyi infection supporting that it is an immune-responsive gene. RNA in...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529015</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:44 +0100</pubDate>
            <guid isPermaLink="false">2529015</guid>        </item>
        <item>
            <title>Isolation and expression profile of a gene encoding for the Signal Transducer and Activator of Transcription STAT2 in Atlantic salmon (Salmo salar).</title>
            <link>http://www.medworm.com/index.php?rid=2529014&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428483%26dopt%3DAbstract</link>
            <description>Authors: Collet B, Ganne G, Bird S, Collins CM
    Signal Transducer and Activator of Transcription (STAT)-2 is a molecule involved in the type I interferon (IFN) signalling pathway. The full length cDNA sequence of Atlantic salmon (Salmo salar) ssSTAT2 was determined and phylogenetic analysis of the amino acid sequence grouped this novel salmon gene to the STAT2 clade. This represents the first fish STAT2 report. The gene encodes for a 802 aa polypeptide that has 38% identity to the human or murine STAT2. The expression was monitored by qPCR in the kidney of animals over the time of infection with the Infectious Salmon Anaemia Virus (ISAV) and in TO cells infected with Infectious Pancreatic Necrosis Virus (IPNV) or with the Salmon Alphavirus (SAV). SAV and ISAV induced an approximate 10-f...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529014</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:41 +0100</pubDate>
            <guid isPermaLink="false">2529014</guid>        </item>
        <item>
            <title>Identification of a kazal-type serine protease inhibitor with potent anti-staphylococcal activity as part of Hydra's innate immune system.</title>
            <link>http://www.medworm.com/index.php?rid=2529013&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428484%26dopt%3DAbstract</link>
            <description>In this study we demonstrate that not only epithelial cells but also gland cells are critically involved in Hydra's innate host defense by producing a kazal-type serine protease inhibitor, kazal2, that has potent in vitro bactericidal activity against Staphylococcus aureus. The discovery of an antimicrobial serine protease inhibitor in Hydra may shed new light on the mechanisms of host defense early in metazoan evolution, and promises to open new avenues for the development of potent anti-staphylococcal compounds.
    PMID: 19428484 [PubMed - in process] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529013</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:39 +0100</pubDate>
            <guid isPermaLink="false">2529013</guid>        </item>
        <item>
            <title>Molecular characterization and expression profiles in response to bacterial infection of Chinese soft-shelled turtle interleukin-8 (IL-8), the first reptilian chemokine gene.</title>
            <link>http://www.medworm.com/index.php?rid=2529012&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428485%26dopt%3DAbstract</link>
            <description>In this study, an IL-8 homologue has been cloned and identified from a reptile, Chinese soft-shelled turtle for the first time. The full-length cDNA of turtle IL-8 was 1188bp and contained a 312bp open reading frame (ORF) coding for a protein of 104 amino acids. The chemokine CXC domain, which contained Glu-Leu-Arg (ELR) motif and four cysteine residues, was well conserved in turtle IL-8. The 4924bp genomic DNA of turtle IL-8 contained four exons and three introns. Phylogenetic analysis showed that the amino acid sequence of turtle IL-8 clustered together with birds. RT-PCR analysis showed that turtle IL-8 mRNA was constitutively expressed liver, spleen, kidney, heart, blood and intestine tissues of control turtles. Real-time quantitative PCR analysis further indicated that the turtle IL-8...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529012</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:36 +0100</pubDate>
            <guid isPermaLink="false">2529012</guid>        </item>
        <item>
            <title>Transferrin and ferritin response to bacterial infection: the role of the liver and brain in fish.</title>
            <link>http://www.medworm.com/index.php?rid=2529011&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428486%26dopt%3DAbstract</link>
            <description>Authors: Neves JV, Wilson JM, Rodrigues PN
    Iron is essential for growth and survival, but it is also toxic when in excess. Thus, there is a tight regulation of iron that is accomplished by the interaction of several genes including the iron transporter transferrin and iron storage protein ferritin. These genes are also known to be involved in response to infection. The aim of this study was to understand the role of transferrin and ferritin in infection and iron metabolism in fish. Thus, sea bass transferrin and ferritin H cDNAs were isolated from liver, cloned and characterized. Transferrin constitutive expression was found to be highest in the liver, but also with significant expression in the brain, particularly in the highly vascularized region connecting the inferior lobe of the h...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529011</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:34 +0100</pubDate>
            <guid isPermaLink="false">2529011</guid>        </item>
        <item>
            <title>A beta integrin subunit regulates bacterial phagocytosis in medfly haemocytes.</title>
            <link>http://www.medworm.com/index.php?rid=2529010&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428487%26dopt%3DAbstract</link>
            <description>Authors: Mamali I, Lamprou I, Karagiannis F, Karakantza M, Lampropoulou M, Marmaras VJ
    We have recently reported that the activation of focal adhesion kinase (FAK) and its downstream targets upon pathogen challenge regulate phagocytosis in medfly haemocytes. The goal of this study was to further explore the signalling pathway underlying the process of phagocytosis. In particular, in this report, we used flow cytometry, RNA interference, enzyme-linked immunosorbent assay, Western blot and immunoprecipitation analysis to demonstrate the haemocyte surface receptor, through which the extracellular signals in response to bacteria are transmitted intracellularly. The presented data demonstrate the expression of a beta integrin subunit in the surface of medfly haemocytes that transmits signal...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529010</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:31 +0100</pubDate>
            <guid isPermaLink="false">2529010</guid>        </item>
        <item>
            <title>Two thymosin-repeated molecules with structural and functional diversity coexist in Chinese mitten crab Eriocheir sinensis.</title>
            <link>http://www.medworm.com/index.php?rid=2529009&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428488%26dopt%3DAbstract</link>
            <description>Authors: Gai Y, Zhao J, Song L, Wang L, Qiu L, Ning X, Zheng X, Zhang Y, Mu C, Zhang Y, Li L
    Recently, beta-thymosin-like proteins with multiple thymosin domains (defined as thymosin-repeated proteins) have been identified from invertebrate. In the present study, the cDNAs of two thymosin-repeated proteins (designated EsTRP1 and EsTRP2) were cloned from Chinese mitten crab by expressed sequence tags (EST) techniques. BLAST analysis presented three and two thymosin domains in EsTRP1 and EsTRP2, respectively, with the identities amongst the five domains varying from 47% to 100%. Both EsTRP1 and EsTRP2 shared high similarities with previously identified vertebrate beta-thymosins and invertebrate thymosin-repeated proteins (TRPs) with the identities ranging from 43% to 78%, indicating that...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529009</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:29 +0100</pubDate>
            <guid isPermaLink="false">2529009</guid>        </item>
        <item>
            <title>Commentary on Galindo et Al. [Dev. Comp. Immunol. 33(4) (2009) 612-617].</title>
            <link>http://www.medworm.com/index.php?rid=2529008&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19428489%26dopt%3DAbstract</link>
            <description>Authors: Macqueen D
    
    PMID: 19428489 [PubMed - in process] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529008</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:27 +0100</pubDate>
            <guid isPermaLink="false">2529008</guid>        </item>
        <item>
            <title>Characterisation and expression analysis of the chicken interleukin-7 receptor alpha chain.</title>
            <link>http://www.medworm.com/index.php?rid=2529007&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19442686%26dopt%3DAbstract</link>
            <description>Authors: van Haarlem DA, van Kooten PJ, Rothwell L, Kaiser P, Vervelde L
    Interleukin-7 (IL-7) is a central regulator of T cell survival and homeostasis and its expression is indicative for na&amp;#xEF;ve and memory T cells. We cloned chicken IL-7Ralpha (CHIL-7Ralpha) and determined its expression profile in chicken lymphocyte subpopulations. The predicted protein sequence contained 460 amino acids. The extracellular domain exhibited features typical of a type I cytokine receptor; a fibronectin type III domain and the GXWSXWS motif were conserved. ChIL-7Ralpha mRNA is highly expressed in lymphoid organs and in CD4+, CD8alpha+ and CD8beta+ cells. A monoclonal antibody was generated and expression of the protein investigated. ChIL-7Ralpha was expressed on CD4+ and CD8alpha+, but not CD8beta+,...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529007</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:24 +0100</pubDate>
            <guid isPermaLink="false">2529007</guid>        </item>
        <item>
            <title>Expression of essential B cell genes and immunoglobulin isotypes suggests active development and gene recombination during equine gestation.</title>
            <link>http://www.medworm.com/index.php?rid=2529006&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19442687%26dopt%3DAbstract</link>
            <description>Authors: Tallmadge RL, McLaughlin K, Secor E, Ruano D, Matychak MB, Flaminio MJ
    Many features of the equine immune system develop during fetal life, yet the na&amp;#xEF;ve or immature immune state of the neonate renders the foal uniquely susceptible to particular pathogens. RT-PCR and immunohistochemical experiments investigated the progressive expression of developmental B cell markers and immunoglobulins in lymphoid tissues from equine fetus, pre-suckle neonate, foal, and adult horses. Serum IgM, IgG isotype, and IgA concentrations were also quantified in pre-suckle foals and adult horses. The expression of essential B cell genes suggests active development and gene recombination during equine gestation, including immunoglobulin isotype switching. The corresponding production of IgM and ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529006</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:22 +0100</pubDate>
            <guid isPermaLink="false">2529006</guid>        </item>
        <item>
            <title>Characterization of an ETS transcription factor in the sea scallop Chlamys farreri.</title>
            <link>http://www.medworm.com/index.php?rid=2529005&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19446578%26dopt%3DAbstract</link>
            <description>Authors: Ma H, Wang J, Wang B, Zhao Y, Yang C
    We have cloned and characterized a cDNA encoding a putative ETS transcription factor, designated Cf-ets. The Cf-ets encodes a 406 amino acid protein containing a conserved ETS domain and a Pointed domain. Phylogenetic analysis revealed that Cf-ets belongs to the ESE group of ETS transcription factor family. Real-time PCR analysis of Cf-ets expression in adult sea scallop tissues revealed that Cf-ets was expressed mainly in gill and hemocytes, in a constitutive manner. Cf-ets mRNA level in hemocytes increased drastically after microbial challenge indicated its indispensable role in the anti-infection process. Simultaneously, the circulating hemocyte number decreased. In mammals, most ETS transcription factors play indispensable roles in bloo...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529005</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:20 +0100</pubDate>
            <guid isPermaLink="false">2529005</guid>        </item>
        <item>
            <title>A novel C-type lectin (FcLec4) facilitates the clearance of Vibrio anguillarum in vivo in Chinese white shrimp.</title>
            <link>http://www.medworm.com/index.php?rid=2529004&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19447130%26dopt%3DAbstract</link>
            <description>Authors: Wang XW, Zhang XW, Xu WT, Zhao XF, Wang JX
    C-type lectins play important roles in innate immunity of invertebrates. In the present study, we report a novel C-type lectin, named FcLec4, from the Chinese white shrimp Fenneropenaeus chinensis. FcLec4 contains a single carbohydrate recognition domain (CRD) with a putative signal peptide. Phylogenetic analysis indicated that FcLec4 was distant from most reported C-type lectins from shrimps. The expression of FcLec4 increased at both mRNA and protein level after stimulation of Vibrio anguillarum. Recombinant FcLec4 could agglutinate both Gram-positive and -negative bacteria in the presence of calcium. The recombinant protein could bind to peptidoglycan and selectively bind to microorganisms. Interestingly, the tight binding of recom...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529004</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:18 +0100</pubDate>
            <guid isPermaLink="false">2529004</guid>        </item>
        <item>
            <title>The diversity of C-type lectins in the genome of a basal metazoan, Nematostella vectensis.</title>
            <link>http://www.medworm.com/index.php?rid=2529002&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454330%26dopt%3DAbstract</link>
            <description>This study provides a N. vectensis CTL database that can be used for further research on the evolution of cnidarian CTLs and the role of CTLs in cnidarian innate immunity.
