C-Type Lectin in Chlamys farreri (CfLec-1) Mediating Immune Recognition and Opsonization

doi:10.1371/journal.pone.0017089

IOCAS-IR > 实验海洋生物学重点实验室

	C-Type Lectin in Chlamys farreri (CfLec-1) Mediating Immune Recognition and Opsonization
	Yang, Jialong 1,2; Wang, Lingling 1; Zhang, Huan 1; Qiu, Limei 1; Wang, Hao 1; Song, Linsheng 1
	2011-02-15
发表期刊	PLOS ONE
ISSN	1932-6203
卷号	6 期号:2 页码:e17089
文章类型	Article
摘要	Background: C-type lectins are a superfamily of Ca(2+) dependent carbohydrate-recognition proteins that play significant diverse roles in nonself-recognition and clearance of invaders. Though they are well characterized in vertebrates, the study of the potential function and mechanism of C-type lectins in invertebrate immunity is still in its infancy.; Background: C-type lectins are a superfamily of Ca(2+) dependent carbohydrate-recognition proteins that play significant diverse roles in nonself-recognition and clearance of invaders. Though they are well characterized in vertebrates, the study of the potential function and mechanism of C-type lectins in invertebrate immunity is still in its infancy. Methodology: A C-type lectin (CfLec-1) from scallop Chlamys farreri, a dominant cultured mollusk species in China, was selected to investigate its mRNA expression, localization and the possible functions in innate immunity in the present study. After scallop was stimulated by three typical PAMPs, the mRNA expression of CfLec-1 in hemocytes was poles apart. It was significantly up-regulated (p < 0.01) after scallops were stimulated by LPS or beta-glucan, but significantly down-regulated (p < 0.01) after PGN stimulation. The binding ability of recombinant CfLec-1 (designated as rCfLec-1) towards eight PAMPs was investigated subsequently by PAMPs microarray, which revealed rCfLec-1 could bind LPS, PGN and mannan in vitro, indicating CfLec-1 served as a PRR involved in the pathogen recognition. Immunofluorescence assay with polyclonal antibody specific for CfLec-1 revealed that CfLec-1 was mainly located in the mantle and gill of the scallop. CfLec-1 could bind to the surface of scallop hemocytes and recruited hemocytes to enhance their encapsulation in vitro, and this process could be specifically blocked by anti-rCfLec-1 antibody. Meanwhile, rCfLec-1 could also enhance the phagocytic activity of scallop hemocytes against Escherichia coli. Conclusions: The results clearly suggested that CfLec-1 in C. farreri not only served as a PRR involved in the PAMPs recognition, but also functioned as an opsonin participating in the clearance of invaders. It is therefore suspected that CfLec-1 could be an attachment-molecule to nonself-agents acting as an alternative to immunoglobulin in vertebrates.
学科领域	Life Sciences & Biomedicine - Other Topics
DOI	10.1371/journal.pone.0017089
URL	查看原文
收录类别	SCI
语种	英语
WOS记录号	WOS:000287369200021
引用统计	被引频次：99[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/337002/11823
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, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing, 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	Yang, Jialong,Wang, Lingling,Zhang, Huan,et al. C-Type Lectin in Chlamys farreri (CfLec-1) Mediating Immune Recognition and Opsonization[J]. PLOS ONE,2011,6(2):e17089.
APA	Yang, Jialong,Wang, Lingling,Zhang, Huan,Qiu, Limei,Wang, Hao,&Song, Linsheng.(2011).C-Type Lectin in Chlamys farreri (CfLec-1) Mediating Immune Recognition and Opsonization.PLOS ONE,6(2),e17089.
MLA	Yang, Jialong,et al."C-Type Lectin in Chlamys farreri (CfLec-1) Mediating Immune Recognition and Opsonization".PLOS ONE 6.2(2011):e17089.

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
C-Type Lectin in Chl（407KB）			限制开放	--	浏览