A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri

doi:10.1016/j.fsi.2007.11.014

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	A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri
	Zheng, Peilin 1,2; Wang, Hao 1; Zhao, Jianmin 1; Song, Linsheng 1; Qiu, Limei 1; Dong, Chaohua 3; Wang, Bo 1,2; Gai, Yunchao 1,2; Mu, Changkao 1,2; Li, Chenghua 1; Ni, Duojiao 1; Xing, Kezhi 4
	2008-03-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	24 期号:3 页码:286-293
文章类型	Article
摘要	Lectins are a family of carbohydrate-recognition proteins which play crucial roles in innate immunity. In this study, a new lectin (CfLec-2) gene was cloned from Chlamys farreri by EST and RACE approaches. The full-length cDNA of CfLec-2 was composed of 708 bp, encoding a typical Long form carbohydrate-recognition domain of 130 residues. The deduced amino acid sequence showed high similarity to Brevican in Homo sapiens, C-type lectin-1 and lectin-2 in Anguilla japonica. The cDNA fragment encoding the mature peptide of CfLec-2 was recombined into plasmid pET-32a (+) and expressed in Escherichia coli Rosseta-Gami (DE3). The recombinant CfLec-2 (rCfLec-2) protein exhibited aggregative activity toward Staphylococcus haemolyticus, and the agglutination could be inhibited by D-mannose but not EDTA or D-galactose, indicating that CfLec-2 was a Ca2+ independent lectin. Moreover, rCfLec-2 could suppress the growth of E. coli TOP10F'. These results suggested that CfLec-2 was perhaps involved in the recognition and clearance of bacterial. pathogens in scallop. (C) 2007 Elsevier Ltd. All rights reserved.; Lectins are a family of carbohydrate-recognition proteins which play crucial roles in innate immunity. In this study, a new lectin (CfLec-2) gene was cloned from Chlamys farreri by EST and RACE approaches. The full-length cDNA of CfLec-2 was composed of 708 bp, encoding a typical Long form carbohydrate-recognition domain of 130 residues. The deduced amino acid sequence showed high similarity to Brevican in Homo sapiens, C-type lectin-1 and lectin-2 in Anguilla japonica. The cDNA fragment encoding the mature peptide of CfLec-2 was recombined into plasmid pET-32a (+) and expressed in Escherichia coli Rosseta-Gami (DE3). The recombinant CfLec-2 (rCfLec-2) protein exhibited aggregative activity toward Staphylococcus haemolyticus, and the agglutination could be inhibited by D-mannose but not EDTA or D-galactose, indicating that CfLec-2 was a Ca2+ independent lectin. Moreover, rCfLec-2 could suppress the growth of E. coli TOP10F'. These results suggested that CfLec-2 was perhaps involved in the recognition and clearance of bacterial. pathogens in scallop. (C) 2007 Elsevier Ltd. All rights reserved.
关键词	Chlamys Farreri Lectin Ca2++ Independent Staphylococcus Haemolyticus
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2007.11.014
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000254375200003
引用统计	被引频次：62[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/5762
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Ocean Univ China, Coll Marine Life Sci, Qingdao 266003, Peoples R China 4.Tianjin Agr Coll, Tianjin 300381, Peoples R China
第一作者单位	中国科学院海洋研究所
推荐引用方式 GB/T 7714	Zheng, Peilin,Wang, Hao,Zhao, Jianmin,et al. A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2008,24(3):286-293.
APA	Zheng, Peilin.,Wang, Hao.,Zhao, Jianmin.,Song, Linsheng.,Qiu, Limei.,...&Xing, Kezhi.(2008).A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,24(3),286-293.
MLA	Zheng, Peilin,et al."A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 24.3(2008):286-293.

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