Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
A C-type lectin (AiCTL-3) from bay scallop Argopecten irradians with mannose/galactose binding ability to bind various bacteria | |
Huang, Mengmeng1,2; Song, Xiaoyan1,3; Zhao, Jianmin1; Mu, Changkao1; Wang, Lingling1; Zhang, Huan1; Zhou, Zhi1; Liu, Xiaolin3; Song, Linsheng1; Wang, LL | |
2013-11-15 | |
发表期刊 | GENE |
ISSN | 0378-1119 |
卷号 | 531期号:1页码:31-38 |
文章类型 | Article |
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.; 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. |
关键词 | Argopecten Irradians C-type Lectin Pamps Binding Microbe Binding Ability Non-self Recognition Innate Immunity |
学科领域 | Genetics & Heredity |
DOI | 10.1016/j.gene.2013.08.042 |
URL | 查看原文 |
收录类别 | SCI |
语种 | 英语 |
WOS研究方向 | Genetics & Heredity |
WOS类目 | Genetics & Heredity |
WOS记录号 | WOS:000325906500005 |
WOS关键词 | PATTERN-RECOGNITION RECEPTOR ; CHLAMYS-FARRERI ; MOLECULAR-CLONING ; MANDUCA-SEXTA ; IMMUNE-SYSTEM ; PROTEIN ; DOMAIN ; GENE ; SEQUENCE ; HEPATOPANCREAS |
WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
引用统计 | |
文献类型 | 期刊论文 |
条目标识符 | http://ir.qdio.ac.cn/handle/337002/16510 |
专题 | 实验海洋生物学重点实验室 |
通讯作者 | Wang, LL |
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 |
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,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.,...&Wang, LL.(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. |
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 C-type lectin (AiC(1464KB) | 限制开放 | CC BY-NC-SA | 浏览 |
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。
修改评论