An EPD/WSD motifs containing C-type lectin from Argopectens irradians recognizes and binds microbes with broad spectrum

被引:36
作者
Huang, Mengmeng [1 ,2 ]
Zhang, Huan [1 ]
Jiang, Shuai [1 ]
Wang, Lingling [1 ]
Liu, Rui [1 ]
Yi, Qilin [1 ,2 ]
Song, Linsheng [1 ]
机构
[1] Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
[2] Univ Chinese Acad Sci, Beijing 100049, Peoples R China
基金
美国国家科学基金会;
关键词
Argopectens irradians; C-type lectin; Innate immunity; PAMPs binding; Microbe binding ability; PATHOGEN RECOGNITION; CHLAMYS-FARRERI; PROTEIN; RECEPTORS; CFLEC-2; DOMAIN;
D O I
10.1016/j.fsi.2014.12.035
中图分类号
S9 [水产、渔业];
学科分类号
0908 ;
摘要
C-type lectins are a superfamily of Ca2+ -dependent carbohydrate-recognition proteins consisting of at least one carbohydrate-recognition domain (CRD), which play significant roles in nonself-recognition and clearance of invaders. The immune function of a C-type lectin (AiCTL-7) with EPD/WSD motifs from Argopectens irradians was investigated in the present study. The recombinant protein of AiCTL-7 (rAiCTL-7) could bind LPS, PGN, mannan, yeast glucan and poly I:C in vitro, and displayed a broader microbes binding spectrum towards Gram-positive bacteria Staphylococcus aureus, Gram-negative bacteria Escherichia coli, Vibrio anguillarum, as well as fungi Pichia pastoris and Yarrowia lipolytica. Moreover, it could also inhibit the growth of E. coli and significantly (P < 0.01) mediate the cell cell adhesion in vitro. The results clearly suggested that EPD/WSD motifs containing lectin AiCTL-7 could serve as PRR with wider recognition spectrum, and function both as collectin and selectin participating in the immunity against invaders in scallops. It could be inferred that the diversity and complexity of motifs in Ca2+ binding site 2 in CRDs endowed C-type lectins with comprehensive recognition spectrum and multiple immune functions against complex living environment. (C) 2015 Elsevier Ltd. All rights reserved.
引用
收藏
页码:287 / 293
页数:7
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