    PMID: 19454330 [PubMed - in process] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529002</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:13 +0100</pubDate>
            <guid isPermaLink="false">2529002</guid>        </item>
        <item>
            <title>Innate hemocyte responses of Malacosoma disstria larvae (C. Insecta) to antigens are modulated by intracellular cyclic AMP.</title>
            <link>http://www.medworm.com/index.php?rid=2529000&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454331%26dopt%3DAbstract</link>
            <description>Authors: Gulii V, Dunphy GB, Mandato CA
    Invertebrate intracellular hemocyte signaling pathways affecting cellular-antigen responses, although defined for molluscs and some arthropods including dipteran insects, is less known for lepidopterans. Hemocytic-antigen responses of the arboreal pest lepidopteran Malacosoma disstria are linked to cAMP-dependent protein kinase A implicating cAMP in cellular hemocyte immune responses. The purpose in the present study was to determine intracellular cAMP effects on larval M. disstria hemocytes adhering to slides and bacteria. Altering adenylate cyclase and phosphodiesterase activities as well as cAMP levels in vitro and in vivo changed hemocyte responses to antigens. Quiescent hemocytes had high cAMP levels due to adenylate cyclase activity and pos...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529000</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:11 +0100</pubDate>
            <guid isPermaLink="false">2529000</guid>        </item>
        <item>
            <title>The vitamin D3 transcriptomic response in skin cells derived from the Atlantic bottlenose dolphin.</title>
            <link>http://www.medworm.com/index.php?rid=2528997&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454332%26dopt%3DAbstract</link>
            <description>Authors: Ellis BC, Gattoni-Celli S, Mancia A, Kindy MS
    The Atlantic bottlenose dolphin has attracted attention due to the evident impact that environmental stressors have taken on its health. In order to better understand the mechanisms linking environmental health with dolphin health, we have established cell cultures from dolphin skin as in vitro tools for molecular evaluations. The vitamin D3 pathway is one mechanism of interest because of its well established chemopreventative and immunomodulatory properties in terrestrial mammals. On the other hand, little is known of the physiological role of this molecule in aquatic animals. 1,25-dihydroxyvitamin D3 (1,25D3), the bioactive and hormonal form of vitamin D3, exerts its biological function by binding to the vitamin D receptor (VDR),...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528997</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:05 +0100</pubDate>
            <guid isPermaLink="false">2528997</guid>        </item>
        <item>
            <title>Antimicrobial activity in the tick Rhipicephalus (Boophilus) microplus eggs: Cellular localization and temporal expression of microplusin during oogenesis and embryogenesis.</title>
            <link>http://www.medworm.com/index.php?rid=2528995&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454333%26dopt%3DAbstract</link>
            <description>Authors: Esteves E, Foga&amp;#xE7;a AC, Maldonado R, Silva FD, Manso PP, Pelajo-Machado M, Valle D, Daffre S
    Arthropods display different mechanisms to protect themselves against infections, among which antimicrobial peptides (AMPs) play an important role, acting directly against invader pathogens. We have detected several factors with inhibitory activity against Candida albicans and Micrococcus luteus on the surface and in homogenate of eggs of the tick Rhipicephalus (Boophilus) microplus. One of the anti-M. luteus factors of the egg homogenate was isolated to homogeneity. Analysis by electrospray mass spectrometry (ESI-MS) revealed that it corresponds to microplusin, an AMP previously isolated from the cell-free hemolymph of R. (B.) microplus. Reverse transcription (RT) quantitative poly...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528995</comments>
            <pubDate>Sat, 27 Jun 2009 13:03:01 +0100</pubDate>
            <guid isPermaLink="false">2528995</guid>        </item>
        <item>
            <title>The search for the IFN-gamma receptor in fish: Functional and expression analysis of putative binding and signalling chains in rainbow trout Oncorhynchus mykiss.</title>
            <link>http://www.medworm.com/index.php?rid=2528992&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454334%26dopt%3DAbstract</link>
            <description>In this report, two putative IFN-gamma receptor chains were identified and sequenced in rainbow trout (Oncorhynchus mykiss), and found to have many common characteristics with mammalian type II IFN receptor family members. The presented gene synteny analysis, phylogenetic tree analysis and ligand binding analysis all suggest that these molecules are the authentic IFNgammaRs in fish. They are widely expressed in tissues, with IFNgammaR1 typically more highly expressed than IFNgammaR2. Using the trout RTG-2 cell line it was possible to show that the individual chains could be differentially modulated, with rIFN-gamma and rIL-1beta down regulating IFNgammaR1 expression but up regulating IFNgammaR2 expression. Over-expression of the two receptor chains in RTG-2 cells revealed that the level of...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528992</comments>
            <pubDate>Sat, 27 Jun 2009 13:02:56 +0100</pubDate>
            <guid isPermaLink="false">2528992</guid>        </item>
        <item>
            <title>Identification and cloning of an invertebrate-type lysozyme from Eisenia andrei.</title>
            <link>http://www.medworm.com/index.php?rid=2528989&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454335%26dopt%3DAbstract</link>
            <description>Authors: Joskov&amp;#xE1; R, Silerov&amp;#xE1; M, Proch&amp;#xE1;zkov&amp;#xE1; P, Bilej M
    Lysozyme is a widely distributed antimicrobial protein having specificity for cleaving the beta-(1,4)-glycosidic bond between N-acetylmuramic acid (NAM) and N-acetylglucosamine (GlcNAc) of peptidoglycan of the bacterial cell walls and thus efficiently contributes to protection against infections caused mainly by Gram-positive bacteria. In the present study, we assembled a full-length cDNA of a novel invertebrate-type lysozyme from Eisenia andrei earthworm (EALys) by RT-PCR and RACE system. The primary structure of EALys shares high homology with other invertebrate lysozymes; however the highest, 72% identity, was shown for the destabilase I isolated from medicinal leech. Recombinant EALys expressed in Escherichi...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528989</comments>
            <pubDate>Sat, 27 Jun 2009 13:02:51 +0100</pubDate>
            <guid isPermaLink="false">2528989</guid>        </item>
        <item>
            <title>Characterization and evolution of MHC class II B genes in Galápagos marine iguanas (Amblyrhynchus cristatus).</title>
            <link>http://www.medworm.com/index.php?rid=2528986&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454336%26dopt%3DAbstract</link>
            <description>In this study, eight class II B cDNA sequences were obtained from the Gal&amp;#xE1;pagos marine iguana (Amblyrhynchus cristatus) which were divided into five locus groups, Amcr-DAB1 through -DAB5, based on similarities along most of the coding and noncoding portions of the transcribed gene. All marine iguana sequences were monophyletic with respect to class II genes from other vertebrates indicating that they originated from a common ancestral locus after squamates split from other reptiles. The beta-1 domain, which is involved in antigen binding, exhibited signatures of positive selection as well as interlocus gene conversion in both long and short tracts-a pattern also observed in birds and fish, but not in mammals. On the other hand, the beta-2 domain was divergent between gene groups, whic...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528986</comments>
            <pubDate>Sat, 27 Jun 2009 13:02:46 +0100</pubDate>
            <guid isPermaLink="false">2528986</guid>        </item>
        <item>
            <title>Report on the 20th annual meeting of the Japanese Association for Developmental and Comparative Immunology (JADCI), which was held from August 25-27, 2008, at University of Tokyo Medical and Dental School, Tokyo, Japan (Local Organizer: Takeshi Yoshida, M.D.).</title>
            <link>http://www.medworm.com/index.php?rid=2528983&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19454337%26dopt%3DAbstract</link>
            <description>Authors: Yoshida T
    
    PMID: 19454337 [PubMed - in process] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528983</comments>
            <pubDate>Sat, 27 Jun 2009 13:02:42 +0100</pubDate>
            <guid isPermaLink="false">2528983</guid>        </item>
        <item>
            <title>Differential modulation of beta-defensin gene expression by Salmonella Enteritidis in intestinal epithelial cells from resistant and susceptible chicken inbred lines.</title>
            <link>http://www.medworm.com/index.php?rid=2528937&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19539093%26dopt%3DAbstract</link>
            <description>Authors: Derache C, Esnault E, Bonsergent C, Le Vern Y, Qu&amp;#xE9;r&amp;#xE9; P, Lalmanach AC
    beta-Defensins are important components of innate immunity in mucosal tissue, a major entry site for several pathogens. These small cationic peptides possess antimicrobial activity against various microorganisms including Salmonella. Two chicken inbred lines, 6 and 15I, diverge phenotypically with respect to levels of Salmonella Enteritidis intestinal carriage and to level of gene expression of two beta-defensins, AvBD1 and AvBD2. The cellular source of these two defensins in the intestinal tissue has not previously been explored. Therefore embryonic intestinal cells were isolated from both chicken lines. Primary intestinal cell cultures expressed epithelial specific markers (villin and E-cadherin) ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528937</comments>
            <pubDate>Sat, 27 Jun 2009 13:01:33 +0100</pubDate>
            <guid isPermaLink="false">2528937</guid>        </item>
        <item>
            <title>The avian Toll-Like receptor pathway--subtle differences amidst general conformity.</title>
            <link>http://www.medworm.com/index.php?rid=2528934&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19539094%26dopt%3DAbstract</link>
            <description>Authors: Cormican P, Lloyd AT, Downing T, Connell SJ, Bradley D, O'Farrelly C
    The Toll-Like receptor (TLR) pathway plays a core role in innate immunity and is maintained with remarkable consistency across all vertebrate species. Amidst this background of overall conservation, subtle differences in the components that make up this pathway may have important implications for species-specific defense against key pathogens. Here we employ a homology-based comparative method to characterize the TLR pathway in the recently sequenced chicken and zebra finch genomes, which represent two distantly related bird species. The key features of the TLR pathway are conserved in birds and mammals, although some clear differences exist. The TLR receptors show a pattern of gene duplication and gene loss ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528934</comments>
            <pubDate>Sat, 27 Jun 2009 13:01:27 +0100</pubDate>
            <guid isPermaLink="false">2528934</guid>        </item>
        <item>
            <title>Identification of a novel relish homolog in Chinese shrimp Fenneropenaeus chinensis and its function in regulating the transcription of antimicrobial peptides.</title>
            <link>http://www.medworm.com/index.php?rid=2528960&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19520110%26dopt%3DAbstract</link>
            <description>Authors: Li F, Yan H, Wang D, Priya TA, Li S, Wang B, Zhang J, Xiang J
    Penaeid shrimp, as an invertebrate, relies on the innate immunity to oppose the microbial invaders. Antimicrobial peptides (AMP) are an integral component of the innate immune system in most organisms and function as an early first line of defense against pathogens, but the knowledge about the pathways to regulate the shrimp AMP gene expression is still absent up to date. In the current study, a Relish homolog (FcRelish) was cloned from Chinese shrimp Fenneropenaeus chinensis. The full length cDNA of FcRelish consists of 2157bp, including 1512bp open reading frame, encoding 505 amino acids. The predicted molecular weight of FcRelish is 57kDa, and the theoretical PI is 7.00. Spatial expression profiles showed that Fc...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528960</comments>
            <pubDate>Thu, 18 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528960</guid>        </item>
        <item>
            <title>Unraveling the protective effect of a Drosophila phosphatidylethanolamine-binding protein upon bacterial infection by means of proteomics.</title>
            <link>http://www.medworm.com/index.php?rid=2528924&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19545586%26dopt%3DAbstract</link>
            <description>This study addresses the biological function of CG18594, a Drosophila melanogaster phosphatidylethanolamine-binding protein (PEBP) that we named PEBP1, by combining fly genetics, survival experiments and differential proteomics. We demonstrate that transgenic flies overexpressing PEBP1 are highly protected against bacterial infection due to the release of immunity-related proteins in their hemolymph. Apart from proteins that have been reported earlier to participate in insect immunity, we also identify proteins involved in metabolism and signaling, and, in addition, twelve (hypothetical) proteins with unknown function. This is the first report demonstrating an immune function for a Drosophila PEBP protein.
    PMID: 19545586 [PubMed - as supplied by publisher] (Source: Developmental and Co...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528924</comments>
            <pubDate>Thu, 18 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528924</guid>        </item>
        <item>
            <title>Bacterial, but not baculoviral infections stimulate Hemolin expression in noctuid moths.</title>
            <link>http://www.medworm.com/index.php?rid=2528926&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19540262%26dopt%3DAbstract</link>
            <description>Authors: Terenius O, Popham HJ, Shelby KS
    Lepidopteran larvae are regularly infected by baculoviruses during feeding on infected plants. The differences in sensitivity to these infections can be substantial, even among closely related species. For example, the noctuids Cotton bollworm (Helicoverpa zea) and Tobacco budworm (Heliothis virescens), have a 1000-fold difference in sensitivity to Autographa californica multiple nucleopolyhedrovirus (AcMNPV) infection. Recent data were interpreted to indicate that the lepidopteran immunoglobulin protein, Hemolin, is synthesized upon viral injection and therefore to participate in anti-viral responses. To investigate whether Hemolin synthesis is affected by a natural viral infection, specific transcription in fat bodies and hemocytes of H. zea ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528926</comments>
            <pubDate>Tue, 16 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528926</guid>        </item>
        <item>
            <title>Immune effects observed after the injection of plasmids coding for rainbow trout (Oncorhynchus mykiss) CK5B, CK6 and CK7A chemokines demonstrate their immunomodulatory capacity and reveal CK6 as a major interferon inducer.</title>
            <link>http://www.medworm.com/index.php?rid=2528929&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19539644%26dopt%3DAbstract</link>
            <description>Authors: Montero J, Chaves-Pozo E, Cuesta A, Tafalla C
    In the current study, we have determined the immune effects of the intramuscular injection of eukaryotic expression plasmids coding for rainbow trout (Oncorhynchusmykiss) CK5B, CK6 or CK7A CC chemokines (pCK5B, pCK6 and pCK7A) as a first step towards the establishment of their biological role. We have studied the levels of expression of several immune genes in the spleen and head kidney by real time PCR in comparison to the levels observed in animals injected with the empty plasmid. Concerning the levels of expression of these CC chemokines and the CXC chemokine, interleukin 8 (IL-8), each plasmid induced up-regulation on expression levels of its coded chemokine in the head kidney and spleen, but also affected the expression of oth...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528929</comments>
            <pubDate>Mon, 15 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528929</guid>        </item>
        <item>
            <title>Differential gene expression in black tiger shrimp, Penaeus monodon, following administration of oxytetracycline and oxolinic acid.</title>
            <link>http://www.medworm.com/index.php?rid=2528964&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19497335%26dopt%3DAbstract</link>
            <description>Authors: Fagutao FF, Yasuike M, Santos MD, Ruangpan L, Sangrunggruang K, Tassanakajon A, Takahashi Y, Ueno R, Kondo H, Hirono I, Aoki T
    The intensification of shrimp farming systems has led to the spreading of a variety of bacterial and viral diseases that continue to plague the shrimp industry worldwide. Efforts to combat these pathogenic organisms include the use of immunostimulants, probiotics, vaccines and antibiotics. Although a few studies have already reported on the effects of various stimuli on shrimp, the effect of antibiotics, particularly on the changes in the shrimp transcriptomic profile have yet to be reported. Here we show that injecting shrimp with oxytetracycline and oxolinic acid alters the expression of genes in the black tiger shrimp, Penaeus monodon, lymphoid orga...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528964</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528964</guid>        </item>
        <item>
            <title>Bacteriolytic activity of the alternative pathway of complement differs kinetically from the classical pathway.</title>
            <link>http://www.medworm.com/index.php?rid=2528956&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527746%26dopt%3DAbstract</link>
            <description>Authors: Kilpi MK, Atosuo JT, Lilius EM
    The interaction between bacterial cells and activated complement components as a kinetic biological event is described. The bacteriolytic activity of complement in human and fish serum was assayed by measuring the decrease of bioluminescence of Escherichia coli transformed with lux genes. From the kinetic curves, the bacteriolytic CB(50)- and AB(50)-units were derived at any desired time point. It was observed that these values were irregular but decreased as a function of incubation time, and reached equal values during prolonged incubation, suggesting that the difference between the classical and alternative pathway activity is kinetic. From the kinetic curves, entirely new parameters could be derived: rate of the activation phase, rate of kill...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528956</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528956</guid>        </item>
        <item>
            <title>Gene expression patterns associated with chicken jejunal development.</title>
            <link>http://www.medworm.com/index.php?rid=2528953&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527747%26dopt%3DAbstract</link>
            <description>Authors: Schokker D, Hoekman AJ, Smits MA, Rebel JM
    Jejunal development occurs in a spatio-temporal pattern and is characterized by morphological and functional changes. To investigate jejunal development at the transcriptomic level, we performed microarray studies in 1-21 day-old chickens. Nine gene clusters were identified, each with a specific gene expression pattern. Subsequently, groups of genes with similar functions could be identified. Genes involved in morphological and functional development were highly expressed immediately after hatch with declining expression patterns afterwards. Immunological development can be roughly divided based on expression patterns in three processes over time; first innate response and immigration of immune cells, secondly differentiation and spec...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528953</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528953</guid>        </item>
        <item>
            <title>Multipeptide precursor structure of acaloleptin A isoforms, antibacterial peptides from the Udo longicorn beetle, Acalolepta luxuriosa.</title>
            <link>http://www.medworm.com/index.php?rid=2528950&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527748%26dopt%3DAbstract</link>
            <description>In this study, we performed cDNA cloning. The cDNA sequence showed a predicted acaloleptin A precursor that consisted of five acaloleptin A isoforms. Four (isoforms 1, 2, 3 and 4) of the five isoforms of the acaloleptin A precursor had high-level sequence identities with each other, but the N-terminal region of isoform 5 differed from those of the other acaloleptin A isoforms. Northern and Western blot analyses showed that acaloleptin A isoforms were mass-produced soon after bacterial inoculation. Finally we purified isoform 5 from hemolymph of the immunized larvae. Isoform 5, unlike acaloleptin A1, A2 and A3, showed antimicrobial activities against a Gram-positive bacterium, Micrococcus luteus and a fungus,Magnaporthe grisea. These results suggest that the multipeptide structure of the ac...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528950</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528950</guid>        </item>
        <item>
            <title>Genomic structure of the whole D-J-C clusters and the upstream region coding V segments of the TRB locus in pig.</title>
            <link>http://www.medworm.com/index.php?rid=2528943&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527749%26dopt%3DAbstract</link>
            <description>In this study, we determined 212,193bp of a continuous porcine genomic sequence covering the entire TRBC region. EPHB6, TRPV6, TRY, and ten TRBV genes were conserved in the vicinity of the TRBD-J-C clusters. Interestingly, three TRBD-J-C clusters were identified in this sequence; each TRBD-J-C cluster consisted of one TRBD and seven TRBJ segments, with one TRBC region composed of four exons. The distribution of repetitive sequences and phylogenetic analysis indicated that the TRBD-J-C cluster, located at the center of the three clusters identified, had a structure combined with the others. Most of the TRBJ segments were available in public databases, suggesting that all three TRBD-J-C clusters are functional in pigs.
