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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>Sun, 21 Mar 2010 13:39:12 +0100</lastBuildDate>
        <item>
            <title>In vivo and in vitro post translational polymorphism of chicken natural auto-antibodies.</title>
            <link>http://www.medworm.com/index.php?rid=3374688&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%3D20230852%26dopt%3DAbstract</link>
            <description>Authors: Bergstra TJ, Smeets K, Nieuwland MG, Parmentier HK
    Natural antibodies (NAb) perform many important functions in various immune responses and are often polyreactive of nature with low binding affinity. Natural auto-antibodies (N(A)Ab) are NAb binding at least one auto-antigen. Polyreactivity of N(A)Ab has been proposed to rest on post-translational polymorphism of the immunoglobulin F(ab)(2) fragment caused by various locally present oxidizing agents, salts and lower or higher pH. Challenge with pathogen-associated molecular patterns (PAMP), such as lipopolysaccharide (LPS) or lipoteichoic acid (LTA), respectively, may underlie N(A)Ab polymorphism by the activation of inflammatory cells whose products affect the three-dimensional structure of N(A)Ab F(ab)(2) fragments. We evalu...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3374688</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3374688</guid>        </item>
        <item>
            <title>The residues 35proline and 41cysteine of chicken IL-2 are critical for binding to chicken CD25.</title>
            <link>http://www.medworm.com/index.php?rid=3374687&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%3D20230853%26dopt%3DAbstract</link>
            <description>In this study, we identified the critical amino acid residues of chicken IL-2 (chIL-2) for binding to chicken CD25 (chCD25) by an Ag-capture ELISA, screening of a phage display peptide library, peptide-competitive ELISA and an in vitro T-cell proliferation assay. Specific ligand elution of phage bound to chCD25 and chIL-2 suggested that the P(35)T(36)C(41)T(42)Q(43)L(46)Q(47)C(48)Y(49)L(50)G(51) motif within chIL-2 molecule interacts with the S(99)F(100)C(101)G(102)M(103)P(104)Q(105)T(106)V(107)P(108)S(111)L(112) motif of chCD25 molecule (chCD25(99-112)), whereas the peptide competition ELISA assay showed the residues (27)KIHLELYTPTETQEC(41) within chIL-2 (chIL-2(27-41)) bound to the chCD25 protein. Lymphocyte proliferation and inhibition assays further confirmed that the binding of chIL-2...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3374687</comments>
            <pubDate>Fri, 12 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3374687</guid>        </item>
        <item>
            <title>Differential cytokine expression in Chlamydophila psittaci genotype A-, B- or D-infected chicken macrophages after exposure to Escherichia coli O2:K1 LPS.</title>
            <link>http://www.medworm.com/index.php?rid=3362993&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%3D20223261%26dopt%3DAbstract</link>
            <description>Authors: Beeckman DS, Rothwell L, Kaiser P, Vanrompay DC
    Chlamydophila (Cp.) psittaci and avian pathogenic Escherichia (E.) coli infections contribute to the respiratory disease complex observed in turkeys. Secondary infection with E. coli exacerbates Cp. psittaci pathogenicity and augments E. coli excretion. The innate immune response initiated by both pathogens in their avian host is unknown. We therefore determined the cytokine responses following Cp. psittaci infection and E. coli superinfection of avian monocytes/macrophages by examining gene transcripts of IL-1beta, IL-6, CXCLi2 (IL-8), CXCLi1 (K60), IL-10, IL-12alpha/beta, IL-18, TGF-beta4 and CCLi2 at 4h post inoculation with different Cp. psittaci strains or 4h post treatment with avian E. coli LPS of Cp. psittaci pre-infected...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3362993</comments>
            <pubDate>Mon, 08 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3362993</guid>        </item>
        <item>
            <title>The C1q domain containing proteins: Where do they come from and what do they do?</title>
            <link>http://www.medworm.com/index.php?rid=3355199&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%3D20214925%26dopt%3DAbstract</link>
            <description>Authors: Carland TM, Gerwick L
    The gene sequence encoding an N-terminal collagen stalk followed by a globular complement 1q domain (gC1q), an architecture that characterizes the C1q A, B and C chains of the first complement component (C1), did not become prevalent until the cephalochordates and urochordates. However, genes encoding only the globular complement 1q domain (ghC1q) are more ancient as they exist within many lower vertebrate and invertebrate genomes, and are even present in the prokaryotes. These genes can be divided into two groups, the first, which appears to be the more ancient form, encodes proteins that are not secreted (cghC1q). The second group encodes proteins in which the globular domain is preceded by a signal peptide indicating secretion (sghC1q). In this review ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3355199</comments>
            <pubDate>Sat, 06 Mar 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3355199</guid>        </item>
        <item>
            <title>Flagellin expression enhances Salmonella accumulation in TLR5-positive macrophages.</title>
            <link>http://www.medworm.com/index.php?rid=3322898&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%3D20188752%26dopt%3DAbstract</link>
            <description>This study suggests that flagellin may be inducing TLR5-dependent internalisation mechanisms in Mcapital EF, Cyrillic which vary qualitatively between different species.
    PMID: 20188752 [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=3322898</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3322898</guid>        </item>
        <item>
            <title>Evolution of Thioester-Containing Proteins Revealed by Cloning and Characterization of Their Genes from a Cnidarian Sea Anemone, Haliplanella lineate.</title>
            <link>http://www.medworm.com/index.php?rid=3322897&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%3D20188753%26dopt%3DAbstract</link>
            <description>Authors: Fujito NT, Sugimoto S, Nonaka M
    To elucidate the evolutionary origin of genes encoding thioester-containing proteins (TEPs), TEP genes were isolated from a Cnidarian, a sea anemone, Haliplanella lineate. Phylogenetic tree analysis of the four identified Cnidarian TEP genes and various TEP genes of many Metazoa, indicated that they could be classified into two subfamilies: the alpha-2-macroglobulin (A2M) subfamily encodining A2M, CD109 and insect TEPs, and the C3 subfamily encoding complement C3, C4 and C5. Two of the four Cnidarian TEP genes belonged to the A2M subfamily, showing a close similarity to human A2M and CD109, respectively and thus were termed HaliA2M and HaliCD109. The other two genes belonged to the C3 subfamily, and were termed HaliC3-1 and HaliC3-2. Cnidarian T...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3322897</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3322897</guid>        </item>
        <item>
            <title>Characterization of porcine CD205.</title>
            <link>http://www.medworm.com/index.php?rid=3322896&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%3D20188754%26dopt%3DAbstract</link>
            <description>Authors: Flores-Mendoza L, Sotelo-Mundo RR, Dawson H, Mwangi W, Hern&amp;#xE1;ndez J
    Dendritic cells express a type cell-surface receptor, CD205 that plays a role in antigen capture and delivery to the endocytic pathway. Besides DCs, high CD205 expression is also detected on thymic epithelial cells but B cells, macrophages, and T cells have limited or no expression. CD205 has been characterized in several animal species except swine. The aim of this work was to characterize porcine CD205 and mRNA expression on different cells and tissues involved in immune responses. A complete porcine CD205 sequence of 5175bp was obtained from porcine thymus cDNA by PCR gene-walking strategy and this gene encoded a protein of 1723 amino acids. The multi-domain structure reported for murine, human, and bov...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3322896</comments>
            <pubDate>Wed, 24 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3322896</guid>        </item>
        <item>
            <title>Identification of new populations of chicken natural killer (NK) cells.</title>
            <link>http://www.medworm.com/index.php?rid=3322899&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%3D20188123%26dopt%3DAbstract</link>
            <description>In conclusion, we generated new monoclonal antibodies and developed two functional assays which will enhance our understanding of the role of NK cells in healthy and diseased chickens.
