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C‐type lectin from red swamp crayfish Procambarus clarkii participates in cellular immune response
Author(s) -
Zhang XiaoWen,
Wang XianWei,
Sun Chen,
Zhao XiaoFan,
Wang JinXing
Publication year - 2011
Publication title -
archives of insect biochemistry and physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.576
H-Index - 66
eISSN - 1520-6327
pISSN - 0739-4462
DOI - 10.1002/arch.20416
Subject(s) - biology , procambarus clarkii , c type lectin , lipoteichoic acid , microbiology and biotechnology , crayfish , peptidoglycan , hepatopancreas , white spot syndrome , vibrio anguillarum , lectin , bacteria , biochemistry , vibrio , staphylococcus aureus , cell wall , fishery , genetics , gene
Lectins are potential immune recognition proteins. In this study, a novel C‐type lectin ( Pc‐Lec1 ) is reported in freshwater crayfish Procambarus clarkii. Pc‐Lec1 encodes a protein of 163 amino acids with a putative signal peptide and a single carbohydrate recognition domain. It was constitutively expressed in various tissues of a normal crayfish, especially in the hepatopancreas and gills. Expressions of Pc‐Lec1 were up‐regulated in the hepatopancreas and gills of crayfish challenged with Vibrio anguillarum , Staphylococcus aureus , or the white spot syndrome virus. Recombinant mature Pc‐Lec1 bound bacteria and polysaccharides (peptidoglycan, lipoteichoic acid, and lipopolysaccharide) but did not agglutinate bacteria. Pc‐Lec1 enhanced hemocyte encapsulation of the sepharose beads in vitro, and the blocking of beads by a polyclonal antibody inhibited encapsulation. Pc‐Lec1 promoted clearance of V. anguillarum in vivo . These results suggest that Pc‐Lec1 is a pattern recognition receptor and participates in cellular immune response. Pc‐Lec1 performs its function as an opsonin by enhancing the encapsulation or clearance of pathogenic bacteria. © 2011 Wiley Periodicals, Inc.