    PMID: 19527749 [PubMed - as supplied by publisher] (Source: Developme...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528943</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528943</guid>        </item>
        <item>
            <title>Trypanosoma carassii hsp70 increases expression of inflammatory cytokines and chemokines in macrophages of the goldfish (Carassius auratus L.).</title>
            <link>http://www.medworm.com/index.php?rid=2528941&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527750%26dopt%3DAbstract</link>
            <description>We report on the cloning and characterization of Trypanosoma carassii 70KDa heat shock protein (hsp70). T. carassii hsp70 was secreted/excreted into culture medium in vitro and was recognized by sera from infected fish. Recombinant hsp70 (rhsp70) activated goldfish macrophages and stimulated the production of pro-inflammatory cytokines including interferon gamma (IFNgamma), tumor necrosis factor (TNF)-alpha, interleukin (IL)-1beta, (IL)-12 and chemokines CCL-1 and CXCL-8 (IL-8). T. carassii hsp70-induced cytokine expression was abrogated by pronase treatment of macrophages confirming the existence of receptor(s) on goldfish macrophage surface that recognize parasite molecule. Parasite hsp70 also up-regulated the expression inducible nitric oxide synthase (iNOS) isoforms A and B and induced...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528941</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528941</guid>        </item>
        <item>
            <title>Molecular and functional characterization of kita and kitla of the goldfish (Carassius auratus L.).</title>
            <link>http://www.medworm.com/index.php?rid=2528939&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19527751%26dopt%3DAbstract</link>
            <description>In this study we report on the molecular and functional characterization of kit receptor A (kita) and kit ligand A (kitla) from the goldfish. Both kita and kitla were ubiquitously expressed in goldfish tissues, with higher mRNA levels observed in the kidney and spleen, the major hematopoietic organs in fish. Furthermore, both kita and kitla expression decreased in a time dependent manner in goldfish primary kidney macrophage (PKM) cultures, as progenitor to macrophage development progressed, and the highest expression of both the receptor and ligand were observed in sorted progenitor cell populations. Activation of mature macrophage cultures increased both kita and kitla expression. Kit ligand A induced chemotactic response, proliferation and survival of PKM cells in a dose-dependent manne...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528939</comments>
            <pubDate>Thu, 11 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528939</guid>        </item>
        <item>
            <title>Identification of phagocytic cells, NK-like cytotoxic cell activity and the production of cellular exudates in the coelomic cavity of adult zebrafish.</title>
            <link>http://www.medworm.com/index.php?rid=2528968&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19477195%26dopt%3DAbstract</link>
            <description>Authors: Moss LD, Monette MM, Jaso-Friedmann L, Leary JH, Dougan ST, Krunkosky T, Evans DL
    Coelomic cavity (CC) cells of mature zebrafish harvested by lavage with media or trypsin-EDTA contained 0.80-1.20x10(5) and 2.0-3.5x10(5) cells, respectively. Media lavage was composed of granulocytes (60-80%), lymphocytes (10-20%), and NCC (4-10%). Granulocytes had large electron dense cytoplasmic paracrystalline granules and a segmented nucleus; they expressed plastin-1, myeloid specific peroxidase and MCSF mRNA; and they were NCAMP-1(+). Lymphocytes had B- and T-cell specific mRNA and were NCAMP-1(-) and NCCRP-1(-). NCC were 3mum, NCAMP-1(+) and NCCRP-1(+) and did not express B- and T-cell specific mRNA. Additionally, trypsin lavage contained monocytes (marginated chromatin, low nuclear:cytopl...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528968</comments>
            <pubDate>Fri, 05 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528968</guid>        </item>
        <item>
            <title>The genomic structure, alternative splicing and immune response of Chlamys farreri thioester-containing protein.</title>
            <link>http://www.medworm.com/index.php?rid=2528972&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19467260%26dopt%3DAbstract</link>
            <description>Authors: Zhang H, Wang L, Song L, Zhao J, Qiu L, Gao Y, Song X, Li L, Zhang Y, Zhang L
    CfTEP is a member of thioester-containing protein (TEP) family found in Zhikong scallop Chlamys farreri and is involved in innate immunity against invading microbes. In the present study, the genomic DNA of CfTEP was cloned and characterized. The genomic DNA sequence of CfTEP consisted of 40 exons and 39 introns spanning 35kb with all exon-intron junction sequences agreeing with the GT/AG consensus. The genomic organization of CfTEP was similar to human and mouse C3 rather than ciona C3-1 and Drosophila dTEP2. By RT-PCR technique, seven different cDNA variants of CfTEP (designated as CfTEP-A-CfTEP-G) were cloned from scallop gonad. CfTEP-A-CfTEP-F were produced by alternative splicing of six mutually...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528972</comments>
            <pubDate>Tue, 02 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528972</guid>        </item>
        <item>
            <title>Characterization of crustin antimicrobial proteins from Japanese spiny lobster Panulirus japonicus.</title>
            <link>http://www.medworm.com/index.php?rid=2528979&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19465048%26dopt%3DAbstract</link>
            <description>Authors: Pisuttharachai D, Fagutao FF, Yasuike M, Aono H, Yano Y, Murakami K, Kondo H, Aoki T, Hirono I
    Crustin antimicrobial proteins (PJC1-4) were identified from a phyllosoma library of Japanese spiny lobster, Panulirus japonicus. The deduced amino acid sequences of PJC1-4 contained open reading frames of 130, 139, 124 and 150 amino acid residues, respectively. These proteins contained a glycine-rich region at the N-terminus and 12 conserved cysteine residues containing a single whey acidic protein (WAP) domain at the C-terminus. A phylogenetic tree and sequences alignment analyses revealed that PJC1-4 are more closely related to shrimp crustins than to other lobster crustins. Transcripts of PJC1, 3 and 4 were detected in heart, nerves, intestine, hemocytes, gills and hepatopancreas...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528979</comments>
            <pubDate>Mon, 01 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528979</guid>        </item>
        <item>
            <title>Bombyx mori transferrin: Genomic structure, expression and antimicrobial activity of recombinant protein.</title>
            <link>http://www.medworm.com/index.php?rid=2528975&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19467259%26dopt%3DAbstract</link>
            <description>In this study, we identified and characterized Bombyx mori transferrin (BmTf). The promoter region of BmTf has numerous putative NF-kappaB binding sites, suggesting its possible function in innate immunity. Analysis of BmTf gene expression shows that it is highly inducible in response to a wide variety of pathogens including bacteria, fungus, and viruses. Recombinant BmTf protein produced in a baculovirus system exhibits iron binding capacity and antibacterial activity against various Gram-positive and -negative bacteria. Taken together, our results indicate that BmTf is an inducible immune effector molecule that may play an important role in pathogen clearance of insect innate immunity.
    PMID: 19467259 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunolog...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2528975</comments>
            <pubDate>Mon, 01 Jun 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2528975</guid>        </item>
        <item>
            <title>Is activated hemocyanin instead of phenoloxidase involved in immune response in woodlice?</title>
            <link>http://www.medworm.com/index.php?rid=2529003&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19447131%26dopt%3DAbstract</link>
            <description>Authors: Jaenicke E, Fraune S, May S, Irmak P, Augustin R, Meesters C, Decker H, Zimmer M
    In the Common woodlouse Porcellio scaber (Crustacea: Isopoda: Oniscidea), experimental immune challenge did not induce the expression of pro-phenoloxidase that, in most other invertebrates studied thus far, can be activated into phenoloxidase via an activation cascade upon immune challenge. Instead, Porcellio hemocyanin proved to exhibit catecholoxidase activity upon activation. However, none of the activating factors known from other invertebrates other than SDS-treatment resulted in activation of hemocyanin into a functional phenoloxidase in vitro. The distinct characteristics of isopod hemocyanin are reflected by the quaternary structure of the hemocyanin dodecamers that differs from that of ot...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529003</comments>
            <pubDate>Wed, 27 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2529003</guid>        </item>
        <item>
            <title>Phagocytosis mediates specificity in the immune defence of an invertebrate, the woodlouse Porcellio scaber (Crustacea: Isopoda).</title>
            <link>http://www.medworm.com/index.php?rid=2529020&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19416736%26dopt%3DAbstract</link>
            <description>Authors: Roth O, Kurtz J
    Specificity and memory are the hallmarks of the adaptive immune system of vertebrates. However, phenomena of specificity upon priming of immunity have recently been demonstrated also in invertebrates, which rely exclusively on innate immune defence. It has been suggested that phagocytosis might represent a core candidate for such specificity in invertebrates. We here developed in vitro phagocytosis measurements for different bacteria in the woodlouse Porcellio scaber (Crustacea: Isopoda). After immune priming with heat-killed bacteria, hemocytes showed increased phagocytosis of a previously encountered bacterial strain compared to other bacteria. These data support the role of phagocytosis in invertebrate immunological specificity and suggest a high degree of s...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2529020</comments>
            <pubDate>Thu, 14 May 2009 23:00:00 +0100</pubDate>
            <guid isPermaLink="false">2529020</guid>        </item>
        <item>
            <title>Identification and comparative analysis of three novel C-type lectins from the silkworm with functional implications in pathogen recognition.</title>
            <link>http://www.medworm.com/index.php?rid=2173193&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19201380%26dopt%3DAbstract</link>
            <description>Authors: Takase H, Watanabe A, Yoshizawa Y, Kitami M, Sato R
    C-type lectins can act as pattern recognition receptors (PRRs) in innate immunity. Previously, we identified two C-type lectins from silkworm (Bombyx mori), BmLBP and BmMBP, as PRRs. In the present study, we identified three homologs of these lectins by searching the silkworm genome database. These novel B. mori low-expression lectins were designated BmLEL-1, BmLEL-2, and BmLEL-3. Although Western-blot analysis failed to detect BmLEL-1, -2, or -3 in plasma, affinity precipitation of larval plasma with various microorganisms revealed that BmLEL-1 and -2 bind to rough and smooth strains of Gram-negative bacteria, respectively. BmLEL-1, -2, and -3 were found to be expressed in testis and ovary, where BmLEL-2 expression was up-re...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2173193</comments>
            <pubDate>Thu, 05 Feb 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2173193</guid>        </item>
        <item>
            <title>Gene profiling studies in the neonatal ovine lung show enhancing effects of VEGF on the immune response.</title>
            <link>http://www.medworm.com/index.php?rid=2163690&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19189846%26dopt%3DAbstract</link>
            <description>We report that VEGF induced the expression of chemokines (IL-8, RANTES, MCP-1), cytokines (IFN-gamma, IL-6, TNF-alpha, GMCSF), Toll-like receptor (TLR)-4, complement family members (C3, CFB, CFH) and collectins (SP-A, SP-D). These results suggest that VEGF can regulate local immune gene expression in vivo and should be further explored as a potential exogenous therapy for various lung diseases.
    PMID: 19189846 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2163690</comments>
            <pubDate>Sat, 31 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2163690</guid>        </item>
        <item>
            <title>Characterization of a C-type lectin from the cotton bollworm, Helicoverpa armigera.</title>
            <link>http://www.medworm.com/index.php?rid=2156702&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19185587%26dopt%3DAbstract</link>
            <description>In this study, recombinant CRD1 and CRD2 were expressed separately in Escherichia coli and purified. They have the ability to agglutinate Gram-negative and Gram-positive bacteria and fungi in the presence of Ca(2+). They also have different spectra of sugar binding abilities. The rHa-lectin, rCRD1 and rCRD2 could inhibit the growth in quantity of Bacillus thuringiensis in vivo by increasing hemocyte phagocytosis. These results suggested that Ha-lectin and its two domains could function as a pattern recognition receptor or an opsonin in vivo to promote the hemocyte phagocytosis of pathogens and protect the insect from bacterial infection.