    PMID: 20188123 [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=3322899</comments>
            <pubDate>Tue, 23 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3322899</guid>        </item>
        <item>
            <title>Antigen-sampling cells in the salmonid intestinal epithelium.</title>
            <link>http://www.medworm.com/index.php?rid=3312365&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%3D20178814%26dopt%3DAbstract</link>
            <description>Authors: Fuglem B, Jirillo E, Bjerk&amp;#xE5;s I, Kiyono H, Nochi T, Yuki Y, Raida M, Fischer U, Koppang EO
    Antigen uptake has been shown to occur in the teleost intestine, but so far, limited information is available on the distribution and nature of cells involved in the process, and M cells, known for their antigen-sampling abilities in mammals, have not been identified. Here, different intestinal segments from salmonid fish were exposed to gold-BSA to identify antigen-sampling cells. Sections from exposed intestine were examined by light and electron microscopy. Uptake of gold-BSA was restricted to very few dendritic-like cells and to a limited number of epithelial cells located in the mucosal folds in the second segment of the mid intestine. Gold-positive epithelial cells displayed di...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3312365</comments>
            <pubDate>Sat, 20 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3312365</guid>        </item>
        <item>
            <title>Differential gene expression of gamma-Actin, Toll-Like Receptor 2 (TLR-2) and Interleukin 1 Receptor-Associated Kinase 4 (IRAK-4) in Mya arenaria haemocytes induced by in vivo infections with two Vibrio splendidus strains.</title>
            <link>http://www.medworm.com/index.php?rid=3280418&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%3D20156478%26dopt%3DAbstract</link>
            <description>Authors: Mateo DR, Greenwood SJ, Araya MT, Berthe FC, Johnson GR, Siah A
    Immune function gene expression in Mya arenaria haemocytes was evaluated following in vivo infection with Vibrio splendidus LGP32-GFP and 7SHRW. Elongation factor 1alpha (EF-1alpha) with 2 (EF-2), after challenge with LGP32-GFP, and EF-1alpha with the ribosomal protein S-18, after challenge with 7SHRW, were found to be the most stable housekeeping genes. Using these internal controls and comparing the regulation induced by both strains, up-regulation of gamma-actin, down-regulation of TLR-2 and up-regulation of IRAK-4 was significantly higher after challenge with LGP32-GFP (p&amp;lt;0.001, p=0.001 and p&amp;lt;0.05, respectively). These results suggest specific responses at a molecular level modulated by the bacterial str...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3280418</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3280418</guid>        </item>
        <item>
            <title>Identification of cytotoxic T lymphocyte-associated antigen-4 (CTLA-4) isoforms in the Pekin duck.</title>
            <link>http://www.medworm.com/index.php?rid=3280417&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%3D20156479%26dopt%3DAbstract</link>
            <description>Authors: Yao Q, Fischer KP, Motyka B, Ferland S, Li L, Tyrrell DL, Gutfreund KS
    Cytotoxic T lymphocyte-associated antigen-4 (CTLA-4, CD152) is an inhibitory T cell receptor predominately expressed on activated T cells. The duck CTLA-4 (DuCTLA-4) cDNA and a transcript lacking the predicted transmembrane encoding region (DuCTLA-4DeltaTM) were isolated from splenocytes using RT-PCR. The predicted DuCTLA-4 protein showed an identity of 92%, 49% and 47% with chicken, human and mouse homologues, respectively. Sequence comparison revealed conservation of residues implicated in the B7 ligand binding, disulfide linkages, glycosylation and intracellular signaling. DuCTLA-4 mRNA was predominately expressed in primary and secondary immune organs. DuCTLA-4 and DuCTLA-4DeltaTM transcripts were diffe...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3280417</comments>
            <pubDate>Fri, 12 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3280417</guid>        </item>
        <item>
            <title>Isolation, gene cloning and expression profile of a pathogen recognition protein: a serine proteinase homolog (Sp-SPH) involved in the antibacterial response in the crab Scylla paramamosain.</title>
            <link>http://www.medworm.com/index.php?rid=3280419&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%3D20153768%26dopt%3DAbstract</link>
            <description>Authors: Liu HP, Chen RY, Zhang M, Wang KJ
    To identify the frontline defense molecules against microbial infection in the crab Scylla paramamosain, a live crab pathogenic microbe, Vibrio parahaemolyticus, was recruited as an affinity matrix to isolate innate immune factors from crab hemocytes lysate. Interestingly, a serine proteinase homolog (Sp-SPH) was obtained together with an antimicrobial peptide-antilipopolysaccharide factor (Sp-ALF). We then determined the full length cDNA sequence of Sp-SPH, which contained 1298bp with an open reading frame of 1107bp encoding 369 amino acid residues. Multiple alignment analysis showed that the deduced amino acid sequences of Sp-SPH shared overall identity (83.8%) with those of SPH-containing proteins from other crab species. Tissue distributio...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3280419</comments>
            <pubDate>Thu, 11 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3280419</guid>        </item>
        <item>
            <title>A differential proteomics study of Caenorhabditis elegans infected with Aeromonas hydrophila.</title>
            <link>http://www.medworm.com/index.php?rid=3270162&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%3D20149819%26dopt%3DAbstract</link>
            <description>This study confirms the involvement of galectins, C-type lectins and lipid binding proteins in the immunity of C. elegans. In addition a number of unknown proteins, which might represent important players of the worm's defence system, were isolated and identified. This work gives a first indication of the complex changes that occur at the protein level during infection.
