中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose/galactose binding ability to bind various bacteria

文献类型:期刊论文

作者Huang, Mengmeng1,2; Song, Xiaoyan1,3; Zhao, Jianmin1; Mu, Changkao1; Wang, Lingling1; Zhang, Huan1; Zhou, Zhi1; Liu, Xiaolin3; Song, Linsheng1
刊名GENE
出版日期2013-11-15
卷号531期号:1页码:31-38
关键词Argopecten irradians C-type lectin PAMPs binding Microbe binding ability Non-self recognition Innate immunity
ISSN号0378-1119
通讯作者Wang, LL
中文摘要C-type lectins are a family of Ca2+-dependent carbohydrate-binding proteins playing crucial roles in innate immunity of vertebrates and invertebrates. In the present study, the cDNA of a C-type lectin with one carbohydrate-recognition domain (CRD) of 127 amino acids was cloned from bay scallop Argopecten irradians (designated AiCTL-3) by rapid amplification of cDNA end (RACE) techniques based on expressed sequence tag (EST) analysis. The mRNA transcripts of AiCTL-3 could be detected in all the tested tissues including hepatopancreas, gonad, adductor muscle, heart, hemocytes, mantle and gill, with the highest expression level in hepatopancreas. After the challenges with Vibrio anguillarum and Micrococcus luteus, the mRNA expression level of AiCTL-3 was obviously up-regulated and reached the maximum level at 9 h (11.87 fold, P <0.01, and 20.02-fold, P < 0.05, respectively). The recombinant AiCTL-3 (designated as rAiCTL-3) could bind LPS, PGN, and glucan in vitro, but could not bind mannan. And it also bound Gram-positive bacteria Staphylococcus aureus as well as Gram-negative bacteria Escherichia coli and V. anguillarum. With a Ca2+ binding site 2 EPN (Glu-Pro-Asn) motif, rAiCTL-3 could bind both mannose and galactose which was quite different from those in vertebrate. Meanwhile, it could significantly enhance the phagocytosis of scallop hemocytes in vitro. The results clearly suggested that AiCTL-3 could serve not only as a PRR participated in the immune response against various PAMPs and bacteria in non-self recognition via mannose/galactose binding specificity but an opsonin playing an important part in clearance of invaders. (C) 2013 Elsevier B.V. All rights reserved.
英文摘要C-type lectins are a family of Ca2+-dependent carbohydrate-binding proteins playing crucial roles in innate immunity of vertebrates and invertebrates. In the present study, the cDNA of a C-type lectin with one carbohydrate-recognition domain (CRD) of 127 amino acids was cloned from bay scallop Argopecten irradians (designated AiCTL-3) by rapid amplification of cDNA end (RACE) techniques based on expressed sequence tag (EST) analysis. The mRNA transcripts of AiCTL-3 could be detected in all the tested tissues including hepatopancreas, gonad, adductor muscle, heart, hemocytes, mantle and gill, with the highest expression level in hepatopancreas. After the challenges with Vibrio anguillarum and Micrococcus luteus, the mRNA expression level of AiCTL-3 was obviously up-regulated and reached the maximum level at 9 h (11.87 fold, P <0.01, and 20.02-fold, P < 0.05, respectively). The recombinant AiCTL-3 (designated as rAiCTL-3) could bind LPS, PGN, and glucan in vitro, but could not bind mannan. And it also bound Gram-positive bacteria Staphylococcus aureus as well as Gram-negative bacteria Escherichia coli and V. anguillarum. With a Ca2+ binding site 2 EPN (Glu-Pro-Asn) motif, rAiCTL-3 could bind both mannose and galactose which was quite different from those in vertebrate. Meanwhile, it could significantly enhance the phagocytosis of scallop hemocytes in vitro. The results clearly suggested that AiCTL-3 could serve not only as a PRR participated in the immune response against various PAMPs and bacteria in non-self recognition via mannose/galactose binding specificity but an opsonin playing an important part in clearance of invaders. (C) 2013 Elsevier B.V. All rights reserved.
WOS标题词Science & Technology ; Life Sciences & Biomedicine
学科主题Genetics & Heredity
类目[WOS]Genetics & Heredity
研究领域[WOS]Genetics & Heredity
关键词[WOS]PATTERN-RECOGNITION RECEPTOR ; CHLAMYS-FARRERI ; MOLECULAR-CLONING ; MANDUCA-SEXTA ; IMMUNE-SYSTEM ; PROTEIN ; DOMAIN ; GENE ; SEQUENCE ; HEPATOPANCREAS
收录类别SCI
原文出处10.1016/j.gene.2013.08.042
语种英语
WOS记录号WOS:000325906500005
公开日期2014-07-17
源URL[http://ir.qdio.ac.cn/handle/337002/16510]  
专题海洋研究所_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.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
3.Northwest A&F Univ, Coll Anim Sci & Technol, Yangling 712100, Peoples R China
推荐引用方式
GB/T 7714
Huang, Mengmeng,Song, Xiaoyan,Zhao, Jianmin,et al. A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose/galactose binding ability to bind various bacteria[J]. GENE,2013,531(1):31-38.
APA Huang, Mengmeng.,Song, Xiaoyan.,Zhao, Jianmin.,Mu, Changkao.,Wang, Lingling.,...&Song, Linsheng.(2013).A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose/galactose binding ability to bind various bacteria.GENE,531(1),31-38.
MLA Huang, Mengmeng,et al."A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose/galactose binding ability to bind various bacteria".GENE 531.1(2013):31-38.

入库方式: OAI收割

来源:海洋研究所

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