    PMID: 19185587 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2156702</comments>
            <pubDate>Wed, 28 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2156702</guid>        </item>
        <item>
            <title>Cflec-4, a multidomain C-type lectin involved in immune defense of Zhikong scallop Chlamys farreri.</title>
            <link>http://www.medworm.com/index.php?rid=2156701&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19185588%26dopt%3DAbstract</link>
            <description>In this study, a novel multidomain C-type lectin gene from scallop Chlamys farreri (designated as Cflec-4) was cloned by RACE approach based on EST analysis. The full-length cDNA of Cflec-4 was of 2086bp. The open reading frame was of 1830bp and encoded a polypeptide of 609 amino acids, including a signal sequence and four dissimilar carbohydrate-recognition domains (CRDs). The deduced amino acid sequence of Cflec-4 shared high similarities to other C-type lectin family members. The phylogenetic analysis revealed the divergence between the three N-terminal CRDs and the C-terminal one, suggesting that the four CRDs in Cflec-4 originated by repeated duplication of different primordial CRD. The potential tertiary structure of each CRD in Cflec-4 was typical double-loop structure with Ca(2+)-b...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2156701</comments>
            <pubDate>Wed, 28 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2156701</guid>        </item>
        <item>
            <title>Involvement of protein kinase C signalling and mitogen-activated protein kinase in the amebocyte-producing organ of Biomphalaria glabrata (Mollusca).</title>
            <link>http://www.medworm.com/index.php?rid=2156703&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19183562%26dopt%3DAbstract</link>
            <description>Authors: Salamat Z, Sullivan JT
    Mechanisms that regulate hemocyte production in molluscs, at either the organismal or cellular levels, are not well understood. In the present study, 24-h saline cultures of the amebocyte-producing organ (APO) of the schistosome-transmitting snail Biomphalaria glabrata were used to test for the potential involvement of protein kinase C (PKC) signalling in hematopoiesis. Exposure to phorbol myristate acetate (PMA), an activator of PKC, resulted in an increase in the number of dividing hematopoietic cells in APOs from schistosome-resistant Salvador snails. PMA-induced cell division was blocked by treatment with U0126, an inhibitor of the mitogen-activated protein kinase kinase, MEK1/2. These results suggest that PKC-induced activation of the mitogen-activa...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2156703</comments>
            <pubDate>Tue, 27 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2156703</guid>        </item>
        <item>
            <title>Identification of a porcine DC-SIGN-related C-type lectin, porcine CLEC4G (LSECtin), and its order of intron removal during splicing: Comparative genomic analyses of the cluster of genes CD23/CLEC4G/DC-SIGN among mammalian species.</title>
            <link>http://www.medworm.com/index.php?rid=2153039&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19166875%26dopt%3DAbstract</link>
            <description>In this study, we have experimentally identified the cDNA and the gene encoding porcine CLEC4G (pCLEC4G). Full-length pCLEC4G cDNA encodes a type II transmembrane protein of 290 amino acids. pCLEC4G gene has the same gene structure as the human and the predicted bovine, canis, mouse and rat CLEC4G genes with nine exons. A multi-species-conserved site at the extreme 3'-untranslated region of CLEC4G mRNAs was predicted to be targeted by microRNA miR-350 in domesticated animals and by miR-145 in primates, respectively. We detected pCLEC4G mRNA expression in liver, lymph node and spleen tissues. We also identified a series of sequential intermediate products of pCLEC4G pre-mRNA during splicing from pig liver. The previously unidentified porcine CD23 cDNA containing the complete coding region w...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2153039</comments>
            <pubDate>Wed, 21 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2153039</guid>        </item>
        <item>
            <title>An fMLP receptor is involved in activation of phagocytosis by hemocytes from specific insect species.</title>
            <link>http://www.medworm.com/index.php?rid=2137814&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19166874%26dopt%3DAbstract</link>
            <description>Authors: Garc&amp;#xED;a-Garc&amp;#xED;a E, Garc&amp;#xED;a-Garc&amp;#xED;a PL, Rosales C
    In mammalian phagocytes, the bacterial formylated peptide fMLP functions both as a potent enhancer of phagocytosis and chemoattractant. fMLP has been reported to be chemotactic for hemocytes of two marine invertebrates, and of the insect Manduca sexta (Lepidoptera). Whether fMLP is also able to activate phagocytosis has not been explored in hemocytes of any invertebrate. To determine the effect of fMLP on insect hemocyte phagocytosis, in vitro phagocytosis assays were performed with hemocytes from the insects: Gromphadorhina portentosa (Blattodea), Acheta domesticus (Orthoptera), Zophobas morio (Coleoptera), and Galleria mellonella (Lepidoptera). Phagocytosis of latex, zymosan (yeast), Gram-positive and Gram-nega...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2137814</comments>
            <pubDate>Tue, 20 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2137814</guid>        </item>
        <item>
            <title>Identification of a porcine DC-SIGN-related C-type lectin, porcine CLEC4G (LSECtin), and its order of intron removal during splicing: Comparative genomic analyses of the cluster of genes CD23/CLEC4G/DC-SIGN gene among mammalian species.</title>
            <link>http://www.medworm.com/index.php?rid=2137813&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19166875%26dopt%3DAbstract</link>
            <description>In this study, we have experimentally identified the cDNA and the gene encoding porcine CLEC4G (pCLEC4G). Full-length pCLEC4G cDNA encodes a type II transmembrane protein of 290 amino acids. pCLEC4G gene has the same gene structure as the human and the predicted bovine, canis, mouse and rat CLEC4G genes with nine exons. A multi-species-conserved site at the extreme 3'-untranslated region of CLEC4G mRNAs was predicted to be targeted by microRNA miR-350 in domesticated animals and by miR-145 in primates, respectively. We detected pCLEC4G mRNA expression in liver, lymph node and spleen tissues. We also identified a series of sequential intermediate products of pCLEC4G pre-mRNA during splicing from pig liver. The previously unidentified porcine CD23 cDNA containing the complete coding region w...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2137813</comments>
            <pubDate>Tue, 20 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2137813</guid>        </item>
        <item>
            <title>The human antimicrobial protein psoriasin acts by permeabilization of bacterial membranes.</title>
            <link>http://www.medworm.com/index.php?rid=2131429&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19162067%26dopt%3DAbstract</link>
            <description>Authors: Michalek M, Gelhaus C, Hecht O, Podschun R, Schr&amp;#xF6;der JM, Leippe M, Gr&amp;#xF6;tzinger J
    Psoriasin, a member of the S100 family of calcium-binding proteins (S100A7) is highly upregulated in the skin of psoriasis patients. As it has recently been found to exhibit antimicrobial activity, an important role of psoriasin in surface defence has been suggested. The similarity of the three-dimensional structures of psoriasin and amoebapore A, an ancient antimicrobial, pore-forming peptide from Entamoeba histolytica, intrigued us to investigate whether the human psoriasin is also able to permeabilize bacterial membranes. Here, we demonstrate that psoriasin exerts pore-forming activity at pH values below 6 demonstrating that disruption of microbial membranes is the basis of its antimic...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2131429</comments>
            <pubDate>Mon, 19 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2131429</guid>        </item>
        <item>
            <title>Nitric oxide production and nitric oxide synthase type 2 expression by cotton rat (Sigmodon hispidus) macrophages reflect the same pattern as human macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=2125425&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19154756%26dopt%3DAbstract</link>
            <description>Authors: Carsillo M, Kutala VK, Puschel K, Blanco J, Kuppusamy P, Niewiesk S
    Our knowledge of the antibacterial role of nitric oxide (NO) during infection is based on studies of murine macrophages, which secrete large amounts of NO. In contrast, human macrophages produce very little NO and its relevance as an antibacterial mediator during infection of humans is uncertain. We have defined bone marrow-derived macrophages from cotton rats (Sigmodon hispidus). These macrophages display phenotypical and functional characteristics similar to other rodent and human macrophages. The most interesting finding was the low level of NO production which is in contrast to findings for murine macrophages, but consistent with those of humans. In spite of these low levels, inhibition of NO production le...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2125425</comments>
            <pubDate>Sat, 17 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2125425</guid>        </item>
        <item>
            <title>Identification and functional characterization of a novel cytidine deaminase in a gastropod abalone, Haliotis diversicolor supertexta.</title>
            <link>http://www.medworm.com/index.php?rid=2116003&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19150626%26dopt%3DAbstract</link>
            <description>Authors: Wu L, Wu X, Zhu B, Cao X
    Cytidine deaminase (CDA, also designated CDD) is a zinc-dependent enzyme involved in the pyrimidine salvage pathways and becoming very important in anticancer and antiviral therapy. Here we report the identification and characterization of a CDA homologue in abalone, which we named ab-CDA. The analysis of the amino acids sequence revealed that the ab-CDA shares conserved signature motifs and belongs to homotetrameric class of CDA family. Real-time PCR analysis indicated that the ab-CDA was ubiquitously expressed in various tissues of abalone and relatively higher expressed in hemocyte. Significant up-regulation of ab-CDA was also observed after LPS or Poly I: C challenge. The biological activity of ab-CDA was identified by spectrophotometry analysis an...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2116003</comments>
            <pubDate>Thu, 15 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2116003</guid>        </item>
        <item>
            <title>The N-terminal half of the Drosophila Rel/NF-kappaB factor Relish, REL-68, constitutively activates transcription of specific Relish target genes.</title>
            <link>http://www.medworm.com/index.php?rid=2101225&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19135474%26dopt%3DAbstract</link>
            <description>Authors: Wiklund ML, Steinert S, Junell A, Hultmark D, St&amp;#xF6;ven S
    The Rel/NF-kappaB transcription factor Relish is a major regulator of the antimicrobial response in Drosophila. Upon immune challenge, Relish is cleaved to generate two fragments, the DNA-binding transcription factor REL-68 and the IkappaB-like REL-49. Using transgenic fly strains we show here that overexpression of REL-68 separately from REL-49 is sufficient to activate strong constitutive transcription of the Diptericin gene, but little constitutive or inducible transcription of Attacin and Cecropin, two other Relish target genes. Their transcription may therefore require additional modifications of Relish. However, phosphorylation of the conserved serine residue S431 is not involved in such modifications. This is u...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2101225</comments>
            <pubDate>Wed, 07 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2101225</guid>        </item>
        <item>
            <title>Expression and localization of rabbit B-cell activating factor (BAFF) and its specific receptor BR3 in cells and tissues of the rabbit immune system.</title>
            <link>http://www.medworm.com/index.php?rid=2087079&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19124039%26dopt%3DAbstract</link>
            <description>Authors: Yang J, Pospisil R, Mage RG
    Rabbits are widely used for vaccine development, and investigations of human infectious and autoimmune diseases such as Systemic Lupus Erythematosus (SLE). For these applications, we cloned, sequenced and expressed rabbit B-cell Activating Factor (BAFF), and localized BAFF in cells and tissues of the rabbit immune system. The rabbit homolog of the human BAFF binding site (miniBR3 peptide) within the BAFF-specific receptor BR3 was synthesized. This 26-residue core domain binds to recombinant rabbit BAFF protein. Flow cytometric analyses using purified recombinant rabbit BAFF combined with real-time PCR findings revealed that BAFF detected on peripheral blood B-cells from normal rabbits is probably complexed to BAFF receptors rather than produced by t...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2087079</comments>
            <pubDate>Fri, 02 Jan 2009 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2087079</guid>        </item>
        <item>
            <title>A serpin from the parasitoid wasp Leptopilina boulardi targets the Drosophila phenoloxidase cascade.</title>
            <link>http://www.medworm.com/index.php?rid=2067798&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19109990%26dopt%3DAbstract</link>
            <description>Authors: Colinet D, Dubuffet A, Cazes D, Moreau S, Drezen JM, Poiri&amp;#xE9; M
    The insect phenoloxidase (PO) cascade is known to be tightly regulated by serine proteases and serine protease inhibitors of the serpin family. As a key component of the insect immune system, it is also suspected to be inhibited by several endoparasitoid wasps, insects that develop inside other arthropods as hosts. However, the underlying mechanisms of this inhibition are largely undescribed. Here, we report the characterization of a gene encoding a serpin, LbSPNy, highly expressed in the venom of the wasp Leptopilina boulardi (IS(y) type), and we show that either the venom or the recombinant LbSPNy inhibit the PO cascade in the hemolymph of Drosophila yakuba host larva. Altogether, our results identify the fir...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2067798</comments>
            <pubDate>Mon, 22 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2067798</guid>        </item>
        <item>
            <title>ProPhenolOxidase in Daphnia magna: cDNA sequencing and expression in relation to resistance to parasitism.</title>
            <link>http://www.medworm.com/index.php?rid=2065444&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19103220%26dopt%3DAbstract</link>
            <description>This study was focused on the proPO gene of Daphnia magna. D. magna possesses a single copy of proPO (as does its congener, D. pulex), but there was some evidence of alternative splicing. Analyses of sequence similarity in a range of arthropod taxa suggested that the proPO gene in Daphnia was as dissimilar to other crustaceans as it was to insects, while analysis on intraspecific variation indicated that the gene is highly conserved. ProPO was found to be significantly up-regulated within 1-4h following exposure to the bacteria. This is the first evidence of a Daphnia immune response, and our observations raise the possibility that the PhenolOxidase (PO) cascade is involved in the defence against pathogenic gram-positive bacteria.
    PMID: 19103220 [PubMed - as supplied by publisher] (Sou...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2065444</comments>
            <pubDate>Fri, 19 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2065444</guid>        </item>
        <item>
            <title>Detection of phenoloxidase activity in early stages of the Pacific oyster Crassostrea gigas (Thunberg).</title>
            <link>http://www.medworm.com/index.php?rid=2061193&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19101590%26dopt%3DAbstract</link>
            <description>This study demonstrated the selective response of PO-like activity by different elicitors and suggested that proPO-PO activating system, which is supposed to play an important function in non-self recognition and host immune reactions in oyster, is expressed early in the Pacific oyster, C. gigas.
