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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. [ABSTRACT FROM AUTHOR]

C-type lectins (CTLs) play important roles in innate immune system of crustaceans as pattern recognition receptors (PRRs). In this study, a novel CTL gene was obtained from the red swamp crayfish, Procambarus clarkii , designated as PcLec. PcLec encodes a peptide with 175 amino acids, with a signal peptide and a single carbohydrate recognition domain (CRD). The PcLec transcripts were specifically expressed in crayfish stomach and were induced by bacterial challenge. In vitro assays with recombinant PcLec protein revealed that it had bacterial binding activity, polysaccharide binding activity, bacterial agglutination activity, and antimicrobial activity. Most importantly, PcLec knockdown significantly impaired the survivability of crayfish upon oral infection with its pathogen A. hydrophila. According to these results, we infer that the PcLec plays a crucial role in antibacterial defense of crayfish. • PcLec is stomach specific and responds to bacterial challenge. • PcLec has direct antimicrobial activity against both Gram+ and Gram-bacteria. • PcLec knockdown impaired the survivability of crayfish upon oral infection with bacteria. [ABSTRACT FROM AUTHOR]

Toll-like receptors (TLRs) play an important role in the activation of innate immune response in animals. In this study, we identified a TLR from the oriental river prawn, Macrobrachium nipponense (MnToll1) and investigated its functions in immunity. The MnToll1 protein shares similar structural characteristics with other known Toll family proteins. MnToll1 transcripts are broadly distributed in all of the examined tissues, and its expression level was significantly up-regulated by bacterial challenge. RNAi-mediated knockdown of MnToll1 significantly impaired the survivability of Vibrio -challenged prawns. RNAi experiments also revealed that the expression of several antimicrobial peptide genes were regulated by MnToll1. Moreover, we found the extracellular region of MnToll1 could directly bind to bacteria and bacterial glycoconjugates. These findings suggest that MnToll1 function as a pattern recognition receptor to recognize invading pathogen and initiate downstream gene expression, to participate in antibacterial defense of M. nipponense. • RNAi-mediated knockdown of MnToll1 significantly impaired the survivability of Vibrio -challenged prawns. • The expression of several antimicrobial peptide genes were regulated by MnToll1. • The extracellular region of MnToll1 could directly bind to bacteria and bacterial glycoconjugates. [ABSTRACT FROM AUTHOR]