Immune-related, lectin-like receptors are differentially expressed in the myeloid and lymphoid lineages of zebrafish

Department of Biology, University of South Florida, 4202 East Fowler Avenue, Tampa, FL 33620, USA.
Immunogenetics (Impact Factor: 2.23). 03/2006; 58(1):31-40. DOI: 10.1007/s00251-005-0064-3
Source: PubMed


The identification of C-type lectin (Group V) natural killer (NK) cell receptors in bony fish has remained elusive. Analyses of the Fugu rubripes genome database failed to identify Group V C-type lectin domains (Zelensky and Gready, BMC Genomics 5:51, 2004) suggesting that bony fish, in general, may lack such receptors. Numerous Group II C-type lectin receptors, which are structurally similar to Group V (NK) receptors, have been characterized in bony fish. By searching the zebrafish genome database we have identified a multi-gene family of Group II immune-related, lectin-like receptors (illrs) whose members possess inhibiting and/or activating signaling motifs typical of Group V NK receptors. Illr genes are differentially expressed in the myeloid and lymphoid lineages, suggesting that they may play important roles in the immune functions of multiple hematopoietic cell lineages.

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    • "To date, many fish CLR genes have been sequenced, such as a mannose receptor (MR) gene in seabream (Sparus aurata L.) [5] and grass carp (Ctenopharyngodon idella) [6], natural killer cell CLRs in Paralabidochromis chilotes and Nile tilapia (Oreochromis niloticus) [7], CLR-like protein A, B, and C genes in Atlantic salmon (Salmo salar) [8], immune-related, lectin-like receptor genes gene in zebrafish (Danio rerio) [9] [10], and a CLR-like protein gene in ayu (Plecoglossus altivelis) [11]. Fish CLRs have been reported to be involved in pathogen-associated molecular patterns (PAMPs) recognition, phagocytosis and clearance of bacteria by phagocytic cells [5e11]. "
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    ABSTRACT: C-type lectin-like receptors (CLRs) are important pathogen pattern recognition molecules that recognize carbohydrate structures. However, the functions of these receptors in fish keep less known. In this study, we characterized a novel CLR from a teleost fish, Plecoglossus altivelis (ayu), tentatively named PaCD209L. The cDNA of PaCD209L is 1464 nucleotides (nts) in length, encoding a polypeptide of 281 amino acid residues with a calculated molecular weight of 31.5 kDa. Multiple alignment of the deduced amino acid sequences of PaCD209L and other related fish CLRs revealed that the PaCD209L sequence had typical characteristics of fish CLRs, but without Ca(2+)-binding sites. Sequence comparison and phylogenetic tree analysis showed that PaCD209L shared the highest amino acid identity (44%) with rainbow trout (Oncorhynchus mykiss) CD209aE. PaCD209L transcripts were detected in all of the tissues examined, mainly expressed in the brain and heart. Upon Vibrio anguillarum infection, PaCD209L transcripts were upregulated in all tested tissues and in monocytes/macrophages (MO/MΦ). We prepared recombinant PaCD209L (rPaCD209L) by prokaryotic expression and raised antiserum against PaCD209L. Western blot analysis revealed that native PaCD209L was glycosylated, and its protein expression significantly increased in ayu MO/MΦ upon V. anguillarum infection. In addition, rPaCD209L was able to bind Gram-positive and Gram-negative bacteria in the absence of Ca(2+). After PaCD209L was blocked by anti-PaCD209L IgG, the phagocytosis and bacterial killing activity of MO/MΦ significantly decreased. These results suggest that PaCD209L plays an important role in the regulation of MO/MΦ functions in ayu. Copyright © 2015. Published by Elsevier Ltd.
    Fish &amp Shellfish Immunology 04/2015; 44(2). DOI:10.1016/j.fsi.2015.03.037 · 2.67 Impact Factor
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    • "A putative homolog for DC-SIGN has recently been proposed and is upregulated in immune-related tissues following infection by Aeromonas anguillarum [105]. Finally, putative homologs for the mammalian C-type lectin NK cell receptors have been identified in zebrafish and are differentially expressed on cells from the myeloid and lymphoid lineages [106]. "
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    ABSTRACT: The zebrafish has proven itself as an excellent model to study vertebrate innate immunity. It presents us with possibilities for in vivo imaging of host-pathogen interactions which are unparalleled in mammalian model systems. In addition, its suitability for genetic approaches is providing new insights on the mechanisms underlying the innate immune response. Here, we review the pattern recognition receptors that identify invading microbes, as well as the innate immune effector mechanisms that they activate in zebrafish embryos. We compare the current knowledge about these processes in mammalian models and zebrafish and discuss recent studies using zebrafish infection models that have advanced our general understanding of the innate immune system. Furthermore, we use transcriptome analysis of zebrafish infected with E. tarda, S. typhimurium, and M. marinum to visualize the gene expression profiles resulting from these infections. Our data illustrate that the two acute disease-causing pathogens, E. tarda and S. typhimurium, elicit a highly similar proinflammatory gene induction profile, while the chronic disease-causing pathogen, M. marinum, induces a weaker and delayed innate immune response.
    Advances in Hematology 07/2012; 2012(7):159807. DOI:10.1155/2012/159807
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    • "In addition to these considerations, the genomes of two species of bony fish, medaka and zebrafish, have been sufficiently resolved and adequately annotated to make possible the consideration of other gene families in the context of what we understand to be the general features of multigene families encoding the polymorphic NK receptors seen in higher vertebrates. Specifically, no compelling evidence exists for sequence orthologs of either KIRs or class V C-type lectin-related receptors (Zelensky and Gready, 2004; Panagos et al., 2008), members of which constitute MHC I receptors on human and mouse NK cells, respectively. "
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    ABSTRACT: Novel immune-type receptors (NITRs) comprise an exceptionally large, diversified family of activating and inhibitory receptors that has been identified in bony fish. Here, we characterized the structure of an activating NITR that is expressed by a cytotoxic natural killer (NK)-like cell line and that specifically binds an allogeneic B cell target. A single amino acid residue within the NITR immunoglobulin variable (V)-type domain accounts for specificity of the interaction. Structures solved by X-ray crystallography revealed that the V-type domains of NITRs form homodimers resembling rearranging antigen-binding receptor heterodimers. CDR1 elements of both subunits of NITR dimers form ligand-binding surfaces that determine specificity for the nonself target. In the evolution of immune function, it appears that a specific NK type of innate recognition may be mediated by a complex germline multigene family of V structures resembling those that are somatically diversified in adaptive immunological responses.
    Immunity 09/2008; 29(2):228-37. DOI:10.1016/j.immuni.2008.05.018 · 21.56 Impact Factor
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