    PMID: 19101590 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2061193</comments>
            <pubDate>Thu, 18 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2061193</guid>        </item>
        <item>
            <title>The role of crustins in Litopenaeus vannamei in response to infection with shrimp pathogens: An in vivo approach.</title>
            <link>http://www.medworm.com/index.php?rid=2061194&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19100764%26dopt%3DAbstract</link>
            <description>In this study, a reverse genetic approach was utilized to test the hypothesis that crustins are antimicrobial in vivo in response to bacterial and fungal challenge. Injection of double-stranded RNA specific to a 120-bp region of LvABP1, one of the most prominent crustin isoforms, yielded a significant reduction in the expression of both crustin mRNA and protein within the hemocytes. To test the role of crustins in the shrimp immune response, RNAi was first used to suppress crustin expression and animals were subsequently injected with low pathogenic doses of either Vibrio penaeicida or Fusarium oxysporum. A significant increase in mortality in crustin-depleted animals was observed in animals infected with V. penaeicida as compared to controls, whereas no significant change in shrimp mortal...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2061194</comments>
            <pubDate>Wed, 17 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2061194</guid>        </item>
        <item>
            <title>The in vitro and in ovo responses of chickens to TLR9 subfamily ligands.</title>
            <link>http://www.medworm.com/index.php?rid=2061195&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19100284%26dopt%3DAbstract</link>
            <description>In this study the response of chicken cells to the TLR9 subfamily of ligands was characterised in vitro and in ovo. It was found that even though chickens appear to have only one functional receptor to represent the TLR9 subfamily, stimulation of chicken splenocytes with TLR7 and TLR9 ligands induced proinflammatory cytokine production and cell proliferation, similar to that observed when the homologous mammalian receptors are stimulated. Furthermore, we demonstrated that the in ovo administration of these TLR ligands elicits a response, such as cytokine production, that can be detected post-hatch. The current knowledge of the action of TLR ligands in mammals, in conjunction with their immunomodulating ability shown in this study, draws attention to their potential use as therapeutic agent...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2061195</comments>
            <pubDate>Tue, 16 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2061195</guid>        </item>
        <item>
            <title>Alloantigen-specific killing is mediated by CD8-positive T cells in fish.</title>
            <link>http://www.medworm.com/index.php?rid=2047205&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19073209%26dopt%3DAbstract</link>
            <description>Authors: Toda H, Shibasaki Y, Koike T, Ohtani M, Takizawa F, Ototake M, Moritomo T, Nakanishi T
    CD8-positive (CD8(+)) cytotoxic T lymphocytes (CTL) have antigen-specific cytotoxic activity. In fish, however, CTL expressing CD8 on their cell surface have not been identified. In order to characterize the cells involved in specific cell-mediated cytotoxicity in teleosts, we separated and sorted ginbuna kidney leucocytes into CD8alpha(+), CD4(+) and surface IgM (sIgM)(+) cells by magnetic activated cell sorting using monoclonal antibodies and examined their cytotoxic activities. Effector donor ginbuna (OB1 clone) were sensitized by allografting scales from S3N clone fish followed by injection of an allogeneic cell line (CFS) derived from S3N fish. In cytotoxic assays, target cells were lab...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2047205</comments>
            <pubDate>Fri, 12 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2047205</guid>        </item>
        <item>
            <title>Characterization of two isoforms of Japanese spiny lobster Panulirus japonicus defensin cDNA.</title>
            <link>http://www.medworm.com/index.php?rid=2047204&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19073210%26dopt%3DAbstract</link>
            <description>In this study, cDNAs of two new isoforms of defensin (designated PJD1 and PJD2) from a Japanese spiny lobster Panulirus japonicus haemocytes cDNA library were cloned and sequenced. PJD1 and PJD2 consist of 656 and 673 nucleotides encoding putative proteins of 66 and 64 amino acids, respectively. The isoforms share 74.2% amino acid identity. In a phylogenetic analysis, the peptides clustered with vertebrate defensins and were closely mostly related to chicken beta-defensin. PJD1 and PJD2 were detected in all tissues examined including heart, nerves, intestine, haemocytes, gills and hepatopancreas.
    PMID: 19073210 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2047204</comments>
            <pubDate>Fri, 12 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2047204</guid>        </item>
        <item>
            <title>Antimicrobial activity-specific to Gram-negative bacteria and immune modulation-mediated NF-kappaB and Sp1 of a medaka beta-defensin.</title>
            <link>http://www.medworm.com/index.php?rid=2047203&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19084554%26dopt%3DAbstract</link>
            <description>In this study, we cloned a novel beta-defensin cDNA from medaka (Oryzias latipes) by rapid amplification of cDNA ends (RACE) technique. The full-length cDNA consists of 480bp, and the open reading frame (ORF) of 189bp encodes a polypeptide of 63 amino acids (aa) with a predicted molecular weight of 7.44kDa. Its genomic organization was analyzed, and Southern blot detection confirmed that only one copy of beta-defensin exists in the medaka HNI strain. RT-PCR, Western blot and immunohistochemistry detections showed that the beta-defensin transcript and protein could be detected in eyes, liver, kidney, blood, spleen and gill, and obviously prevalent expression was found in eyes. Antimicrobial activity of the medaka beta-defensin was evaluated, and the antibacterial activity-specific to Gram-n...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2047203</comments>
            <pubDate>Wed, 10 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2047203</guid>        </item>
        <item>
            <title>Development of macrophages of cyprinid fish.</title>
            <link>http://www.medworm.com/index.php?rid=2027425&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19063916%26dopt%3DAbstract</link>
            <description>Authors: Hanington PC, Tam J, Katzenback BA, Hitchen SJ, Barreda DR, Belosevic M
    The innate immune responses of early vertebrates, such as bony fishes, play a central role in host defence against infectious diseases and one of the most important effector cells of innate immunity are macrophages. In order for macrophages to be effective in host defence they must be present at all times in the tissues of their host and importantly, the host must be capable of rapidly increasing macrophage numbers during times of need. Hematopoiesis is a process of formation and development of mature blood cells, including macrophages. Hematopoiesis is controlled by soluble factors known as cytokines, that influence changes in transcription factors within the target cells, resulting in cell fate changes a...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2027425</comments>
            <pubDate>Fri, 05 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2027425</guid>        </item>
        <item>
            <title>An antiserum against Atlantic salmon IFNa1 detects IFN and neutralizes antiviral activity produced by poly I:C stimulated cells.</title>
            <link>http://www.medworm.com/index.php?rid=2027424&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19063917%26dopt%3DAbstract</link>
            <description>Authors: Berg K, Svingerud T, Sun B, Robertsen B
    Type I interferons (IFNs) play a crucial role in innate immune responses against virus infections in vertebrates. Two IFNs (IFNa1 and IFNa2) have previously been cloned from Atlantic salmon. In the present work a polyclonal antiserum, which was generated against salmon IFNa1 was used to study its production in cells by immunoblot detection and neutralization of antiviral activity. The antiserum was first confirmed to detect and neutralize the antiviral activity of recombinant salmon IFNa1 produced in HEK293 cells. The antiserum also detected IFNa1 and neutralized 95-98% of the antiviral activity in supernatants of poly I:C stimulated salmon TO cells. This suggests that IFNa1/IFNa2 are the major IFNs produced by poly I:C stimulated TO cel...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2027424</comments>
            <pubDate>Fri, 05 Dec 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2027424</guid>        </item>
        <item>
            <title>Isolation and functional characterization of neutrophil-like cells, from goldfish (Carassius auratus L.) kidney.</title>
            <link>http://www.medworm.com/index.php?rid=2011325&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19046985%26dopt%3DAbstract</link>
            <description>We report on the isolation, cultivation and characterization of neutrophil-like cells isolated from the goldfish kidney. Neutrophil-like cells stained positive for acid phosphatase and Sudan black, expressed MPO, and produced a dose-dependent respiratory burst response after stimulation with phorbol esters (PMA) and calciumionophore A23187 (CaI). Treatment of neutrophil-like cultures with PMA, CaI or zymosan induced a dose-dependent non-reversible degranulation of neutrophil-like cells. Goldfish neutrophil-like cells also exhibited a chemotactic response, degranulation, and respiratory burst response when exposed to the virulent fish pathogen, Aeromonas salmonicida A449.
    PMID: 19046985 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2011325</comments>
            <pubDate>Fri, 28 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2011325</guid>        </item>
        <item>
            <title>Marek's disease virus-induced expression of cytokine genes in feathers of genetically defined chickens.</title>
            <link>http://www.medworm.com/index.php?rid=2006086&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19041890%26dopt%3DAbstract</link>
            <description>Authors: Abdul-Careem MF, Read LR, Parvizi P, Thanthrige-Don N, Sharif S
    Marek's disease (MD) vaccines, although effective in reducing lymphoproliferation, cannot control infectious virus production in the feather follicle epithelium (FFE) which is the site of virus shedding. Therefore, we investigated Marek's disease virus (MDV) replication as well as the expression of cytokine genes in feathers of MDV-infected chickens belonging to genetically defined lines (N2a or B(21)/B(21) haplotype-resistant and P2a or B(19)/B(19) haplotype-susceptible). Though there was not a difference in MDV genome load and transcripts between feathers of these chicken lines at 4 and 10 days post-infection (d.p.i.), feathers of resistant chickens carried significantly lower viral genome load and transcripts a...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2006086</comments>
            <pubDate>Thu, 27 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2006086</guid>        </item>
        <item>
            <title>Tick subolesin is an ortholog of the akirins described in insects and vertebrates.</title>
            <link>http://www.medworm.com/index.php?rid=2006087&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19041667%26dopt%3DAbstract</link>
            <description>The objective of this research was to provide evidence of the sequence and functional homology between tick subolesin and akirins. The phylogenetic analysis of subolesin and akirins showed that they are evolutionary conserved. The effect of subolesin and akirin2 knockdown was compared in adult ticks and mice, respectively. The results demonstrated that tick subolesin is an ortholog of insect and vertebrate akirins and suggested that these proteins function in the regulation of NF-kappaB-dependent and independent expression of signal transduction and innate immune response genes. These results suggest that these proteins have an important role in host-pathogen interactions.
    PMID: 19041667 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2006087</comments>
            <pubDate>Wed, 26 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2006087</guid>        </item>
        <item>
            <title>Characterization of crustins from the hemocytes of the spider crab, Hyas araneus, and the red king crab, Paralithodes camtschaticus.</title>
            <link>http://www.medworm.com/index.php?rid=2006088&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19041340%26dopt%3DAbstract</link>
            <description>In this study, two crustin isoforms from Hyas araneus hemocytes were purified and tested for antimicrobial activity against selected microorganisms. They show both antibacterial and antifungal activity, with highest activity against the Gram-positive bacteria Corynebacterium glutamicum. Sequencing of the transcripts showed them to have a mature peptide of 90 amino acids and differing in three positions in the mature peptide. They were named CruHa1 and CruHa2. Real-time RT-PCR revealed that they mainly are expressed in hemocytes. Screening a cDNA library detected a crustin sequence in Paralithodes camtschaticus hemocytes, coding for a mature peptide of 98 amino acids. It was named CruPc. Based on phylogenetic inference and primary structure, CruHa1 and CruHa2 were placed within the Type I g...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=2006088</comments>
            <pubDate>Tue, 25 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">2006088</guid>        </item>
        <item>
            <title>Diverse splicing pathways of the membrane IgHM pre-mRNA in a Chondrostean, the Siberian sturgeon.</title>
            <link>http://www.medworm.com/index.php?rid=1991128&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19027787%26dopt%3DAbstract</link>
            <description>Authors: Lundqvist M, Str&amp;#xF6;mberg S, Bouchenot C, Pilstr&amp;#xF6;m L, Boudinot P
    Teleosts and tetrapods have evolved different splice patterns to generate their membrane-bound IgM. In the tetrapod lineage, the first transmembrane exon is spliced to an internal cryptic site located close to the end of the fourth constant exon. Because teleosts lack this site they use the regular 3'-splice site of the CH3 exon instead. We characterized the mum splicing patterns in a Chondrostean, the Siberian sturgeon. We observed a surprising diversity of splice patterns, the TM1 exon being spliced to a cryptic site at the end of CH4, to a cryptic site in CH3 or to the 3'-end of CH1. These different pathways lead to mIGHM transcripts encoding four, two or one complete C-domain(s), respectively. The shor...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1991128</comments>
            <pubDate>Thu, 20 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1991128</guid>        </item>
        <item>
            <title>Differential localization and bacteriostasis of Vibrio campbellii among tissues of the Eastern oyster, Crassostrea virginica.</title>
            <link>http://www.medworm.com/index.php?rid=1981068&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19022286%26dopt%3DAbstract</link>
            <description>In this study, Crassostrea virginica were injected in the adductor muscle with 10(5) live Vibrio campbellii. Major tissues were dissected at 10, 30, 60 or 120min postinjection (PI); in each tissue undegraded (intact) bacteria were quantified by real-time PCR and culturable bacteria by selective plating. At 10min PI, accumulation of bacteria varied among tissues from approximately 2.4x10(3) (labial palps, digestive gland) to 24.2x10(3) (gonads) intact Vibriog(-1). Neither distribution nor accumulation of intact bacteria changed with time except in the hemolymph. In most tissues, more than 80% of intact bacteria were culturable at 10min PI and culturability decreased with time. In contrast, only 19% of intact bacteria in gonadal tissue could be cultured at 10min PI, pointing to a major role ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1981068</comments>
            <pubDate>Mon, 17 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1981068</guid>        </item>
        <item>
            <title>A novel focal adhesion kinase from Marsupenaeus japonicus and its response to WSSV infection.</title>
            <link>http://www.medworm.com/index.php?rid=1969101&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19013481%26dopt%3DAbstract</link>
            <description>Authors: Zhang M, Wang H, Li D, Xu X
    Focal adhesion kinase (FAK) is a cytoplasmic protein-tyrosine kinase involved in integrin-mediated signal transduction which regulates multiple cell functions in mammalian cells. In contrast to the well document of FAK in mammalian cells, the properties of FAK in crustacean have not been reported yet and even none of their gene or protein sequences is known to date. Here, we report for the first time the cloning of FAK from Marsupenaeus japonicus (designated as MjFAK) and the identification of its involvement in the virus infection and host defense. Sequence analysis displayed that MjFAK shared strong similarity to FAK family protein-tyrosine kinase, including conserved tyrosine phosphorylation sites, PTK domain and FAT domain. Immunofluorescence st...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1969101</comments>
            <pubDate>Wed, 12 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1969101</guid>        </item>
        <item>
            <title>Development of reagents to study the turkey's immune response: Identification and molecular cloning of turkey CD4, CD8alpha and CD28.</title>
            <link>http://www.medworm.com/index.php?rid=1969105&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19013189%26dopt%3DAbstract</link>
            <description>Authors: Powell F, Lawson S, Rothwell L, Kaiser P
    The cDNAs of three turkey CD markers, CD4, CD8alpha and CD28, were identified by screening a turkey cDNA library. The coding regions of the chicken and turkey genes are highly conserved, with 91.3-96.1% nucleotide (nt) and 84.2-95.5% amino acid (aa) identity. Identity was less conserved between avian CD markers and their mammalian homologues, ranging from 44.7 to 59.8% and 22.4 to 50.4% at the nt and aa levels, respectively. Anti-chicken CD8alpha and CD28 monoclonal antibodies were demonstrated to specifically cross-react with turkey CD8alpha and CD28, respectively.