    PMID: 20149819 [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=3270162</comments>
            <pubDate>Mon, 08 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3270162</guid>        </item>
        <item>
            <title>Molecular characterization and expression of a crustin-like gene from Chinese mitten crab, Eriocheir sinensis.</title>
            <link>http://www.medworm.com/index.php?rid=3263448&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%3D20144896%26dopt%3DAbstract</link>
            <description>Authors: Mu C, Zheng P, Zhao J, Wang L, Zhang H, Qiu L, Gai Y, Song L
    Crustin is a cysteine rich antibacterial peptide which widely distributes within decapod crustaceans. In the present study, the cDNA encoding crustin-like peptide (designated CrusEs) was cloned from Chinese mitten crab Eriocheir sinensis by using and rapid amplification of cDNA ends (RACE) approaches and expressed sequence tag analysis. The full-length cDNA of CrusEs was of 796bp, containing a 5' untranslated region (UTR) of 214bp, a 3' UTR of 267bp with a poly (A) tail, and an open reading frame (ORF) of 315bp encoding a polypeptide of 104 amino acids including a putative signal peptide of 21 amino acids. A WAP domain and the consensus framework existing in class I crustins were both identified in CrusEs, suggesting...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3263448</comments>
            <pubDate>Sat, 06 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3263448</guid>        </item>
        <item>
            <title>Infection with the trypanosome Crithidia bombi and expression of immune-related genes in the bumblebee Bombus terrestris.</title>
            <link>http://www.medworm.com/index.php?rid=3263449&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%3D20144650%26dopt%3DAbstract</link>
            <description>Authors: Schl&amp;#xFC;ns H, Sadd BM, Schmid-Hempel P, Crozier RH
    Social bees and other insects are frequently parasitized by a large range of different microorganisms. Among these is Crithidia bombi (Kinetoplastida: Trypanosomatidae), a common gut parasite of bumblebees, Bombus spp. (Insecta: Apidae). Bumblebees are important pollinators in commercial and natural environments. There are clear detrimental effects of C. bombi infections on the fitness of bumblebees. However, little has been known about how the bee's immune system responds to infections with trypanosome parasites. Here, we study the immune response of B. terrestris on infection by C. bombi. We measured the expression of four immune-related genes (Hemomucin, MyD88, Relish, and TEP7) using RT-qPCR in adult B. terrestris worker...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3263449</comments>
            <pubDate>Fri, 05 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3263449</guid>        </item>
        <item>
            <title>Proteomic Analysis of Host Responses to Marek's Disease Virus Infection in Spleens of Genetically Resistant and Susceptible Chickens.</title>
            <link>http://www.medworm.com/index.php?rid=3255524&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%3D20138080%26dopt%3DAbstract</link>
            <description>Authors: Thanthrige-Don N, Parvizi P, Sarson AJ, Shack LA, Burgess SC, Sharif S
    Resistance to Marek's disease (MD) in chickens is genetically regulated and there are lines of chickens with differential susceptibility or resistance to this disease. The present study was designed to study comparative changes in the spleen proteomes of MD-susceptible B19 and MD-resistant B21 chickens in response to MDV infection. Spleen proteomes were examined at 4, 7, 14 and 21 days post-infection (d.p.i.) using two dimensional gel electrophoresis and subsequently the protein spots were identified by one dimensional liquid chromatography electrospray ionization tandem mass spectrometry (1D LC ESI MS/MS). On average, there were 520+/-27 distinct protein spots on each gel and 1.6+/-0.7% of the spots differ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3255524</comments>
            <pubDate>Tue, 02 Feb 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3255524</guid>        </item>
        <item>
            <title>Demonstration of T cell and macrophage progenitors in carp (Cyprinus carpio) kidney, hematopoietic tissues. Development of clonal assay system for carp hematopoietic cells.</title>
            <link>http://www.medworm.com/index.php?rid=3232042&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%3D20117130%26dopt%3DAbstract</link>
            <description>Authors: Katakura F, Yamaguchi T, Yoshida M, Moritomo T, Nakanishi T
    Single hematopoietic cells from carp (Cyprinus carpio) kidney were seeded to each well of 96-well plates and cultured in the presence of a supporting cell layer and conditioned media (CM). The CM were obtained from bulk cultured carp hematopoietic cells in which T and macrophage-lineage cells rapidly proliferated as previously reported. After 2-3 weeks, colony formation was found in 0 - 4 wells of each plate. Three different morphological types of colonies were observed, &quot;type I colonies&quot;, &quot;type II colonies&quot; and &quot;mixed type colonies&quot;. Type I colony cells were interpreted as composed by macrophage lineage cells, since they expressed a specific macrophage marker, M-CSFR/csf1r gene, and most of them phagocytosed latex pa...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3232042</comments>
            <pubDate>Thu, 28 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3232042</guid>        </item>
        <item>
            <title>Multiple forms of alpha-2 macroglobulin in shrimp Fenneropenaeus chinesis and their transcriptional response to WSSV or Vibrio pathogen infection.</title>
            <link>http://www.medworm.com/index.php?rid=3221179&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%3D20105438%26dopt%3DAbstract</link>
            <description>Authors: Ma H, Wang B, Zhang J, Li F, Xiang J
    Alpha-2 macroglobulin (A2M) is a non-specific protease inhibitor involved in host defense. By full length cloning and sequencing we identified three distinct cDNAs for A2M in Chinese shrimp Fenneropenaeus chinesis, designated FcA2M-1, FcA2M-2 and FcA2M-3, respectively. Expression profiles in normal tissues as well as tissues after challenge by white spot syndrome virus (WSSV) and Vibrio pathogen were conducted for FcA2M-1 and FcA2M-2. The FcA2M-1 and FcA2M-2 cDNAs encode proteins with 1501 or 1502 amino acids respectively, containing the typical conserved domain architecture of A2M. Similar to complement component C3, FcA2M-2 has a catalytic histidine, which may confer opsonic properties on this shrimp A2M. Six variants in the bait region w...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3221179</comments>
            <pubDate>Sun, 24 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3221179</guid>        </item>
        <item>
            <title>The cellular context of AID expressing cells in fish lymphoid tissues.</title>
            <link>http://www.medworm.com/index.php?rid=3221178&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%3D20105439%26dopt%3DAbstract</link>
            <description>Authors: Saunders HL, Oko AL, Scott AN, Fan CW, Magor BG
    It has long been held that the cold-blooded vertebrates lack mammalian-like germinal centers, though they do have affinity maturation and the immunoglobulin mutator activation-induced cytidine deaminase or AID. Using AID as a marker of sites of somatic hypermutation, we have identified discrete cell clusters of up to several thousand cells, in the spleen and kidney of channel catfish (Ictalurus punctatus), which may be primordial germinal centers. In situ hybridization revealed that AID expressing cells are interspersed or surrounded by a population of pigmented CSF1-R expressing cells called melano-macrophages. Significantly, melano-macrophages or associated reticular cells have been previously noted for their ability to retain ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3221178</comments>
            <pubDate>Sun, 24 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3221178</guid>        </item>
        <item>
            <title>Cockroach allergens Per a 3 are oligomers.</title>
            <link>http://www.medworm.com/index.php?rid=3213305&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%3D20100511%26dopt%3DAbstract</link>
            <description>Authors: Mindykowski B, Jaenicke E, Tenzer S, Cirak S, Schweikardt T, Schild H, Decker H
    Allergens from cockroaches cause major asthma-related health problems worldwide. Among them Pera3 belongs to the most potent allergens. Although the sequences of some members of the Pera3-family are known, their biochemical and biophysical properties have not been investigated. Here we present for the first time a thorough structural characterization of these allergens, which have recently been tested to induce an increase of allergy specific indicators in blood of Europeans. We isolated two Pera3-isoforms, which occur freely dissolved in the hemolymph as hexamers with molecular masses of 465+/-25kDa (PII) and 512+/-25kDa (P I). Their sedimentation coefficients (S(20,W)) were determined to be 17.4+...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3213305</comments>
            <pubDate>Fri, 22 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3213305</guid>        </item>
        <item>
            <title>Molecular strategies used by fish pathogens to interfere with host-programmed cell death.</title>
            <link>http://www.medworm.com/index.php?rid=3205354&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%3D20097221%26dopt%3DAbstract</link>
            <description>In this study, we will summarize the different molecular strategies displayed by major fish bacterial and viral pathogens to interfere with programmed cell death of the host as well as the relevance of cell death in the resolution of the infectious diseases caused by these pathogens.
