A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination

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	A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination
	Mu, Changkao 1,2; Song, Xiaoyan 2; Zhao, Jianmin 2; Wang, Lingling 2; Qiu, Limei 2; Zhang, Huan 2; Zhou, Zhi 2; Wang, Mengqiang2 ; Song, Linsheng 2; Wang, Chunlin 1
刊名	FISH & SHELLFISH IMMUNOLOGY
	2012-05-01
卷号	32 期号:5 页码:716-723
关键词	Argopecten irradians C-type lectin Agglutinating activity Ca2+-dependent
ISSN号	1050-4648
通讯作者	Wang, LL (reprint author), Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China.
英文摘要	C-type lectins are a family of calcium-dependent carbohydrate-binding proteins. In the present study, a C-type lectin (designated as AiCTL5) was identified and characterized from Argopecten irradians. The full-length cDNA of AiCTL5 was of 673 bp, containing a 5' untranslated region (UTR) of 24 bp, a 3' UTR of 130 bp with a poly (A) tail, and an open reading frame (ORF) of 519 bp encoding a polypeptide of 172 amino acids with a putative signal peptide of 17 amino acids. A C-type lectin-like domain (CRD) containing 6 conserved cysteines and a putative glycosylation sites were identified in the deduced amino acid sequence of AiCTL5. AiCTL5 shared 11%-27.5% identity with the previous reported C-type lectin from A. irradians. The cDNA fragment encoding the mature peptide of AiCTL5 was recombined into pET-21a (+) with a C-terminal hexa-histidine tag fused in-frame, and expressed in Escherichia coli Origami (DE3). The recombinant AiCTL5 (rAiCTL5) agglutinated Gram-negative E. coli TOP1OF' and Listonella anguillarum, but did not agglutinate Gram-positive bacteria Bacillus thuringiensis and Micrococcus luteus, and the agglutination could be inhibited by EDTA, indicating that AiCTL5 was a Ca2+-dependent lectin. rAiCTL5 exhibited a significantly strong activity to bind LPS from E. coli, which conformed to the agglutinating activity toward Gram-negative bacteria. Moreover, rAiCTL5 also agglutinated rabbit erythrocytes. These results indicated that AiCTL5 could function as a pattern recognition receptor to protect bay scallop from Gram-negative bacterial infection, and also provide evidence to understand the structural and functional diverse of lectin. (C) 2012 Elsevier Ltd. All rights reserved.
学科主题	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
收录类别	SCI
原文出处	10.1016/j.fsi.2012.01.020
语种	英语
WOS记录号	WOS:000302667200012
公开日期	2013-09-24
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/12268]
专题	海洋研究所_实验海洋生物学重点实验室
作者单位	1.Ningbo Univ, Sch Marine Sci, Ningbo 315211, Zhejiang, Peoples R China 2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
推荐引用方式 GB/T 7714	Mu, Changkao,Song, Xiaoyan,Zhao, Jianmin,et al. A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination[J]. FISH & SHELLFISH IMMUNOLOGY,2012,32(5):716-723.
APA	Mu, Changkao.,Song, Xiaoyan.,Zhao, Jianmin.,Wang, Lingling.,Qiu, Limei.,...&Wang, Chunlin.(2012).A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination.FISH & SHELLFISH IMMUNOLOGY,32(5),716-723.
MLA	Mu, Changkao,et al."A scallop C-type lectin from Argopecten irradians (AiCTL5) with activities of lipopolysaccharide binding and Gram-negative bacteria agglutination".FISH & SHELLFISH IMMUNOLOGY 32.5(2012):716-723.