    PMID: 19013189 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1969105</comments>
            <pubDate>Tue, 11 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1969105</guid>        </item>
        <item>
            <title>Uncovering the evolutionary history of innate immunity: The simple metazoan Hydra uses epithelial cells for host defence.</title>
            <link>http://www.medworm.com/index.php?rid=1969104&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19013190%26dopt%3DAbstract</link>
            <description>Authors: Bosch TC, Augustin R, Anton-Erxleben F, Fraune S, Hemmrich G, Zill H, Rosenstiel P, Jacobs G, Schreiber S, Leippe M, Stanisak M, Gr&amp;#xF6;tzinger J, Jung S, Podschun R, Bartels J, Harder J, Schr&amp;#xF6;der JM
    Although many properties of the innate immune system are shared among multicellular animals, the evolutionary origin remains poorly understood. Here we characterize the innate immune system in Hydra, one of the simplest multicellular animals known. In the complete absence of both protective mechanical barriers and mobile phagocytes, Hydra's epithelium is remarkably well equipped with potent antimicrobial peptides to prevent pathogen infection. Induction of antimicrobial peptide production is mediated by the interaction of a leucine-rich repeats (LRRs) domain containing prote...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1969104</comments>
            <pubDate>Tue, 11 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1969104</guid>        </item>
        <item>
            <title>Cell surface expression of channel catfish leukocyte immune-type receptors (IpLITRs) and recruitment of both Src homology 2 domain-containing protein tyrosine phosphatase (SHP)-1 and SHP-2.</title>
            <link>http://www.medworm.com/index.php?rid=1969103&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19013191%26dopt%3DAbstract</link>
            <description>Authors: Montgomery BC, Mewes J, Davidson C, Burshtyn DN, Stafford JL
    Channel catfish leukocyte immune-type receptors (IpLITRs) are immunoglobulin superfamily (IgSF) members believed to play a role in the control and coordination of cellular immune responses in teleost. Putative stimulatory and inhibitory IpLITRs are co-expressed by different types of catfish immune cells (e.g. NK cells, T cells, B cells, and macrophages) but their signaling potential has not been determined. Following cationic polymer-mediated transfections into human cell lines we examined the surface expression, tyrosine phosphorylation, and phosphatase recruitment potential of two types of putative inhibitory IpLITRs using 'chimeric' expression constructs and an epitope-tagged 'native' IpLITR. We also cloned and ex...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1969103</comments>
            <pubDate>Tue, 11 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1969103</guid>        </item>
        <item>
            <title>Rainbow trout (Oncorhynchus mykiss) possess multiple novel immunoglobulin-like transcripts containing either an ITAM or ITIMs.</title>
            <link>http://www.medworm.com/index.php?rid=1969102&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19013192%26dopt%3DAbstract</link>
            <description>Authors: Ostergaard AE, Martin SA, Wang T, Stet RJ, Secombes CJ
    The recognition of pathogens by the innate immune system relies on a wide range of inhibitory and activating receptors. Some of these non-rearranging receptors belong to the immunoglobulin superfamily (IgSF) and in teleost fish the novel immune-type receptor (NITR) and the novel immunoglobulin-like transcript (NILT) have been reported. Here we describe the identification and characterisation of three new NILTs from rainbow trout (Oncorhynchus mykiss), with one NILT alternatively spliced into a long isoform containing two Ig domains and a short isoform containing one Ig domain. The cytoplasmic regions contain either immunoreceptor tyrosine-based inhibitory motifs (ITIMs) or an immunoreceptor tyrosine-based activating motif ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1969102</comments>
            <pubDate>Tue, 11 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1969102</guid>        </item>
        <item>
            <title>Differential antimicrobial peptide gene expression patterns during early chicken embryological development.</title>
            <link>http://www.medworm.com/index.php?rid=1964212&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19007808%26dopt%3DAbstract</link>
            <description>In this study, we demonstrate distinct expression patterns of innate immune genes including - Toll-like receptors (TLRs) (TLR2, TLR15 and TLR21, but not TLR4), the complete repertoire of AvBDs, CTHLs and both pro- and anti-inflammatory cytokines (IL1B, IL8, IFNG and IL10) during early chicken embryonic development. AvBD9 was significantly increased by over 150 fold at day 9; and AvBD10 was increased by over 100 fold at day 12 in the abdomen of the embryo, relative to day 3 expression levels (P&amp;lt;0.01). In contrast, AvBD14 was preferentially expressed in the head of the embryo. This is the first study to demonstrate differential patterns of AMP gene expression in the sterile environment of the developing embryo. Our results propose novel roles for AMPs during development and reveal the inn...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1964212</comments>
            <pubDate>Mon, 10 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1964212</guid>        </item>
        <item>
            <title>Identification of an Atlantic salmon IFN multigene cluster encoding three IFN subtypes with very different expression properties.</title>
            <link>http://www.medworm.com/index.php?rid=1964211&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19007809%26dopt%3DAbstract</link>
            <description>Authors: Sun B, Robertsen B, Wang Z, Liu B
    A cluster of 11 IFN genes was identified in the Atlantic salmon genome linked to the growth hormone 1 gene. The genes encode three different IFN subtypes; IFNa (2 genes), IFNb (four genes) and IFNc (five genes), which show 22-32% amino acid sequence identity. Expression of the fish IFNs were studied in head kidney, leukocytes or TO cells after stimulation with the dsRNA poly I:C or the imidazoquinoline S-27609. In mammals, poly I:C induces IFN-beta through the RIG-I/MDA5 or the TLR3 pathway, both of which are dependent on NF-kB. In contrast, S-27609 induces mammalian IFN-alpha in plasmacytoid dendritic cells through the TLR7 pathway independent of NF-kappaB. The presence of an NF-kappaB site in their promoters and their strong up-regulation by...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1964211</comments>
            <pubDate>Mon, 10 Nov 2008 05:00:00 +0100</pubDate>
            <guid isPermaLink="false">1964211</guid>        </item>
        <item>
            <title>Expression profiles of cytokines released in intestinal epithelial cells of the rainbow trout, Oncorhynchus mykiss, in response to bacterial infection.</title>
            <link>http://www.medworm.com/index.php?rid=1914871&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18952122%26dopt%3DAbstract</link>
            <description>Authors: Komatsu K, Tsutsui S, Hino K, Araki K, Yoshiura Y, Yamamoto A, Nakamura O, Watanabe T
    To determine whether fish intestinal epithelial cells (IECs) contribute to mucosal immunity, we established a method for isolating IECs from the rainbow trout Oncorhynchus mykiss and examined cytokine production in these cells. Components of the intestinal epithelium were released by incubation of intestinal pieces with 1mM dithiothreitol (DTT)/ethylenediamine tetraacetic acid (EDTA). The IEC-rich fraction (purity &amp;gt;90%; survival rate approximately 95%) was obtained by centrifugation on a 35%/40% Percoll gradient, followed by magnetic cell sorting using an anti-trout IgM antiserum. The gene expression profiles of 14 cytokines in trout IECs were investigated after culturing the cells for 6h ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1914871</comments>
            <pubDate>Thu, 23 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1914871</guid>        </item>
        <item>
            <title>Porcine DC-SIGN: Molecular cloning, gene structure, tissue distribution and binding characteristics.</title>
            <link>http://www.medworm.com/index.php?rid=1914872&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18951915%26dopt%3DAbstract</link>
            <description>Authors: Huang YW, Dryman BA, Li W, Meng XJ
    DC-SIGN, a human C-type lectin, is involved in the transmission of many enveloped viruses. Here we report the cloning and characterization of the cDNA and gene encoding porcine DC-SIGN (pDC-SIGN). The full-length pDC-SIGN cDNA encodes a type II transmembrane protein of 240 amino acids. Phylogenetic analysis revealed that pDC-SIGN, together with bovine, canis and equine DC-SIGN, are more closely related to mouse SIGNR7 and SIGNR8 than to human DC-SIGN. pDC-SIGN has the same gene structure as bovine, canis DC-SIGN and mouse SIGNR8 with eight exons. pDC-SIGN mRNA expression was detected in pig spleen, thymus, lymph node, lung, bone marrow and muscles. pDC-SIGN protein was found to express on the surface of monocyte-derived macrophages and dendri...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1914872</comments>
            <pubDate>Wed, 22 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1914872</guid>        </item>
        <item>
            <title>IrAM-An alpha(2)-macroglobulin from the hard tick Ixodes ricinus: Characterization and function in phagocytosis of a potential pathogen Chryseobacterium indologenes.</title>
            <link>http://www.medworm.com/index.php?rid=1907775&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18948134%26dopt%3DAbstract</link>
            <description>Authors: Buresova V, Hajdusek O, Franta Z, Sojka D, Kopacek P
    The universal protease inhibitors of the alpha(2)-macroglobulin (alpha(2)M) family are evolutionarily conserved constituents of innate immunity, presumably because they guard organisms against undesired proteolytic attacks of a different origin. Here, we determined the primary structure of alpha(2)-macroglobulin from the hard tick Ixodes ricinus (IrAM) by sequencing of overlapping PCR products. Predicted disulfide and glycosylation patterns, post-translational cleavage and alternative splicing within its 'bait region' demonstrate that IrAM is closely related to the alpha(2)-macroglobulin from the soft tick Ornithodoros moubata. The IrAM message is expressed in all tick developmental stages and tissues, except for the gut, an...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1907775</comments>
            <pubDate>Mon, 20 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1907775</guid>        </item>
        <item>
            <title>Domain inhibitory and bacteriostatic activities of the five-domain Kazal-type serine proteinase inhibitor from black tiger shrimp Penaeus monodon.</title>
            <link>http://www.medworm.com/index.php?rid=1895253&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18930077%26dopt%3DAbstract</link>
            <description>Authors: Donpudsa S, Tassanakajon A, Rimphanitchayakit V
    Serine proteinase inhibitors (SPIs) in multi-cellular organisms are important modulators of proteinase activities in various biological processes. A five-domain Kazal-type serine proteinase inhibitor SPIPm2 from the black tiger shrimp Penaeus monodon is presumably involved in innate immune response. The SPIPm2 with the domain P1 residues T, A, E, K and E was isolated from the hemocyte cDNA libraries and found to strongly inhibit subtilisin and elastase, and weakly inhibit trypsin. To unravel further the inhibitory activity of each domain, we subcloned, over-expressed and purified each individual SPI domain. Their inhibitory specificities against trypsin, subtilisin and elastase were determined. Domain 1 was found to be inactive. ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1895253</comments>
            <pubDate>Wed, 15 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1895253</guid>        </item>
        <item>
            <title>Ontogeny of innate and adaptive immune defense components in free-living tree swallows, Tachycineta bicolor.</title>
            <link>http://www.medworm.com/index.php?rid=1876304&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18848578%26dopt%3DAbstract</link>
            <description>Authors: Palacios MG, Cunnick JE, Vleck D, Vleck CM
    Little is known about the development of immune function in wild animals. We investigated the ontogeny of immune defense in a free-living bird, the tree swallow. We assessed total and differential leukocyte counts, natural antibodies, complement activity, in vivo skin swelling response, and in vitro lymphocyte proliferation and compared the levels of development between nestlings and young adults. We also assessed whether body condition explained variation in these immune components. We found some support for the prediction that innate defenses, which do not need to generate a broad repertoire of specific receptors, would reach adult levels earlier than adaptive defenses. In contrast, we found limited support for the prediction that a...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1876304</comments>
            <pubDate>Tue, 07 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1876304</guid>        </item>
        <item>
            <title>Differential cytokine mRNA expression in single lymphatic follicles of the calf ileal and jejunal Peyer's patches.</title>
            <link>http://www.medworm.com/index.php?rid=1870971&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18845180%26dopt%3DAbstract</link>
            <description>Authors: Yasuda M, Nasu T, Murakami T
    The ruminant gut-associated lymphoid tissues are broadly classified into ileal and jejunal Peyer's patches (PP). We isolated single lymphatic follicles from ileal and jejunal PP and examined mRNA expression of 13 cytokines using RT-PCR. Four patterns of differential expression were identified. In Pattern 1, the cytokines IL-7, IL-10, IL-12, and IL-18 were detected in all follicles of both ileal and jejunal PP. In Pattern 2, the cytokines IL-2, IL-4, and IL-13 were expressed in most jejunal PP follicles, but were undetectable in the ileal PP follicles. The cytokines characterizing Pattern 3 (IL-1beta, IFN-gamma, and IL-6) were detected in all follicles of the jejunal PP, but were differentially expressed in each follicle of ileal PP. In Pattern 4, t...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1870971</comments>
            <pubDate>Tue, 07 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1870971</guid>        </item>
        <item>
            <title>Identification and characterization of a chitinase-coding gene from Lamprey (Lampetra japonica) with a role in gonadal development and innate immunity.</title>
            <link>http://www.medworm.com/index.php?rid=1870970&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18845181%26dopt%3DAbstract</link>
            <description>We report here the identification and characterization of a chitinase-coding gene from the lamprey Lampetra japonica. The predicted amino acid sequence of the chitinase gene consisted of a typical catalytic domain and a peritrophin-A type chitin-binding domain. Real time RT-PCR analysis showed that the chitinase gene was expressed in various tissues of adult L. japonica, particularly in the liver, where a significant difference between male and female was observed during the pre-spawning period. A significant increase in expression was also observed in vivo following stimulation by bacteria or fungi. These findings seemed to suggest that in L. japonica, chitinase probably plays an important role in gonadal development as well as in innate immunity in response to invasion by microorganisms....</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1870970</comments>
            <pubDate>Tue, 07 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1870970</guid>        </item>
        <item>
            <title>Purification and characterization of silkworm hemocytes by flow cytometry.</title>
            <link>http://www.medworm.com/index.php?rid=1862951&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18840462%26dopt%3DAbstract</link>
            <description>Authors: Nakahara Y, Shimura S, Ueno C, Kanamori Y, Mita K, Kiuchi M, Kamimura M
    Hemocyte functions are well-investigated in the silkworm, Bombyx mori, however, detailed analysis of each hemocyte subset has been hampered by the lack of appropriate separation method. Here we use an array of flow cytometric analyses to characterize silkworm hemocytes with various molecular probes, such as propidium iodide, green fluorescence protein, monoclonal antibodies, and fluorescent lectins. Of these, separation using propidium iodide was the simplest and provided most reliable results for the isolation of the hemocyte subsets. cDNAs were then synthesized from these sorted populations and subset-specific gene expression was examined by RT-PCR. Granulocytes, plasmatocytes, and oenocytoids expressed ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1862951</comments>
            <pubDate>Sat, 04 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1862951</guid>        </item>
        <item>
            <title>Form, function and phylogenetics of NITRs in bony fish.</title>
            <link>http://www.medworm.com/index.php?rid=1862950&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18840463%26dopt%3DAbstract</link>
            <description>Authors: Yoder JA
    Novel immune-type receptors (NITRs) are encoded by clusters of multigene families and have been identified in multiple bony fish species. All NITRs possess one extracellular immunoglobulin (Ig) domain of the variable (V) type and recent crystal structures of NITR V domains demonstrate their high degree of similarity to V domains of antigen receptors. Many NITRs possess a second extracellular Ig domain of the intermediate (I) type which helps differentiate NITRs from other V domain receptors. The majority of NITRs are type I transmembrane receptors; however, a small number are predicted to encode secreted proteins. Based on their sequence and structure, NITRs have been proposed to be &quot;functional orthologs&quot; of mammalian natural killer receptors (NKRs). Like NKRs, most N...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1862950</comments>
