A C-type lectin with antibacterial activity in weather loach, Misgurnus anguillicaudatus.
J Fish Dis
; 43(12): 1531-1539, 2020 Dec.
Article
em En
| MEDLINE
| ID: mdl-32924173
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 Ca2+ -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 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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Base de dados:
MEDLINE
Assunto principal:
Cipriniformes
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Lectinas Tipo C
/
Doenças dos Peixes
Limite:
Animals
Idioma:
En
Ano de publicação:
2020
Tipo de documento:
Article