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A C‐type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus
Author(s) -
Zhang XiaoWen,
Yang CongHui,
Zhang HongQuan,
Pan XinTong,
Jin ZeYu,
Zhang HongWei,
Xia XiaoHua
Publication year - 2020
Publication title -
journal of fish diseases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.819
H-Index - 85
eISSN - 1365-2761
pISSN - 0140-7775
DOI - 10.1111/jfd.13255
Subject(s) - misgurnus , biology , lectin , c type lectin , microbiology and biotechnology , recombinant dna , peptide , antimicrobial , bacteria , pathogen , immune system , antimicrobial peptides , biochemistry , gene , immunology , genetics , fishery , fish <actinopterygii>
Abstract C‐type lectins are carbohydrate‐binding proteins that play important roles in immunity by serving as pattern recognition receptors. In the present study, a novel nattectin‐like C‐type lectin was obtained from the weather loach, Misgurnus anguillicaudatus , designated as MaCTL. MaCTL encodes a peptide with 165 amino acids, with a signal peptide and a single C‐type lectin domain (CTLD), containing a galactose‐specific QPD motif and a conserved Ca 2+ ‐binding site. Transcripts of MaCTL were significantly upregulated after immune challenge with its pathogen A. hydrophila . In vitro assays with recombinant MaCTL protein revealed that it exhibited hemagglutinating and bacterial agglutinating activities, in a Ca 2+ ‐dependent manner. MaCTL was found to bind to a wide range of bacteria, as well as bind to bacterial polysaccharides LPS and PGN. Moreover, MaCTL displayed antimicrobial activity by inhibiting the growth of bacteria. These results collectively suggest that MaCTL is involved in the antibacterial defence of weather loach.