            <pubDate>Sat, 04 Oct 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1862950</guid>        </item>
        <item>
            <title>Two prophenoloxidases are important for the survival of Vibrio harveyi challenged shrimp Penaeus monodon.</title>
            <link>http://www.medworm.com/index.php?rid=1856257&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18834900%26dopt%3DAbstract</link>
            <description>Authors: Amparyup P, Charoensapsri W, Tassanakajon A
    Phenoloxidase (PO) plays an important role in arthropod melanization. Previously, a prophenoloxidase (PmproPO1) gene was cloned and characterized from the hemocytes of the black tiger shrimp, Penaeus monodon. In the present study, we report a novel proPO gene (PmproPO2) belonging to the proPO family identified from the P. monodon EST database (http://pmonodon.biotec.or.th). The full-length sequence of PmproPO2 consists of 2513bp encoding a predicted 689 amino acid residues with a calculated molecular mass and pI of 79.21kDa and 6.69, respectively. It is predicted to possess all the expected features of proPO members, including two putative tyrosinase copper-binding motifs with six histidine residues and a thiol ester-like motif, shar...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1856257</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1856257</guid>        </item>
        <item>
            <title>Baseline circulating immunoglobulin G levels in managed collection and free-ranging bottlenose dolphins (Tursiops truncatus).</title>
            <link>http://www.medworm.com/index.php?rid=1856256&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18835295%26dopt%3DAbstract</link>
            <description>Authors: Ruiz CL, Nollens HH, Venn-Watson S, Green LG, Wells RS, Walsh MT, Nolan EC, McBain JF, Jacobson ER
    Serum immunoglobulin levels can be used as markers for immune status. However, tools to evaluate immune function and status of cetaceans under veterinary care have been limited, including the lack of an assay quantifying serum immunoglobulin G. Here, we report on the development of a validated competitive enzyme-labeled immunosorbent assays (cELISA) for the quantification of bottlenose dolphin (Tursiops truncatus) IgG. Using the cELISA, baseline serum IgG levels were established for two managed collections and one free-ranging dolphin population. Serum IgG levels ranged from 3.2 to &amp;gt;11.49mg/ml. Overall, free-ranging dolphins had higher serum IgG levels than managed collection ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1856256</comments>
            <pubDate>Tue, 30 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1856256</guid>        </item>
        <item>
            <title>Molecular characterization, expression and functional analysis of goldfish (Carassius aurutus L.) interferon gamma.</title>
            <link>http://www.medworm.com/index.php?rid=1852697&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18831986%26dopt%3DAbstract</link>
            <description>We report on the characterization and functional analysis of IFNgamma of the goldfish. Quantitative analysis indicated the highest expression of goldfish IFNgamma in the spleen, with lower expressions in brain, gill, kidney, heart, intestine and muscle. An increase in IFNgamma expression was observed in kidney leukocytes following stimulation with PHA, PolyI:C and during mixed leukocyte reaction. IFNgamma was expressed in different goldfish immune cell populations and this expression was upregulated in several of these populations following treatment of cells with recombinant goldfish TNFalpha-2. A recombinant form of goldfish IFNgamma (rgIFNgamma) was produced and functionally analyzed. The rgIFNgamma primed goldfish macrophages and neutrophils for enhanced respiratory burst responses and...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1852697</comments>
            <pubDate>Mon, 29 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1852697</guid>        </item>
        <item>
            <title>Defense system by mesenchyme cells in bipinnaria larvae of the starfish, Asterina pectinifera.</title>
            <link>http://www.medworm.com/index.php?rid=1844941&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18824193%26dopt%3DAbstract</link>
            <description>Authors: Furukawa R, Takahashi Y, Nakajima Y, Dan-Sohkawa M, Kaneko H
    Here we characterize starfish larval mesenchyme cells, in terms of not only their phagocytic behavior, but also their structural and functional properties as a defense system. Our study reveals the following: (1) most mesenchyme cells construct a dynamic network structure beneath the body wall; (2) mesenchyme cells phagocytically respond to almost all foreign materials and form syncytial aggregates to conceal relatively large amounts and large sizes of foreign material; (3) the morphologies of the syncytial aggregates differ from one another depending on the species and the surface configuration of the cellular foreign material; (4) no mesenchyme cells respond to live mesenchyme cells even though they phagocytose che...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1844941</comments>
            <pubDate>Fri, 26 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1844941</guid>        </item>
        <item>
            <title>Expression profiles of cloned channel catfish (Ictalurus punctatus) lymphoid cell lines and mixed lymphocyte cultures.</title>
            <link>http://www.medworm.com/index.php?rid=1844942&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18824023%26dopt%3DAbstract</link>
            <description>This study illustrates the utility of microarray analyses in profiling RNA expression patterns in catfish lymphoid cell lines and will serve as a platform for examining catfish immune responses following virus infection or poly [I:C] treatment.
    PMID: 18824023 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1844942</comments>
            <pubDate>Thu, 25 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1844942</guid>        </item>
        <item>
            <title>The immunogenic properties of protozoan glycosylphosphatidylinositol in the mosquito Anopheles gambiae.</title>
            <link>http://www.medworm.com/index.php?rid=1837374&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18822312%26dopt%3DAbstract</link>
            <description>This study allowed us to test the antigenic properties of protozoan glycosylphosphatidylinositol (GPI) on the mosquito immune system. We found that both P. falciparum GPI and T. gondii GPI induce the strong expression of several antimicrobial peptides following ingestion, and that as a result of the immune response against the GPIs, the number of eggs produced by the mosquito is reduced dramatically. Such effects have been associated with malaria infected mosquitoes, but never associated with a Plasmodium specific antigen. This study demonstrates that protozoan GPIs can be considered as protozoan specific immune elicitors in mosquitoes, and that P. falciparum GPI plays a critical role in the malaria parasite manipulation of the mosquito vector to facilitate its transmission.
    PMID: 1882...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1837374</comments>
            <pubDate>Tue, 23 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1837374</guid>        </item>
        <item>
            <title>The function of rhamnose-binding lectin in innate immunity by restricted binding to Gb3.</title>
            <link>http://www.medworm.com/index.php?rid=1826001&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18809432%26dopt%3DAbstract</link>
            <description>Authors: Watanabe Y, Tateno H, Nakamura-Tsuruta S, Kominami J, Hirabayashi J, Nakamura O, Watanabe T, Kamiya H, Naganuma T, Ogawa T, Naud&amp;#xE9; RJ, Muramoto K
    l-Rhamnose-binding lectins (RBLs) have been isolated from various kinds of fish and invertebrates and interact with various kinds of bacteria, suggesting RBLs are involved in various inflammatory reactions. We investigated the effect of RBLs from chum salmon (Oncorhynchus keta), named CSL1, 2 and 3, on the peritoneal macrophage cell line from rainbow trout (Oncorhynchus mykiss) (RTM5) and an established fibroblastic-like cell line derived from gonadal tissue of rainbow trout (RTG-2). CSLs were bound to the surface of RTM5 and RTG-2 cells and induced proinflammatory cytokines, including IL-1beta1, IL-1beta2, TNF-alpha1, TNF-alpha2...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1826001</comments>
            <pubDate>Fri, 19 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1826001</guid>        </item>
        <item>
            <title>Immunoglobulins, antibody repertoire and B cell development.</title>
            <link>http://www.medworm.com/index.php?rid=1815521&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18804488%26dopt%3DAbstract</link>
            <description>Authors: Butler JE, Zhao Y, Sinkora M, Wertz N, Kacskovics I
    Swine share with most placental mammals the same five antibody isotypes and same two light chain types. Loci encoding lambda, kappa and Ig heavy chains appear to be organized as they are in other mammals. Swine differ from rodents and primates, but are similar to rabbits in using a single VH family (VH3) to encode their variable heavy chain domain, but not the family used by cattle, another artiodactyl. Distinct from other hoofed mammals and rodents, Ckappa:Clambda usage resembles the 1:1 ratio seen in primates. Since IgG subclasses diversified after speciation, same name subclass homologs do not exist among swine and other mammals unless very closely related. Swine possess six putative IgG subclasses that appear to have dive...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1815521</comments>
            <pubDate>Wed, 17 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1815521</guid>        </item>
        <item>
            <title>Isolation and partial characterisation of four novel plasma lectins from the American lobster Homarus americanus.</title>
            <link>http://www.medworm.com/index.php?rid=1802846&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18793666%26dopt%3DAbstract</link>
            <description>Authors: Battison AL, Summerfield RL
    Although numerous haemolymph-derived crustacean lectins are described, few have been reported for the American lobster Homarus americanus. In the present study, affinity chromatography was used to isolate and partially describe the carbohydrate affinity of four new lectins from H. americanus plasma. HaMBP and HaDNABP were homodimers of approximately 30kDa subunits which bound to mannan- and DNA-agarose columns, respectively. These proteins had partially overlapping elution profiles, and both shared and unique amino acid sequences and fragmentation patterns after trypsin digestion. A third homodimer of approximately 29kDa subunits eluted with HaMBP and HaDNABP under certain conditions. HaNBP occurred as a monomer and dimer of approximately 40kDa subu...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1802846</comments>
            <pubDate>Fri, 12 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1802846</guid>        </item>
        <item>
            <title>Genes associated with an effective host response by Chinook salmon to Renibacterium salmoninarum.</title>
            <link>http://www.medworm.com/index.php?rid=1802845&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18793667%26dopt%3DAbstract</link>
            <description>Authors: Rhodes LD, Wallis S, Demlow SE
    An effective host response to Renibacterium salmoninarum, the etiologic agent of bacterial kidney disease, is poorly characterized. Using suppression subtractive hybridization, we exploited the difference in early host response in the pronephros of fish challenged by an attenuated strain (MT239) or a virulent strain (ATCC 33209) of R. salmoninarum. Among the 132 expressed sequence tag (EST) clones that were sequenced, 20 were selected for expression analysis at 24 and 72h after challenge. ESTs matching two interferon inducible genes (IFN-inducible GBP and VLIG1), the ligand GAS6, and the kinase VRK2 were upregulated in fish exposed to MT239, but downregulated or unchanged in fish exposed to 33209. A second group of ESTs matching genes involved in...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1802845</comments>
            <pubDate>Fri, 12 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1802845</guid>        </item>
        <item>
            <title>Evidence of high individual diversity on myticin C in mussel (Mytilus galloprovincialis).</title>
            <link>http://www.medworm.com/index.php?rid=1798326&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18789353%26dopt%3DAbstract</link>
            <description>Authors: Costa MM, Dios S, Alonso-Gutierrez J, Romero A, Novoa B, Figueras A
    Several antimicrobial peptides (AMP) have been described in Mytilus galloprovincialis. However, only in myticin C a high variability on the nucleotide sequence was detected. To determine the individual variability of this AMP, the myticin C present in more than 100 mussels was analyzed by Denaturing Gradient Gel Electrophoresis (DGGE). This technique helped us to describe a very high myticin C diversity as compared with a non-immune related gene such as the beta-actin. Moreover, each mussel showed a specific and exclusive myticin C band pattern. Our results showed that the individual sequences of myticin C are unique for each mussel, independently of their geographic origin, age, sex, gonad maturation stage or...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1798326</comments>
            <pubDate>Tue, 09 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1798326</guid>        </item>
        <item>
            <title>Maternal transfer of antibodies to eggs in Xenopus laevis.</title>
            <link>http://www.medworm.com/index.php?rid=1786080&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18782588%26dopt%3DAbstract</link>
            <description>Authors: Poorten TJ, Kuhn RE
    The immune system of the African clawed frog, Xenopus laevis, includes nearly the full repertoire of lymphoid organs and immune cell types found in mammals. In contrast to the mammalian immune system, the development of the amphibian immune system occurs in the open environment. Oviparity necessitates a rapid ontogeny of the immune system. X. laevis larvae become immunocompetent about 2 weeks after fertilization of the egg. During this 2-week window, larvae cannot mount an adaptive immune response to potential pathogens and presumably must depend on innate responses. In the present study, the possibility of maternal transfer of antibodies to eggs was examined. Adult female X. laevis were injected three times at weekly intervals with the hapten-carrier compl...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1786080</comments>
            <pubDate>Sat, 06 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1786080</guid>        </item>
        <item>
            <title>Structural and functional studies of an IRF-7-like gene from Atlantic salmon.</title>
            <link>http://www.medworm.com/index.php?rid=1782782&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18778729%26dopt%3DAbstract</link>
            <description>Authors: Kileng O, Bergan V, Workenhe ST, Robertsen B
    Interferon regulatory factor 7 (IRF-7) plays a crucial role in virus-induced activation of interferon-alpha/beta transcription in mammals. This work describes a structural and functional homologue of mammalian IRF-7 from Atlantic salmon. The cloned gene encodes a putative protein of 415 amino acids (aa), which groups with mammalian IRF-7 and other fish IRF-7-like proteins in a phylogenetic analysis of vertebrate IRFs. Using an IFN promoter-luciferase assay we showed that salmon IRF-7 gave increased promoter activity after poly I:C stimulation. Transcript levels of IRF-7 were measured by real-time RT-PCR and compared to those of signal transducer and activator of transcription 1 (STAT1), which is important for transcriptional activat...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1782782</comments>
            <pubDate>Fri, 05 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1782782</guid>        </item>
        <item>
            <title>A longitudinal study of the protein components of marsupial milk from birth to weaning in the tammar wallaby (Macropus eugenii).</title>
            <link>http://www.medworm.com/index.php?rid=1782781&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18778730%26dopt%3DAbstract</link>
            <description>Authors: Joss JL, Molloy MP, Hinds L, Deane E
    The major milk whey proteins of the tammar wallaby (Macropus eugenii) have been identified over the total period of lactation using proteomic analysis techniques comprising two-dimensional electrophoresis, comparative image analysis, matrix assisted laser desorption ionisation mass spectrometry (MALDI MS), de novo peptide sequencing and cross species protein matching. Samples were collected at the periods coinciding with major milestones of immunological development in the developing marsupial and in the four phases of milk production, specifically, Days 0, 5 (Phase 1); 27, 68 (Phase 2A); 137, 174 (Phase 2B) and 250 (Phase 3). Major changes in the protein content of marsupial milk whey correlated with the changing needs of the pouch young f...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1782781</comments>
            <pubDate>Fri, 05 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1782781</guid>        </item>
        <item>
            <title>Anatomical particularities of the porcine immune system-A physician's view.</title>
            <link>http://www.medworm.com/index.php?rid=1779434&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18775744%26dopt%3DAbstract</link>
            <description>Authors: Rothk&amp;#xF6;tter HJ
