期刊
JOURNAL OF FISH DISEASES
卷 43, 期 12, 页码 1531-1539出版社
WILEY
DOI: 10.1111/jfd.13255
关键词
agglutination; antimicrobial; C-type lectin; innate immunity; loach; pattern recognition receptor
资金
- Henan Institute of Sciences and Technology [208010618001]
- Henan Normal University [20180554]
- National Natural Science Foundation of China [31873047, 31902405]
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.MaCTLencodes 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 Ca2+-binding site. Transcripts ofMaCTLwere significantly upregulated after immune challenge with its pathogenA. hydrophila. In vitro assays with recombinant MaCTL protein revealed that it exhibited hemagglutinating and bacterial agglutinating activities, in a Ca2+-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.
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