A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains

doi:10.1016/j.fsi.2009.02.017

IOCAS-IR > 实验海洋生物学重点实验室

	A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains
	Zhang, Huan 1,2; Wang, Hao 1; Wang, Lingling 1; Song, Xiaoyan 3; Zhao, Jianmin 1; Qiu, Limei 1; Li, Ling 1,2; Cong, Ming 1; Song, Linsheng 1
	2009-05-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	26 期号:5 页码:707-715
文章类型	Article
摘要	C-type lectins are a superfamily of carbohydrate-recognition proteins which play crucial roles in the innate immunity. In this study, the gene of a C-type lectin with multiple carbohydrate-recognition domains (CRDs) from scallop Chlamys farreri (designated as Cflec-3) was cloned by rapid amplification of cDNA ends (RACE) approach based on expression sequence tag (EST) analysis. The full-length cDNA of Cflec-3 was of 2256 bp. The open reading frame encoded a polypeptide of 516 amino acids, including a signal sequence and three CRDs. The deduced amino acid sequence of Cflec-3 showed high similarity to members of C-type lectin superfamily. By fluorescent quantitative real-time PCR, the Cflec-3 mRNA was mainly detected in hepatopancreas, adductor, mantle, and marginally in gill, gonad and hemocytes of healthy scallops. After scallops were challenged by Listonella anguillarum, the mRNA level of Cflec-3 in hemocytes was up-regulated and was significantly higher than that of blank at 8 h and 12 h post-challenge. The function of Cflec-3 was investigated by recombination and expression of the cDNA fragment encoding its mature peptide in Escherichia coli BL21 (DE3)-pLysS. The recombined Cflec-3 (rCflec-3) agglutinated Gram-negative bacteria Pseudomonas stutzeri. The agglutinating activity was calcium-dependent and could be inhibited by D-mannose. These results collectively suggested that Cflec-3 was involved in the immune response against microbe infection and contributed to nonself-recognition and clearance of bacterial pathogens in scallop. (C) 2009 Elsevier Ltd. All rights reserved.; C-type lectins are a superfamily of carbohydrate-recognition proteins which play crucial roles in the innate immunity. In this study, the gene of a C-type lectin with multiple carbohydrate-recognition domains (CRDs) from scallop Chlamys farreri (designated as Cflec-3) was cloned by rapid amplification of cDNA ends (RACE) approach based on expression sequence tag (EST) analysis. The full-length cDNA of Cflec-3 was of 2256 bp. The open reading frame encoded a polypeptide of 516 amino acids, including a signal sequence and three CRDs. The deduced amino acid sequence of Cflec-3 showed high similarity to members of C-type lectin superfamily. By fluorescent quantitative real-time PCR, the Cflec-3 mRNA was mainly detected in hepatopancreas, adductor, mantle, and marginally in gill, gonad and hemocytes of healthy scallops. After scallops were challenged by Listonella anguillarum, the mRNA level of Cflec-3 in hemocytes was up-regulated and was significantly higher than that of blank at 8 h and 12 h post-challenge. The function of Cflec-3 was investigated by recombination and expression of the cDNA fragment encoding its mature peptide in Escherichia coli BL21 (DE3)-pLysS. The recombined Cflec-3 (rCflec-3) agglutinated Gram-negative bacteria Pseudomonas stutzeri. The agglutinating activity was calcium-dependent and could be inhibited by D-mannose. These results collectively suggested that Cflec-3 was involved in the immune response against microbe infection and contributed to nonself-recognition and clearance of bacterial pathogens in scallop. (C) 2009 Elsevier Ltd. All rights reserved.
关键词	Chlamys Farreri C-type Lectin Innate Immunity Bacterial Agglutination Recombinant Expression Real-time Rt-pcr
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2009.02.017
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000266659400005
引用统计	被引频次：61[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/337002/3068
专题	实验海洋生物学重点实验室
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.NW A&F Univ, Yangling 712100, Shaanxi, Peoples R China
第一作者单位	实验海洋生物学重点实验室
推荐引用方式 GB/T 7714	Zhang, Huan,Wang, Hao,Wang, Lingling,et al. A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains[J]. FISH & SHELLFISH IMMUNOLOGY,2009,26(5):707-715.
APA	Zhang, Huan.,Wang, Hao.,Wang, Lingling.,Song, Xiaoyan.,Zhao, Jianmin.,...&Song, Linsheng.(2009).A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains.FISH & SHELLFISH IMMUNOLOGY,26(5),707-715.
MLA	Zhang, Huan,et al."A novel C-type lectin (Cflec-3) from Chlamys farreri with three carbohydrate-recognition domains".FISH & SHELLFISH IMMUNOLOGY 26.5(2009):707-715.

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
zhang-A novel C-type（1902KB）			限制开放	--	浏览