    PMID: 20097221 [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=3205354</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3205354</guid>        </item>
        <item>
            <title>Identification and characterization of the parasitic wasp Nasonia defensins: positive selection targeting the functional region?</title>
            <link>http://www.medworm.com/index.php?rid=3205353&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%3D20097222%26dopt%3DAbstract</link>
            <description>Authors: Gao B, Zhu S
    Defensin is a crucial component of innate immunity highly conserved across different insect orders. Here, we report identification and characterization of defensins in the parasitic wasp Nasonia (Hymenoptera: Pteromalidae). In comparison with those in the non-parasitic insect Apis mellifera, two different subtypes of defensins (defensin1 and defensin2) have undergone independent gene duplication to create a mutigene family of five members (named 1-1, 1-2, 2-1, 2-2 and 2-3) in the Nasonia lineage. Such duplication occurred before the divergence of three sibling species (N. vitripennis, N. giraulti and N. longicornis) and the duplicated genes was subsequently subjected to positive selection at the amino-terminal loop and the gamma-core region. RT-PCR identified that...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3205353</comments>
            <pubDate>Thu, 21 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3205353</guid>        </item>
        <item>
            <title>Functional analysis of four processing products from multiple precursors encoded by a lebocin-related gene from Manduca sexta.</title>
            <link>http://www.medworm.com/index.php?rid=3205356&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%3D20096726%26dopt%3DAbstract</link>
            <description>Authors: Rayaprolu S, Wang Y, Kanost MR, Hartson S, Jiang H
    Antimicrobial peptides (AMPs) are a crucial component of the natural immune system in insects. Five types of AMPs have been identified in the tobacco hornworm Manduca sexta, including attacin, cecropin, moricin, gloverin, and lebocin. Here we report the isolation of lebocin-related cDNA clones and antibacterial activity of their processed protein products. The seventeen cDNA sequences are composed of a constant 5' end and a variable 3' region containing 3 approximately 16 copies of an 81-nucleotide repeat. The sequence of the corresponding gene isolated from a M. sexta genomic library and Southern blotting results indicated that the gene lacks introns and exists as a single copy in the genome. The genomic sequence contained 13...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3205356</comments>
            <pubDate>Wed, 20 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3205356</guid>        </item>
        <item>
            <title>Viral hemorrhagic septicemia and infectious pancreatic necrosis viruses replicate differently in rainbow trout gonad and induce different chemokine transcription profiles.</title>
            <link>http://www.medworm.com/index.php?rid=3205355&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%3D20096727%26dopt%3DAbstract</link>
            <description>Authors: Chaves-Pozo E, Montero J, Cuesta A, Tafalla C
    Viral haemorrhagic septicaemia virus (VHSV) and infectious pancreatic necrosis virus (IPNV) are two rainbow trout (Oncorhynchus mykiss) pathogens. While IPNV is known to be vertically transmitted to the next generation through the oocyte, VHSV is known to replicate in the ovary and be transmitted horizontally through the ovarian fluid. In this work, we wanted to study whether these differences had an effect on the immune response triggered in the ovary, with a focus on the chemokine response. We have studied the kinetics of viral gene expression and the sites of replication, confirming that great differences exist between the replication of the two viruses in the gonad. Next, we studied the levels of expression of several CXC and C...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3205355</comments>
            <pubDate>Wed, 20 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3205355</guid>        </item>
        <item>
            <title>Expression of antimicrobial peptides from Hyas araneus haemocytes following bacterial challenge in vitro.</title>
            <link>http://www.medworm.com/index.php?rid=3189629&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%3D20083137%26dopt%3DAbstract</link>
            <description>This study aims to establish primary cell cultures of the three main haemocyte types in Hyas araneus haemocytes, and to measure the in vitro expression of AMP genes in the cells following microbial challenge. The haemocyte populations were separated on Percoll gradients and cultured in modified L-15 media. Expression analysis by real-time RT-PCR showed that the granular cells are the main producers of crustin, hyastatin and arasin 1 AMPs, but the hyaline cells and semigranular cells also show some expression of these genes. Incubating the cell populations with Aerococcus viridans var. homari (a Gram-positive bacterium) or Listonella anguillarum (a Gram-negative pathogen) provoked no dramatic changes in the gene expression of any of the AMP, and although there was a small (single doubling) ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3189629</comments>
            <pubDate>Fri, 15 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3189629</guid>        </item>
        <item>
            <title>Assembled catalog of immune-related genes from allogeneic challenged corals that unveils the participation of vWF-like transcript.</title>
            <link>http://www.medworm.com/index.php?rid=3189630&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%3D20080125%26dopt%3DAbstract</link>
            <description>Authors: Oren M, Amar KO, Douek J, Rosenzwieg T, Paz G, Rinkevich B
    While reef-building corals portray highly complex and specific allorecognition responses, still, no available synthesis on historecognition at the molecular level exists for this group of organisms. Here, we present the first subtractive library of expressed sequence tags (ESTs) from allogeneic challenged coral (Stylophora pistillata) colonies revealing the differential expression of a wide range of immune-related genes. 1760 unique ESTs were clustered and assembled into 230 contigs and 1530 singlets with 28% that showed homology (E-value &amp;lt;/= 0.005) to known database sequences, of which 16% (n=80) homologues were identified as immune-relevant genes, encoding for stress proteins, pattern recognition receptors and com...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3189630</comments>
            <pubDate>Thu, 14 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3189630</guid>        </item>
        <item>
            <title>The Toll immune signaling pathway control conserved anti-dengue defenses across diverse Ae. aegypti strains and against multiple dengue virus serotypes.</title>
            <link>http://www.medworm.com/index.php?rid=3189631&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%3D20079370%26dopt%3DAbstract</link>
            <description>Authors: Ramirez JL, Dimopoulos G
    Dengue virus has become one of the most important arboviral pathogens affecting the world today. The virus is transmitted among humans by the mosquitoes Aedes aegypti and Ae. albopictus. Like other vector-borne pathogens, this virus encounters innate immune defenses within the mosquito vector that limit infection. We have previously demonstrated the involvement of the Toll pathway in the anti-dengue defense at 7 days after infection. In the present study, we have investigated the activity of this immune signaling pathway against different dengue virus serotypes at the early stages of infection in laboratory and field-derived mosquito strains. Our studies corroborate the importance of the Toll pathway in the anti-dengue defense repertoire at 3 days afte...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3189631</comments>
            <pubDate>Tue, 12 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3189631</guid>        </item>
        <item>
            <title>Identification of genes expressed in response to yellow head virus infection in the black tiger shrimp, Penaeus monodon, by suppression subtractive hybridization.</title>
            <link>http://www.medworm.com/index.php?rid=3172807&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%3D20067803%26dopt%3DAbstract</link>
            <description>Authors: Prapavorarat A, Pongsomboon S, Tassanakajon A
    Suppression subtractive hybridization (SSH) was employed to identify yellow head virus (YHV)-responsive genes from the hemocytes of the black tiger shrimp, Penaeus monodon. Two SSH cDNA libraries were constructed to identify viral responsive genes in the early (24I) and late (48/72I) phases of YHV infection. From 240 randomly selected clones from each library, 155 and 30 non-redundant transcripts were obtained for the early and late libraries, respectively. From these clones, 72 and 16, respectively, corresponded to known genes (E-values&amp;lt;1x10(-4)) that could be categorized according to their putative functions. The upregulated genes identified as likely to be associated with cell defense and homeostasis were found at a high prop...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172807</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172807</guid>        </item>
        <item>
            <title>Functional analysis of Rousettus aegyptiacus &quot;Signal Transducer and Activator of Transcription 1&quot; (STAT1).</title>
            <link>http://www.medworm.com/index.php?rid=3172806&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%3D20067804%26dopt%3DAbstract</link>
            <description>In this study, we focused on STAT1, one of the critical components in interferon (IFN)-signaling and antiviral activity, which is often targeted by viral proteins to reduce antiviral activity and increase viral replication. We found that Rousettus aegyptiacus STAT1 (bat STAT1) is phosphorylatable and translocates to the nucleus when stimulated with human IFN-alpha (hIFN-alpha). Furthermore, phosphorylation of bat STAT1 and inhibition of nuclear translocation was observed in IFN-stimulated cells infected with the HEP-Flury strain of rabies virus, in the same manner as in other mammals. Additionally, quantitative real-time RT-PCR revealed that bat STAT1 mRNA was highly expressed in the liver, while low in muscle and spleen.