    In this article the anatomical structure of the porcine immune organs is described. The focus is on their particularities that are related to the use of pigs as an animal model. Key issues of the intrauterine development of the lymphoid organs are presented, such as the specific epithelio-chorial placenta, the appearance of the thymic tissue and the initial development of B cells. The role of the thymus for the development of alpha/beta and gamma/delta T cells and the location of tonsillar tissue in the naso-pharynx, in the oral cavity and at the basis of the tongue are described. The porcine spleen is of interest for surgical techniques to treat splenic trauma adequately. The observation of the inverted lymph node structure of pigs is puzzling and it remain...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779434</comments>
            <pubDate>Thu, 04 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1779434</guid>        </item>
        <item>
            <title>Dnr1-dependent regulation of the Drosophila immune deficiency signaling pathway.</title>
            <link>http://www.medworm.com/index.php?rid=1779433&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18775745%26dopt%3DAbstract</link>
            <description>Authors: Guntermann S, Primrose DA, Foley E
    Innate immunity is a critical metazoan defense strategy that rapidly detects and neutralizes invading microbes. As the signaling pathways that drive innate immune responses are evolutionarily conserved, there is considerable interest in the characterization of innate immune signaling in genetically tractable models, such as Drosophila melanogaster. Drosophila responds to detection of diamonopimelic-type microbial peptidoglycan through activation of the immune deficiency (Imd) pathway, a signaling pathway with numerous similarities to the mammalian pro-inflammatory TNF pathway. In this manuscript, we focus on a molecular and in vivo characterization of Dnr1, a putative regulator of Imd pathway activity. A previous cell culture RNAi screen indi...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779433</comments>
            <pubDate>Thu, 04 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1779433</guid>        </item>
        <item>
            <title>A novel prophenoloxidase 2 exists in shrimp hemocytes.</title>
            <link>http://www.medworm.com/index.php?rid=1779438&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18773916%26dopt%3DAbstract</link>
            <description>Authors: Ai HS, Liao JX, Huang XD, Yin ZX, Weng SP, Zhao ZY, Li SD, Yu XQ, He JG
    The prophenoloxidase (proPO)-activating system in crustaceans and other arthropods is regarded as a constituent of the immune system and plays an important role in defense against pathogens. Hitherto in crustaceans, only one proPO gene per species has been identified. Here we report the identification of a novel proPO-2 (LvproPO-2) from the hemocytes of Litopenaeus vannamei, which shows 72% identity to proPO-1 (LvproPO-1) cloned previously. Northern blotting analysis and quantitative real-time PCR reveal that LvproPO-2 is mainly expressed in the hemocytes, and its expression is down-regulated in shrimp challenged with white spot syndrome virus (WSSV). Western blotting analysis shows that most LvproPO-2/LvP...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779438</comments>
            <pubDate>Wed, 03 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1779438</guid>        </item>
        <item>
            <title>Induction of mucosal immunity in the avian Harderian gland with a replication-deficient Ad5 vector expressing avian influenza H5 hemagglutinin.</title>
            <link>http://www.medworm.com/index.php?rid=1779437&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18773917%26dopt%3DAbstract</link>
            <description>Authors: van Ginkel FW, Toro H, Tang DC, Gulley SL
    The chicken Harderian gland (HG) plays an important role in adaptive immune responses upon ocular exposure to avian pathogens such as avian influenza (AI). To determine the role of HGs in generating immunity, chickens were immunized ocularly with an adenovirus (Ad5) vector expressing the AI hemagglutinin H5 gene. The Ad5-H5 vector induced H5 transgene expression and induced H5- and Ad5-specific IgA and IgG spot-forming cells (SFCs) in the HGs. The IgA and IgG SFC peaked on day 9 for Ad5 and day 11 for the H5 protein. In addition, Ad5- and H5-specific antibodies were induced in serum. IgA in chicken tears was predominantly dimeric, while in serum monomeric IgA was most abundant. Analysis of HG mRNA confirmed expression of the polymeric ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779437</comments>
            <pubDate>Wed, 03 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1779437</guid>        </item>
        <item>
            <title>Production of monoclonal antibody specific for bottlenose dolphin neutrophils and its application to cell separation.</title>
            <link>http://www.medworm.com/index.php?rid=1779436&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18773918%26dopt%3DAbstract</link>
            <description>Authors: Kato M, Itou T, Nagatsuka N, Sakai T
    The authors produced a monoclonal antibody (mAb) against dolphin neutrophils by fusing mouse myeloma cells with lymph node cells from a Wistar rat immunized with bottlenose dolphin (Tursiops truncatus) polymorphonuclear leukocytes (PMNs). This mAb (DN1) was reactive against 77.1+/-8.6% of dolphin peripheral blood PMN by flow cytometric analysis; furthermore, there was no cross-reactivity with human or bovine leukocytes. The DN1-positive cells isolated with a sorting cytometer were almost all (99.7%) neutrophils. By using DN1 in conjunction with magnetic-activated cell sorting (MACS), the authors isolated neutrophils and eosinophils from density gradient-fractionated PMN with 100% and 95.6+/-4.8% purities, respectively. These results suggest...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779436</comments>
            <pubDate>Wed, 03 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1779436</guid>        </item>
        <item>
            <title>Age-dependent changes in porcine alveolar macrophage function during the postnatal period of alveolarization.</title>
            <link>http://www.medworm.com/index.php?rid=1779435&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18775449%26dopt%3DAbstract</link>
            <description>Authors: Dickie R, Tasat DR, Alanis EF, Delfosse V, Tsuda A
    During early postnatal ontogeny in most mammals, the lung is structurally and functionally immature. In some species with relatively altricial lung morphology, there is evidence of a coupling between functional maturity of the pulmonary cellular immune system and alveolar maturation. Herein, we examine changes in alveolar macrophage (AM) number and function occurring during alveolarization in a more precocial species, the pig, to determine if heightened oxidative metabolism and phagocytic ability is similarly delayed until completion of lung morphogenesis. We assessed cell differential in lavage fluid and evaluated two main functional parameters of AM phagocytic response, the generation of reactive oxygen species (ROS), and pa...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1779435</comments>
            <pubDate>Tue, 02 Sep 2008 04:00:00 +0100</pubDate>
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        <item>
            <title>Study of MHC class I peptide-binding motif of a Chinese chicken allele BF2*01sh for its binding of nonapeptide derived from the avian influenza virus.</title>
            <link>http://www.medworm.com/index.php?rid=1773286&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18771682%26dopt%3DAbstract</link>
            <description>Authors: Zhao H, Xia C, Luo Y
    In order to investigate a MHC class I peptide-binding motif of a Chinese chicken allele BF2*01sh, the BF2 gene was linked to the beta2m gene via a (G4S)3 linker by splicing overlap extension PCR (SOE-PCR). The recombinant BF2-linker-beta(2)m protein complex was purified by DEAE-Sepharose chromatography and its conformation was determined by circular dichroism (CD). It was further applied to bind nonapeptides derived from the hemagglutinins (HAs) of the avian influenza virus (AIV) H5N1 and H9N2 subtypes. The BF2-linker-beta(2)m associated peptides were detected by mass spectrometry (MS), the molecular weights and amino acid sequences of the peptides were confirmed by primary and secondary spectra, respectively. The BF*01sh haplotype is very common in Chines...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1773286</comments>
            <pubDate>Mon, 01 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1773286</guid>        </item>
        <item>
            <title>Targeting the porcine immune system-Particulate vaccines in the 21st century.</title>
            <link>http://www.medworm.com/index.php?rid=1773285&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18771683%26dopt%3DAbstract</link>
            <description>Authors: McCullough KC, Summerfield A
    During the last decade, the propagation of immunological knowledge describing the critical role of dendritic cells (DC) for in the induction of efficacious immune responses has promoted research and development of vaccines systematically targeting DC. Based on the promise for the rational design of vaccine platforms, the current review will provide an update on particle-based vaccines of both viral and synthetic origin giving examples of recombinant virus carriers such as adenoviruses and biodegradable particulate carriers. The viral carriers carry pathogen-associated molecular patterns (PAMP) used by the original virus for targeting DC and are particularly efficient and versatile gene delivery vectors. Efforts in the field of synthetic vaccine car...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1773285</comments>
            <pubDate>Mon, 01 Sep 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1773285</guid>        </item>
        <item>
            <title>Special issue on porcine immunology: An introduction from the guest editor.</title>
            <link>http://www.medworm.com/index.php?rid=1773284&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18771684%26dopt%3DAbstract</link>
            <description>Authors: Summerfield A
    
    PMID: 18771684 [PubMed - as supplied by publisher] (Source: Developmental and Comparative Immunology)</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1773284</comments>
            <pubDate>Mon, 01 Sep 2008 04:00:00 +0100</pubDate>
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        <item>
            <title>Stable expression in a Chinese hamster ovary (CHO) cell line of bioactive recombinant chelonianin, which plays an important role in protecting fish against pathogenic infection.</title>
            <link>http://www.medworm.com/index.php?rid=1764067&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18765249%26dopt%3DAbstract</link>
            <description>Authors: Chiou MJ, Chen LK, Peng KC, Pan CY, Lin TL, Chen JY
    Chelonianin, originally isolated from the shrimp (Penaeus monodon), exhibits antimicrobial effects in vitro and in vivo and is used to treat infectious fish diseases. Herein, we report that the recombinant chelonianin protein fused to a fluorescent protein (rcf protein) was expressed from a stably transfected Chinese hamster ovary (CHO) cells. The in vitro experiments showed that the rcf protein exhibited antimicrobial activity against several bacteria, while the recombinant fluorescent protein alone did not. In addition, pretreatment and post-treatment with the rcf protein were both effective in promoting a significant decrease in fish mortality and decreasing the number of infectious bacteria. We utilized the quantitative r...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1764067</comments>
            <pubDate>Sat, 30 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1764067</guid>        </item>
        <item>
            <title>Identification and molecular characterization of a complement C3 molecule in a lophotrochozoan, the Hawaiian bobtail squid Euprymna scolopes.</title>
            <link>http://www.medworm.com/index.php?rid=1764066&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18765250%26dopt%3DAbstract</link>
            <description>Authors: Castillo MG, Goodson MS, McFall-Ngai M
    Examination of the EST database of the light organ of the Hawaiian bobtail squid Euprymna scolopes revealed a sequence with similarity to complement C3. RACE yielded the full open reading frame of this protein. Analysis of the resultant sequence revealed that Es-C3 (E. scolopes-C3) has conserved residues and domains known to be critical for C3 function. The gene encoding C3 was expressed in all tissues tested, indicating that its expression is widely distributed throughout the animal's body. Immunocytochemistry using an antibody against Es-C3 revealed that the protein is produced principally in the apical surfaces of epithelial cells. The finding of the gene encoding C3 in this mollusk extends the occurrence of this molecule to the lophot...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1764066</comments>
            <pubDate>Sat, 30 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1764066</guid>        </item>
        <item>
            <title>The ontogeny of the porcine immune system.</title>
            <link>http://www.medworm.com/index.php?rid=1760083&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18762210%26dopt%3DAbstract</link>
            <description>Authors: Sinkora M, Butler JE
    Cellular and humoral aspects of the immune response develop sequentially in the fetus. During the ontogeny, the pluripotent stem cells emerge and differentiate into all hematopoietic lineages. Basic questions including the identification of the first lympho-hematopoietic sites, the origin of T and B lymphocytes, the development of different subpopulations of alphabeta T, gammadelta T and B lymphocytes as well as development of innate immunity and the acquisition of full immunological capacities are discussed here for swine and compared with other species. The description of related topics such as fertilization, morphogenesis, maternal-fetal-neonatal physiology and early neonatal development are also discussed.
    PMID: 18762210 [PubMed - as supplied by pu...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1760083</comments>
            <pubDate>Fri, 29 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1760083</guid>        </item>
        <item>
            <title>Subversion of complement by hematophagous parasites.</title>
            <link>http://www.medworm.com/index.php?rid=1760082&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18762211%26dopt%3DAbstract</link>
            <description>Authors: Schroeder H, Skelly P, Zipfel PF, Losson B, Vanderplasschen A
    The complement system is a crucial part of innate and adaptive immunity which exerts a significant evolutionary pressure on pathogens. It has selected not only for those pathogens, mainly microorganisms but also parasites, that have evolved countermeasures. The characterization of how pathogens evade complement attack is a rapidly developing field of current research. In recent years, multiple complement evasion strategies have been characterized. In this review, we focus on complement escape mechanisms expressed by hematophagous parasites, a heterogeneous group of metazoan parasites that share the property of ingesting the whole blood of their host. Complement inhibition is crucial for parasite survival within the ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1760082</comments>
            <pubDate>Fri, 29 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1760082</guid>        </item>
        <item>
            <title>Chicken CD14, unlike mammalian CD14, is trans-membrane rather than GPI-anchored.</title>
            <link>http://www.medworm.com/index.php?rid=1755004&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18761368%26dopt%3DAbstract</link>
            <description>Authors: Wu Z, Rothwell L, Hu T, Kaiser P
    A cDNA encoding the chicken homologue of the human myelomonocytic differentiation antigen, CD14, was cloned by RT-PCR from chicken bone marrow cell RNA, using oligonucleotide primers based on the predicted cDNA sequence. The cloned chicken CD14 (chCD14) cDNA encodes an open reading frame of 465 amino acids (aa), with 31-34% aa identity to mouse, bovine and human (hu) CD14. As in mouse and man, chCD14 is a leucine-rich protein. In mammals, CD14 is a GPI-anchored protein. Protein structure analysis suggested that chCD14, by contrast, was potentially a trans-membrane protein. The predicted aa sequence comprises an extracellular domain of 417aa, followed by a 23-aa trans-membrane segment, and a 25-aa intracytoplasmic region, the latter containing n...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1755004</comments>
            <pubDate>Thu, 28 Aug 2008 04:00:00 +0100</pubDate>
            <guid isPermaLink="false">1755004</guid>        </item>
        <item>
            <title>Gene structure and differential modulation of multiple rockbream (Oplegnathus fasciatus) hepcidin isoforms resulting from different biological stimulations.</title>
            <link>http://www.medworm.com/index.php?rid=1755003&amp;cid=s_35509_3_f&amp;fid=35509&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18761369%26dopt%3DAbstract</link>
            <description>In this study, four isoforms of hepcidin genes were characterized from a marine Perciform fish, rockbream (Oplegnathus fasciatus), and the transcriptional modulations of these isoforms in response to different biological stimulations were also examined. All rockbream hepcidin isoform genes exhibited a tripartite structure and their promoter regions displayed typical binding motifs for the transcription factors including C/EBP, HNF, AP, NF-kbeta, GATA, USF and/or STAT. Hepcidin transcripts in juvenile or fingerling tissues were dramatically induced during experimental challenges with various bacterial species, iron overload and rockbream iridovirus infection. The transcription of hepcidins was regulated in an isoform- and tissue-specific fashion. In addition, we identified for the first tim...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=1755003</comments>
            <pubDate>Thu, 28 Aug 2008 04:00:00 +0100</pubDate>
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