IOCAS-IR  > 实验海洋生物学重点实验室
A four-CRD C-type lectin from Chlamys farreri mediating nonself-recognition with broader spectrum and opsonization
Huang, Mengmeng1,2; Wang, Lingling1; Yang, Jialong1,2; Zhang, Huan1; Wang, Leilei1,2; Song, Linsheng1; Zhang, H
2013-04-01
发表期刊DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
ISSN0145-305X
卷号39期号:4页码:363-369
文章类型Article
摘要C-type lectins are a superfamily of Ca2+-dependent carbohydrate-recognition proteins consisting of at least one carbohydrate-recognition domain (CRD), which participate in nonself-recognition and clearance of invaders. In invertebrate, some multidomain C-type lectins have been identified, but their relative functions and binding mechanism are still meager. In the present study, A C-type lectin (CfLec-4) with four CRDs from Chlamys farreri was selected to investigate its possible function in innate immunity. The mRNA expression of CfLec-4 in hemocytes was significantly up-regulated (P < 0.01) after the stimulations of beta-glucan, LPS or PGN, and reached the highest expression level at 3, 6, 12 h post-stimulation, which was 27.9-, 22.6- or 47.9-fold of that in blank group, respectively. Immunohistochemistry assay with polyclonal antibody specific for CfLec-4 revealed that the endogenous CfLec-4 was mainly located in the hepatopancreas, kidney and gonad of the scallops. The recombinant CfLec-4 (rCflec-4) could bind LPS, PGN, glucan and mannose in vitro, but could not bind LTA. Furthermore, rCflec-4 displayed a broader bacteria binding spectrum towards Gram-positive bacteria Staphylococcus aureus and Micrococcus luteus as well as Gram-negative bacteria Escherichia coil, Vibrio anguillarum and fungi Pichia pastoris. Meanwhile, rCfLec-4 could significantly (P < 0.01) enhance the phagocytosis of hemocytes in vitro. The results clearly suggested that four-CRD containing CfLec-4 not only served as PRR with wider recognition spectrum, but also functioned as an opsonin participating in the clearance of invaders in scallops. It could be inferred that the diversity and complexity of CRDs in C-type lectins endowed these receptors with comprehensive recognition spectrum and multiple immune functions against complex living environment. (C) 2012 Elsevier Ltd. All rights reserved.; C-type lectins are a superfamily of Ca2+-dependent carbohydrate-recognition proteins consisting of at least one carbohydrate-recognition domain (CRD), which participate in nonself-recognition and clearance of invaders. In invertebrate, some multidomain C-type lectins have been identified, but their relative functions and binding mechanism are still meager. In the present study, A C-type lectin (CfLec-4) with four CRDs from Chlamys farreri was selected to investigate its possible function in innate immunity. The mRNA expression of CfLec-4 in hemocytes was significantly up-regulated (P < 0.01) after the stimulations of beta-glucan, LPS or PGN, and reached the highest expression level at 3, 6, 12 h post-stimulation, which was 27.9-, 22.6- or 47.9-fold of that in blank group, respectively. Immunohistochemistry assay with polyclonal antibody specific for CfLec-4 revealed that the endogenous CfLec-4 was mainly located in the hepatopancreas, kidney and gonad of the scallops. The recombinant CfLec-4 (rCflec-4) could bind LPS, PGN, glucan and mannose in vitro, but could not bind LTA. Furthermore, rCflec-4 displayed a broader bacteria binding spectrum towards Gram-positive bacteria Staphylococcus aureus and Micrococcus luteus as well as Gram-negative bacteria Escherichia coil, Vibrio anguillarum and fungi Pichia pastoris. Meanwhile, rCfLec-4 could significantly (P < 0.01) enhance the phagocytosis of hemocytes in vitro. The results clearly suggested that four-CRD containing CfLec-4 not only served as PRR with wider recognition spectrum, but also functioned as an opsonin participating in the clearance of invaders in scallops. It could be inferred that the diversity and complexity of CRDs in C-type lectins endowed these receptors with comprehensive recognition spectrum and multiple immune functions against complex living environment. (C) 2012 Elsevier Ltd. All rights reserved.
关键词Chlamys Farreri C-type Lectin Innate Immunity Nonself-recognition Opsonization Microbe Binding Ability
学科领域Immunology ; Zoology
DOI10.1016/j.dci.2012.12.002
URL查看原文
收录类别SCI
语种英语
WOS研究方向Immunology ; Zoology
WOS类目Immunology ; Zoology
WOS记录号WOS:000317248900006
WOS关键词PATTERN-RECOGNITION ; INNATE IMMUNITY ; BINDING LECTIN ; MANDUCA-SEXTA ; PATHOGEN RECOGNITION ; COMPLEMENT PATHWAY ; SELF-RECOGNITION ; BOMBYX-MORI ; PROTEIN ; LIPOPOLYSACCHARIDE
WOS标题词Science & Technology ; Life Sciences & Biomedicine
引用统计
被引频次:39[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/337002/16511
专题实验海洋生物学重点实验室
通讯作者Zhang, H
作者单位1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
2.Univ Chinese Acad Sci, Beijing 100049, 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
Huang, Mengmeng,Wang, Lingling,Yang, Jialong,et al. A four-CRD C-type lectin from Chlamys farreri mediating nonself-recognition with broader spectrum and opsonization[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2013,39(4):363-369.
APA Huang, Mengmeng.,Wang, Lingling.,Yang, Jialong.,Zhang, Huan.,Wang, Leilei.,...&Zhang, H.(2013).A four-CRD C-type lectin from Chlamys farreri mediating nonself-recognition with broader spectrum and opsonization.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,39(4),363-369.
MLA Huang, Mengmeng,et al."A four-CRD C-type lectin from Chlamys farreri mediating nonself-recognition with broader spectrum and opsonization".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 39.4(2013):363-369.
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
A four-CRD C-type le(1114KB) 限制开放CC BY-NC-SA浏览
个性服务
推荐该条目
保存到收藏夹
查看访问统计
导出为Endnote文件
谷歌学术
谷歌学术中相似的文章
[Huang, Mengmeng]的文章
[Wang, Lingling]的文章
[Yang, Jialong]的文章
百度学术
百度学术中相似的文章
[Huang, Mengmeng]的文章
[Wang, Lingling]的文章
[Yang, Jialong]的文章
必应学术
必应学术中相似的文章
[Huang, Mengmeng]的文章
[Wang, Lingling]的文章
[Yang, Jialong]的文章
相关权益政策
暂无数据
收藏/分享
文件名: A four-CRD C-type lectin from Chlamys farreri mediating nonself-recognition with broader spectrum and opsonization.pdf
格式: Adobe PDF
此文件暂不支持浏览
所有评论 (0)
暂无评论
 

除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。