    PMID: 20067804 [PubMed - as supplied by publisher] (Source: Deve...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172806</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172806</guid>        </item>
        <item>
            <title>Cloning of the sixth complement component and, spatial and temporal expression profile of MAC structural and regulatory genes in chicken.</title>
            <link>http://www.medworm.com/index.php?rid=3172805&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%3D20067805%26dopt%3DAbstract</link>
            <description>Authors: Mikrou A, Zarkadis IK
    Humoral cytotoxicity results from the assembly of terminal components of complement, called membrane attack complex (MAC), which lead to the formation of pores on pathogen membranes. The complement components involved in MAC formation are C5b, C6, C7, C8alpha, C8beta, C8gamma and C9. Among them, C6 protein interacts with C5b through a metastable binding site to form a soluble C5b-6 dimer in the vicinity of the activating cell. Formation of the MAC is controlled by complement regulatory molecules, such as CD59, vitronectin and clusterin. Here, we report the molecular characterization of the C6 complement component, as well as the spatial and temporal expression profile of MAC structural (C6, C7, C8alpha, C8beta, C8gamma) and regulatory (CD59, vitronectin a...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3172805</comments>
            <pubDate>Sat, 09 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3172805</guid>        </item>
        <item>
            <title>Identification and characterization of matrix metalloproteinase-13 sequence structure and expression during embryogenesis and infection in channel catfish (Ictalurus punctatus).</title>
            <link>http://www.medworm.com/index.php?rid=3164709&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%3D20060415%26dopt%3DAbstract</link>
            <description>The objective of this study was to characterize the MMP-13 gene in channel catfish, and to determine its pattern of expression in various healthy tissues and during embryogenesis. Since MMP-13 has been shown to have importance in tissue remodelling and some pathological processes, we further studied its involvement in the defense responses of catfish after bacterial infection. The channel catfish MMP-13 cDNA contains an open reading frame of 1416bp encoding 471 amino acids. Using RT-PCR analysis, MMP-13 was widely expressed in various health tissues. Using quantitative real-time PCR analysis, expression of MMP-13 gene was up-regulated by bacterial infection. During normal embryological development, MMP-13 expression was slightly increased in the first day post-fertilization and sharply up-...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3164709</comments>
            <pubDate>Thu, 07 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3164709</guid>        </item>
        <item>
            <title>Phylogeny, genomic organization and expression of lambda and kappa immunoglobulin light chain genes in a reptile, Anolis carolinensis.</title>
            <link>http://www.medworm.com/index.php?rid=3156705&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%3D20056120%26dopt%3DAbstract</link>
            <description>Authors: Wu Q, Wei Z, Yang Z, Wang T, Ren L, Hu X, Meng Q, Guo Y, Zhu Q, Robert J, Hammarstr&amp;#xF6;m L, Li N, Zhao Y
    The reptiles are the last major taxon of jawed vertebrates in which immunoglobulin light chain isotypes have not been well characterized. Using the recently released genome sequencing data, we show in this study that the reptile Anolis carolinensis expresses both lambda and kappa light chain genes. The genomic organization of both gene loci is structurally similar to their respective counterparts in mammals. The identified lambda locus contains three constant region genes each preceded by a joining gene segment, and a total of 37 variable gene segments. In contrast, the kappa locus contains only a single constant region gene, and two joining gene segments with a single fa...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3156705</comments>
            <pubDate>Mon, 04 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3156705</guid>        </item>
        <item>
            <title>Co-stimulation with TLR7/8 and TLR9 Agonists Induce Downregulation of Innate Immune Responses in Sheep Blood Mononuclear and B Cells.</title>
            <link>http://www.medworm.com/index.php?rid=3149551&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%3D20051250%26dopt%3DAbstract</link>
            <description>In this study, we investigated the effects of co-stimulation of sheep peripheral blood mononuclear cells (PBMC) and B cells with agonists for TLR3, 4, 7/8 and 9. Sheep PBMC stimulated with either CpG (TLR9 agonist) or RNA oligoribonucleotides ([ORN], TLR7/8 agonist) exhibited significant IL-12 production, but only CpG induced IFNalpha, IgM and proliferative responses. In contrast, poly(I:C) (TLR3 agonist) and LPS (TLR4 agonist) did not induce any of these responses. Interestingly, we observed that co-stimulation of PBMC with CpG+ORN or CpG+imiquimod (another TLR7/8 agonist) resulted in significant reduction in CpG-induced IFN-alpha production, B cell proliferation and IgM responses. Pre-incubation of cells with CpG prior to exposure of the cells to imiquimod resulted in similar inhibitory ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3149551</comments>
            <pubDate>Sat, 02 Jan 2010 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3149551</guid>        </item>
        <item>
            <title>Identification and functional characterization of a human sTRAIL homolog, CasTRAIL, in an invertebrate oyster Crassostrea ariakensis.</title>
            <link>http://www.medworm.com/index.php?rid=3143130&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%3D20045024%26dopt%3DAbstract</link>
            <description>Authors: Yang S, Wu X
    Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL/Apo2L) is one of the tumor necrosis factor (TNF) superfamily members, participating in many biological processes including apoptosis and immune responses. In present study, a novel human soluble TRAIL (sTRAIL) homolog, CasTRAIL was identified from the oyster, Crassostrea ariakensis. CasTRAIL has a 99% and 98% similarity to human sTRAIL over the cDNA sequence and the amino acid sequence, respectively. It mostly distributes in tissues of the oyster defense system and was mainly localized at cell membrane, and has no cytotoxicity to normal hemocytes of oyster. The phosphorylation state of MAP kinases revealed that CasTRAIL induced a rapid increase in the phospho-ERK and phospho-p38 levels, which indicated...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3143130</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3143130</guid>        </item>
        <item>
            <title>Polymorphism of the superoxide dismutase gene family in the bay scallop (Argopecten irradians) and its association with resistance/susceptibility to Vibrio anguillarum.</title>
            <link>http://www.medworm.com/index.php?rid=3143129&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%3D20045025%26dopt%3DAbstract</link>
            <description>Authors: Bao Y, Li L, Zhang G
    The superoxide dismutases (SODs) are a family of enzymes that function as the first line of antioxidant defense against highly reactive superoxide radicals. The bay scallop Argopecten irradians contains three unique superoxide dismutases: Ai-icCuZnSOD, Ai-MnSOD and Ai-ecCuZnSOD, which were characterized in our previous studies. qRT-PCR was also performed to characterize the temporal expression of SODs in the hemocytes of bay scallops injected with the bacterium Vibrio anguillarum. To characterize the SOD family in A. irradians completely, we evaluated the polymorphism in the SOD genes and investigated the association of this polymorphism with resistance/susceptibility to V. anguillarum. Fifty-nine SNPs were identified in the promoter, exon and partial intr...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3143129</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3143129</guid>        </item>
        <item>
            <title>Zebrafish larvae are unable to mount a protective antiviral response against waterborne infection by spring viremia of carp virus.</title>
            <link>http://www.medworm.com/index.php?rid=3143128&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%3D20045026%26dopt%3DAbstract</link>
            <description>ZEBRAFISH LARVAE ARE UNABLE TO MOUNT A PROTECTIVE ANTIVIRAL RESPONSE AGAINST WATERBORNE INFECTION BY SPRING VIREMIA OF CARP VIRUS.
