Identification and molecular analysis of a novel C-type lectin from Scophthalmus maximus

doi:10.1016/j.fsi.2010.02.023

IOCAS-IR > 实验海洋生物学重点实验室

	Identification and molecular analysis of a novel C-type lectin from Scophthalmus maximus
	Zhang, Min; Hu, Yong-hua; Sun, Li
	2010-07-01
发表期刊	FISH & SHELLFISH IMMUNOLOGY
ISSN	1050-4648
卷号	29 期号:1 页码:82-88
文章类型	Article
摘要	C-type lectins are calcium-dependent carbohydrate-binding proteins that play Important roles in innate immunity In this study, a C-type lectin homologue (SmLec1) was identified from turbot (Scophthalmus maximus) and analyzed at expression and functional levels. The open reading frame of SmLec1 is 504 bp, with a 5'-untranslated region (UTR) of 101 bp and a 3'-UTR of 164 bp The deduced amino acid sequence of SmLec1 shares 34%-38% overall identities with the C-type lectins of several fish species In silico analysis identified in SmLec1 conserved C-type lectin features, including a carbohydrate-recognition domain, four disulfide bond-forming cysteine residues, and the mannose-type carbohydrate-binding motif In addition, SmLec1 possesses a putative signal peptide sequence and is predicted to be localized in the extracellular. Expression of SmLec1 was highest in liver and responded positively to experimental challenges with fish pathogens Recombinant SmLec1 (rSmLec1) purified from yeast was able to agglutinate the Gram-negative fish pathogen Listonella anguillarum but not the Gram-positive pathogen Streptococcus uncle The agglutinating ability of rSmLec1 was abolished in the presence of mannose and ethylenediaminetetraacetic acid and by elevated temperature (65 degrees C) Further analysis showed that rSmLec1 could stimulate kidney lymphocyte proliferation and enhance the killing of bacterial pathogen by macrophages Taken together, these results suggest that SmLec1 is a unique mannose-binding C-type lectin that possesses apparent immunomodulating property and is likely to be involved in host defense against bacterial infection (C) 2010 Elsevier Ltd. All rights reserved; C-type lectins are calcium-dependent carbohydrate-binding proteins that play Important roles in innate immunity In this study, a C-type lectin homologue (SmLec1) was identified from turbot (Scophthalmus maximus) and analyzed at expression and functional levels. The open reading frame of SmLec1 is 504 bp, with a 5'-untranslated region (UTR) of 101 bp and a 3'-UTR of 164 bp The deduced amino acid sequence of SmLec1 shares 34%-38% overall identities with the C-type lectins of several fish species In silico analysis identified in SmLec1 conserved C-type lectin features, including a carbohydrate-recognition domain, four disulfide bond-forming cysteine residues, and the mannose-type carbohydrate-binding motif In addition, SmLec1 possesses a putative signal peptide sequence and is predicted to be localized in the extracellular. Expression of SmLec1 was highest in liver and responded positively to experimental challenges with fish pathogens Recombinant SmLec1 (rSmLec1) purified from yeast was able to agglutinate the Gram-negative fish pathogen Listonella anguillarum but not the Gram-positive pathogen Streptococcus uncle The agglutinating ability of rSmLec1 was abolished in the presence of mannose and ethylenediaminetetraacetic acid and by elevated temperature (65 degrees C) Further analysis showed that rSmLec1 could stimulate kidney lymphocyte proliferation and enhance the killing of bacterial pathogen by macrophages Taken together, these results suggest that SmLec1 is a unique mannose-binding C-type lectin that possesses apparent immunomodulating property and is likely to be involved in host defense against bacterial infection (C) 2010 Elsevier Ltd. All rights reserved
关键词	C-type Lectin Scophthalmus Maximus Immunity Agglutination Phagocytosis
学科领域	Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences
DOI	10.1016/j.fsi.2010.02.023
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000278649000009
引用统计	被引频次：50[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/337002/5980
专题	实验海洋生物学重点实验室
作者单位	Chinese Acad Sci, Inst Oceanol, Qingdao 266071, 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	Zhang, Min,Hu, Yong-hua,Sun, Li. Identification and molecular analysis of a novel C-type lectin from Scophthalmus maximus[J]. FISH & SHELLFISH IMMUNOLOGY,2010,29(1):82-88.
APA	Zhang, Min,Hu, Yong-hua,&Sun, Li.(2010).Identification and molecular analysis of a novel C-type lectin from Scophthalmus maximus.FISH & SHELLFISH IMMUNOLOGY,29(1),82-88.
MLA	Zhang, Min,et al."Identification and molecular analysis of a novel C-type lectin from Scophthalmus maximus".FISH & SHELLFISH IMMUNOLOGY 29.1(2010):82-88.

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-Identification（1045KB）			限制开放	--	浏览