An EPD/WSD motifs containing C-type lectin from Argopectens irradians recognizes and binds microbes with broad spectrum. Issue 1 (March 2015)

• Record Type: Journal Article
• Authors: Huang, Mengmeng; Zhang, Huan; Jiang, Shuai; Wang, Lingling; Liu, Rui; Yi, Qilin; Song, Linsheng
• Is Part Of: Fish & shellfish immunology. Volume 43:Issue 1(2015:Mar.)
• Page Start: 287
• Page End: 293
• Publication Date: 2015-03
• Subjects: Fishes -- Immunology -- Periodicals; Shellfish -- Immunology -- Periodicals; Poissons -- Immunologie -- Périodiques; Crustacés -- Immunologie -- Périodiques; 571.9617
• DOI: 10.1016/j.fsi.2014.12.035
• Languages: English
• ISSNs: 1050-4648

Abstract

<abstract xml:lang="en" abstract-type="author" id="abs0010"> <title id="sectitle0010">Abstract</title> <sec> <p id="abspara0010">C-type lectins are a superfamily of Ca<sup>2+</sup>-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 <italic>Argopectens irradians</italic> 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 <italic>in vitro</italic>, and displayed a broader microbes binding spectrum towards Gram-positive bacteria <italic>Staphylococcus aureus</italic>, Gram-negative bacteria <italic>Escherichia coli</italic>, <italic>Vibrio anguillarum</italic>, as well as fungi <italic>Pichia pastoris</italic> and <italic>Yarrowia lipolytica</italic>. Moreover, it could also inhibit the growth of <italic>E. coli</italic> and significantly (<italic>P</italic> < 0.01) mediate the cell–cell adhesion <italic>in vitro</italic>. 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 Ca<sup>2+</sup> binding site 2 in CRDs endowed C-type lectins with comprehensive recognition spectrum and multiple immune functions against complex living environment.</p> </sec> </abstract>