    Dev Comp Immunol. 2009 Dec 29;
    Authors: L&amp;#xF3;pez-Mu&amp;#xF1;oz A, Roca FJ, Sepulcre MP, Meseguer J, Mulero V
    Interferons (IFNs) and their receptors exist in all classes of vertebrates, where they represent early elements in innate and adaptive immunity. Both types I and II IFNs have been discovered in fish and type I IFN has recently been classified into two groups based on their primary protein sequences and biological activities. Thus, although group I and II zebrafish IFN show powerful antiviral activities, only group I (IFNvarphi1) is able to protect the fish against bacterial infection. In addition, group II IFNs (IFNvarphi2 and IFNvarphi3) indu...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3143128</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3143128</guid>        </item>
        <item>
            <title>Epithelial induction of porcine suppressor of cytokine signaling 2 (SOCS2) gene expression in response to Entamoeba histolytica.</title>
            <link>http://www.medworm.com/index.php?rid=3143127&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%3D20045027%26dopt%3DAbstract</link>
            <description>Authors: Bruel T, Guibon R, Melo S, Guill&amp;#xE9;n N, Salmon H, Girard-Misguich F, Meurens F
    Suppressor of cytokine signaling (SOCS) proteins are key physiological regulators of both innate and adaptive immunity. These proteins belong to the three major classes of modulators of cytokines signalling. In the following article, we used porcine polarized intestinal cells to study early response to the protozoan, Entamoeba histolytica, and we identified by rapid amplification of cDNA ends (RACE) PCR porcine SOCS1, SOCS4, SOCS5 and SOCS6 encoding sequences. With more than 92% identity predicted porcine SOCS proteins are very similar to their human counterparts. Among SOCS transcripts, only SOCS2 mRNA was significantly induced in epithelial intestinal cells in response to the cytolytic activity...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3143127</comments>
            <pubDate>Tue, 29 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3143127</guid>        </item>
        <item>
            <title>Activation of immune-associated phospholipase A(2) is functionally linked to Toll/Imd signal pathways in the red flour beetle, Tribolium castaneum.</title>
            <link>http://www.medworm.com/index.php?rid=3137819&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%3D20043940%26dopt%3DAbstract</link>
            <description>This study set up a hypothesis that PLA(2) activation is linked to Toll and Imd pathways in T. castaneum. Bacterial challenge to the larvae of T. castaneum induced expressions of Toll and Imd genes. Different AMP genes were induced in larvae infected with Gram-positive or -negative bacteria. RNA interference using double-stranded RNAs (dsRNAs) specific to different Toll and Imd genes showed differential inhibition of these AMP expressions, indicating that the Toll and Imd pathways play critical roles in the production of AMPs by specifically responding to various bacterial challenges in T. castaneum. These Toll and Imd immune signals are also linked to the activation of PLA(2) in T. castaneum. Activation of PLA(2) was significantly induced in response to bacterial challenge, but was inhibi...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137819</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137819</guid>        </item>
        <item>
            <title>Effects of Cyclosporin A induced T-lymphocyte depletion on the course of Avian Metapneumovirus (aMPV) infection in turkeys.</title>
            <link>http://www.medworm.com/index.php?rid=3137818&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%3D20043941%26dopt%3DAbstract</link>
            <description>In this study we investigated the role of T-lymphocytes in aMPV-pathogenesis in a T-cell-suppression model in turkeys. T-cell-intact turkeys and turkeys partly depleted of functional CD4(+) and CD8(+) T-lymphocytes by Cyclosporin A (CsA) treatment were inoculated with the virulent aMPV subtype A strain BUT 8544. CsA-treatment resulted in a significant reduction of absolute numbers of circulating CD4(+) and CD8alpha(+) T- by up to 82 and 65%, respectively (P&amp;lt;0.05). Proportions of proliferating T-cells within mitogen-stimulated peripheral blood mononuclear cells were reduced by similar levels in CsA-treated birds compared to untreated controls (P&amp;lt;0.05). CsA-treated turkeys showed delayed recovery from aMPV-induced clinical signs and histopathological lesions and a prolonged detection o...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137818</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137818</guid>        </item>
        <item>
            <title>Identification of Key Cytosolic Kinases Containing Evolutionarily Conserved Kinase Tyrosine-based Inhibitory Motifs (KTIMs).</title>
            <link>http://www.medworm.com/index.php?rid=3137817&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%3D20043942%26dopt%3DAbstract</link>
            <description>Authors: Abu-Dayyeh I, Ralph B, Grayfer L, Belosevic M, Cousineau B, Olivier M
    We previously reported that SHP-1 regulates IRAK-1 activity by binding to an ITIM-like motif found within its kinase domain, which we named Kinase Tyrosine-based Inhibitory Motif (KTIM). Herein, we further investigated the presence, number, location, and evolutionary time of emergence of potential KTIMs in many cytosolic kinases, all known to play important roles in the signalling and function of immune cells. We unveil that several kinases contain potential KTIMs, mostly located within their kinase domain and appearing predominantly at the level of early vertebrates becoming highly conserved thereafter. Regarding the KTIMs that were found conserved in both vertebrates and invertebrates, we provide experimen...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3137817</comments>
            <pubDate>Mon, 28 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3137817</guid>        </item>
        <item>
            <title>Variation in expression of membrane IgM, CD21 (CR2) and CD32 (Fcgamma RIIB) on bovine lymphocytes with age: a longitudinal study.</title>
            <link>http://www.medworm.com/index.php?rid=3125421&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%3D20036278%26dopt%3DAbstract</link>
            <description>Authors: Chattha KS, Firth MA, Hodgins DC, Shewen PE
    Typically, neonatal calves have poor active antibody responses to vaccination, attributed to immaturity of the neonatal immune system and suppressive effects of maternal (colostral) antibodies. Responses of na&amp;#xEF;ve B cells are regulated by ligation of opposing activating (CD21, membrane IgM [mIgM]) and inhibitory (CD32) receptors. Expression of these receptors on blood lymphocytes of 15 calves, from birth to 6 months of age, was investigated by three-colour flow cytometry. Although the absolute number of mIgM(+) B lymphocytes was low in calves under 6 weeks, the intensity of mIgM expression per cell was significantly higher than for adults and &amp;gt;90% expressed both CD21 and CD32. The intensity of CD21 expression in calves did not...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3125421</comments>
            <pubDate>Wed, 23 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3125421</guid>        </item>
        <item>
            <title>Identification and expression analysis of the g-type and c-type lysozymes in grass carp Ctenopharyngodon idellus.</title>
            <link>http://www.medworm.com/index.php?rid=3123548&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%3D20034515%26dopt%3DAbstract</link>
            <description>Authors: Zhang L, Ye X, Tian Y, Tan A, Bai J, Li S
    Lysozyme is an important molecule of innate immune system for the defense against bacterial infections. We identified two genes encoding g-type and c-type lysozymes from grass carp Ctenopharyngodon idellus by the RACE method. The deduced amino acids of both lysozymes possessed typical structural residues and conserved catalytic sites similar to their counterparts across the species. In contrast, there was only 8.6% similarity of amino acid sequence between these two lysozymes. Phylogenetic analyses revealed that these two genes evolved at different rate. C-type lysozyme of grass carp was diverged early in the evolutionary history. Moreover, the expression patterns of these two genes differed. The mRNA levels of both genes were increase...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3123548</comments>
            <pubDate>Mon, 21 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3123548</guid>        </item>
        <item>
            <title>Isolation and characterization of chicken lung mesenchymal stromal cells and their susceptibility to avian influenza virus.</title>
            <link>http://www.medworm.com/index.php?rid=3115673&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%3D20026347%26dopt%3DAbstract</link>
            <description>In this study, we isolated and characterized mesenchymal stromal cells (MSCs) from the lungs of 1- to 2-week old chickens. Microscopically, the cultured cells showed fibroblast-like morphology. Phenotypically these cells expressed CD44, CD90, CD105 and the transcription factor PouV, which has been shown to be critical for stem cell self-renewal and pluripotency. The multipotency of chicken MSCs was demonstrated by their ability to undergo adipogenic and osteogenic differentiation. Like chicken bone marrow MSCs and mammalian MSCs, chicken lung MSCs had immunoregulatory activity and profoundly suppressed the proliferative capacity of T cells in response to a mitogenic stimulus. Next, we examined the susceptibility of these cells to H1N1 and H9N5 avian influenza (AI) viruses. The lung MSCs we...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3115673</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3115673</guid>        </item>
        <item>
            <title>In search of the origin of FREPs: Characterization of Aplysia californica fibrinogen-related proteins.</title>
            <link>http://www.medworm.com/index.php?rid=3115672&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%3D20026348%26dopt%3DAbstract</link>
            <description>Authors: Gorbushin AM, Panchin YV, Iakovleva NV
    All hemolymph lectins with uniquely juxtaposed N-terminal domain similar to the immunoglobulin superfamily (IgSF) and C-terminal fibrinogen (FBG) termed FBG-related proteins (FREP) are documented till now only in the pulmonate mollusc Biomphalaria glabrata. Using genomic WGS database we have found two FREP genes from marine opistobranch Aplysia californica named AcFREP1 and AcFREP2. The AcFREP1 and AcFREP2 mRNA molecules have been subsequently isolated from cDNA of sea hare larvae as well as adult mollusc tissues. These genes encode proteins (504 aa and 510 aa respectively) with domain architecture typical for FREPs with two N-terminal IgSF-domains and C-terminal FBG domain. Although cDNA sequences of AcFREP1 and AcFREP2 are 81% identical...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3115672</comments>
            <pubDate>Fri, 18 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3115672</guid>        </item>
        <item>
            <title>Mosquito immune defenses against Plasmodium infection.</title>
            <link>http://www.medworm.com/index.php?rid=3115674&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%3D20026176%26dopt%3DAbstract</link>
            <description>Authors: Cirimotich CM, Dong Y, Garver LS, Sim S, Dimopoulos G
    The causative agent of malaria, Plasmodium, has to undergo complex developmental transitions and survive attacks from the mosquito's innate immune system to achieve transmission from one host to another through the vector. Here we discuss recent findings on the role of the mosquito's innate immune signaling pathways in preventing infection by the Plasmodium parasite, the identification and mechanistic description of novel anti-parasite molecules, the role that natural bacteria harbored in the mosquito midgut might play in this immune defense, and the crucial parasite and vector molecules that mediate midgut infection.
    PMID: 20026176 [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=3115674</comments>
            <pubDate>Thu, 17 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3115674</guid>        </item>
        <item>
            <title>Structure and function of invertebrate Kazal-type serine proteinase inhibitors.</title>
            <link>http://www.medworm.com/index.php?rid=3076151&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%3D19995574%26dopt%3DAbstract</link>
            <description>Authors: Rimphanitchayakit V, Tassanakajon A
    Proteinases and proteinase inhibitors are involved in several biological and physiological processes in all multicellular organisms. The proteinase inhibitors function as modulators for controlling the extent of deleterious proteinase activity. The Kazal-type proteinase inhibitors (KPIs) in family I1 are among the well-known families of proteinase inhibitors, widely found in mammals, avian and a variety of invertebrates. Like those classical KPIs, the invertebrate KPIs can be single or multiple domain proteins containing one or more Kazal inhibitory domains linked together by peptide spacers of variable length. All invertebrate Kazal domains of about 40-60 amino acids in length share a common structure which is dictated by six conserved cyst...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3076151</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3076151</guid>        </item>
        <item>
            <title>Identification and characterization of multiple beta-glucan binding proteins in the Pacific oyster, Crassostrea gigas.</title>
            <link>http://www.medworm.com/index.php?rid=3076150&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%3D19995575%26dopt%3DAbstract</link>
            <description>Authors: Itoh N, Kamitaka R, Takahashi KG, Osada M
    The present study reports on the characterization of two cDNAs coding beta-glucan binding proteins (betaGBPs), designated as Cg-betaGBP-1 and Cg-betaGBP-2, from the Pacific oyster, Crassostrea gigas. Cg-betaGBP-1 consists of 555 amino acid residues and possesses two possible integrin recognition sites. The other protein, Cg-betaGBP-2, is composed of 447 amino acid residues without integrin recognition sites. Domain structures of both Cg-betaGBPs are similar to other invertebrate betaGBPs, but phylogenetic positions and major expression tissues for these proteins are different. Cg-betaGBP-1 is expressed in circulatory hemocytes and Cg-betaGBP-2 in digestive glands. Functional assays using recombinant proteins revealed that Cg-betaGBP-2 ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3076150</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3076150</guid>        </item>
        <item>
            <title>Identification of protein components of egg masses indicates parental investment in immunoprotection of offspring by Biomphalaria glabrata (Gastropoda, Mollusca).</title>
            <link>http://www.medworm.com/index.php?rid=3076149&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%3D19995576%26dopt%3DAbstract</link>
            <description>Authors: Hathaway JJ, Adema CM, Stout BA, Mobarak CD, Loker ES
    The macromolecules contributed by the freshwater gastropod Biomphalaria glabrata, intermediate host of Schistosoma mansoni, to developing offspring inside egg masses are poorly known. SDS-PAGE fractionated egg mass fluids (EMF) of M line and BB02 B. glabrata were analyzed by MALDI-TOF (MS and tandem MS). A MASCOT database was assembled with EST data from B. glabrata and other molluscs to aid in sequence characterization. Of approximately 20 major EMF polypeptides, 16 were identified as defense-related, including protease inhibitors, a hemocyanin-like factor and tyrosinase (each with possible phenoloxidase activity), extracellular Cu-Zn SOD, two categories of C-type lectins, Gram negative bacteria-binding protein (GNBP), apl...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3076149</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3076149</guid>        </item>
        <item>
            <title>Induction of interleukin-4 production in neonatal IgE(+) cells after crosslinking of maternal IgE.</title>
            <link>http://www.medworm.com/index.php?rid=3076148&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%3D19995577%26dopt%3DAbstract</link>
            <description>In conclusion, stimulation via maternal IgE antibodies mediated innate IL-4 production in neonatal basophils which might provide a paragenetic mechanism to promote the development of adaptive T-cell responses in the neonate after birth. (172 words).
    PMID: 19995577 [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=3076148</comments>
            <pubDate>Sat, 05 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3076148</guid>        </item>
        <item>
            <title>Protective immunity induced by CpG ODN against white spot syndrome virus (WSSV) via intermediation of virus replication indirectly in Litopenaeus vannamei.</title>
            <link>http://www.medworm.com/index.php?rid=3067847&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%3D19963004%26dopt%3DAbstract</link>
            <description>Authors: Zhang Y, Song L, Zhao J, Wang L, Kong P, Liu L, Wang M, Qiu L
    The worldwide shrimp culture is beset with diseases mainly caused by white spot syndrome virus (WSSV) and suffered huge economic losses, which bring out an urgent need to develop the novel strategies to better protect shrimps against WSSV. In the present study, CpG-rich plasmid pUC57-CpG, plasmid pUC57 and PBS were employed to pre-treat shrimps comparatively to evaluate the protective effects of CpG ODNs on shrimps against WSSV. The survival rates, WSSV copy numbers, and antiviral associated factors (Dicer, Argonaute, STAT and ROS) were detected in Litopenaeus vannamei. There were higher survival proportion, lower WSSV copy numbers, and higher mRNA expression of Dicer and STAT in pUC57-CpG-pretreatment shrimps than ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3067847</comments>
            <pubDate>Thu, 03 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3067847</guid>        </item>
        <item>
            <title>Two interleukin-17C-like genes exist in rainbow trout Oncorhynchus mykiss that are differentially expressed and modulated*</title>
            <link>http://www.medworm.com/index.php?rid=3067848&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%3D19961871%26dopt%3DAbstract</link>
            <description>Authors: Wang T, Martin SA, Secombes CJ
    Interleukin (IL)-17 family members (IL-17A-F) are key players in adaptive immune responses and have a central role in coordinating innate and adaptive immunity. Here, we report on two novel IL-17 homologues in rainbow trout Oncorhynchus mykiss, trout (t) IL-17C1 and tIL-17C2, that share 73.7% amino acid identity. The two tIL-17C-like molecules have relatively higher sequence identities to IL-17Cs from fish and mammals and the fish IL-17C-like molecules phylogenetically form a specific clade that groups with the mammalian IL-17C and IL-17E clades. However, the gene organisation of the fish IL-17C-like molecules is closer to mammalian IL-17Es than to IL-17Cs, and this taken together with other factors suggest the fish IL-17C-like genes may have ari...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3067848</comments>
            <pubDate>Tue, 01 Dec 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3067848</guid>        </item>
        <item>
            <title>Innate immunity and Gut-microbe mutualism in Drosophila.</title>
            <link>http://www.medworm.com/index.php?rid=3057528&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%3D19958789%26dopt%3DAbstract</link>
            <description>Authors: Ryu JH, Ha EM, Lee WJ
    Metazoan guts face a wide variety of microorganisms upon exposure to the environment, including beneficial symbionts, non-symbionts, food-borne microbes and life-threatening pathogens. Recent evidence has shown that the innate immunity of gut epithelia, such as antimicrobial peptide- and reactive oxygen species- based immune systems, actively participate in gut-microbe homeostasis by shaping the commensal community while efficiently eliminating unwanted bacteria. Therefore, elucidation of the regulatory mechanism by which gut innate immunity occurs at the molecular level will provide a novel perspective of gut-microbe mutualisms as well as of gut diseases caused by alterations in the innate immunity.
    PMID: 19958789 [PubMed - as supplied by publisher] ...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3057528</comments>
            <pubDate>Mon, 30 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3057528</guid>        </item>
        <item>
            <title>Cloning of and Functional Characterization of Chicken Stem Cell Antigen 2.</title>
            <link>http://www.medworm.com/index.php?rid=3044717&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%3D19945479%26dopt%3DAbstract</link>
            <description>Authors: Mao W, Hunt HD, Cheng HH
    Stem cell antigen 2 (SCA2) is a Ly-6 family member whose function is largely unknown. To characterize biological properties and tissue distribution of chicken SCA2, SCA2 was expressed in E. coli, purified, and a polyclonal antibody developed. Utilizing the polyclonal antibody, SCA2 is a 13 kDa cell surface protein anchored by a glycosyl-phosphatidylinositol (GPI) moiety. SCA2 is expressed in connective tissues of thymus and bursa based on immunohistochemistry, immunoprecipitation, and western blots. In bursal follicles, SCA2 is specifically expressed on the cortical-medullary epithelial cells (CMEC) surrounded by MHC class II presenting cells. Expression profiles of bursal cells induced by contact with SCA2-expressing cells shows down-regulation of num...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3044717</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3044717</guid>        </item>
        <item>
            <title>Regional and global changes in TCRalphabeta T cell repertoires in the gut are dependent upon the complexity of the enteric microflora.</title>
            <link>http://www.medworm.com/index.php?rid=3044716&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%3D19945480%26dopt%3DAbstract</link>
            <description>Authors: Mwangi WN, Beal RK, Powers C, Wu X, Humphrey T, Watson M, Bailey M, Friedman A, Smith AL
    The repertoire of gut associated T cells is shaped by exposure to microbes, including the natural enteric microflora. Previous studies compared the repertoire of gut associated T cell populations in germ-free (GF) and conventional mammals often focussing on intra-epithelial lymphocyte compartments. Using GF, conventional and monocolonised (gnotobiotic) chickens and chicken TCRbeta-repertoire analysis techniques, we determined the influence of microbial status on global and regional enteric TCRbeta repertoires. The gut of conventionally reared chickens exhibited non-Gaussian distributions of CDR3 lengths with some shared over-represented peaks in neighbouring gut segments. Sequence analysis...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3044716</comments>
            <pubDate>Thu, 26 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3044716</guid>        </item>
        <item>
            <title>Expression of zebrafish cxcl8 (Interleukin-8) and its receptors during development and in response to immune stimulation.</title>
            <link>http://www.medworm.com/index.php?rid=3037194&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%3D19941893%26dopt%3DAbstract</link>
            <description>Authors: Oehlers SH, Flores MV, Hall CJ, O'Toole R, Swift S, Crosier KE, Crosier PS
    Cxcl8 is a pro-inflammatory chemokine, best known for its role in neutrophil chemotaxis. Signalling through its receptors, Cxcr1 and Cxcr2, is induced by inflammatory stimuli evoked by microbial, chemical or environmental stress, and hormonal signals. While it is recognised that Cxcl8 signalling is active in the gut mucosa, this is not as well understood as its role in leukocyte trafficking. Here, we report the characterisation of genes encoding the zebrafish Cxcl8, Cxcr1 and Cxcr2. By a combination of genomic, expression and functional analyses, we show that the Cxcl8 signalling pathway is conserved in zebrafish. As in humans, cxcl8 is expressed in zebrafish leukocytes. Transcripts were also detected i...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3037194</comments>
            <pubDate>Mon, 23 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3037194</guid>        </item>
        <item>
            <title>Comparison of Global Transcriptional Responses To Primary and Secondary Eimeria acervulina Infections in Chickens.</title>
            <link>http://www.medworm.com/index.php?rid=3037193&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%3D19941894%26dopt%3DAbstract</link>
            <description>Authors: Kim CH, Lillehoj HS, Hong YH, Keeler CL, Lillehoj EP
    In the current study, we compared chicken gene transcriptional profiles following primary and secondary infections with Eimeria acervulina using a 9.6K avian intestinal intraepithelial lymphocyte cDNA microarray (AVIELA). Gene Ontology analysis showed that primary infection significantly modulated the levels of mRNAs for genes involved in the metabolism of lipids and carbohydrates as well as those for innate immune-related genes. By contrast, secondary infection increased the levels of transcripts encoded by genes related to humoral immunity and reduced the levels of transcripts for the innate immune-related genes. Because the observed modulation in transcript levels for gene related to energy metabolism and immunity occurre...</description>
            <author>Developmental and Comparative Immunology</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3037193</comments>
            <pubDate>Mon, 23 Nov 2009 00:00:00 +0100</pubDate>
            <guid isPermaLink="false">3037193</guid>        </item>
        <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>
            <guid isPermaLink="false">3004330</guid>        </item>
        <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>
            <guid isPermaLink="false">2891083</guid>        </item>
        <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>
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