A novel C-type lectin from bay scallop Argopecten irradians (AiCTL-7) agglutinating fungi with mannose specificity
文献类型：期刊论文
| 作者 | Kong, Pengfei1,2; Wang, Lingling1; Zhang, Huan1,2; Song, Xiaoyan1; Zhou, Zhi1,2; Yang, Jialong1,2; Qiu, Limei1; Wang, Leilei1,2; Song, Linsheng1 |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2011-03-01 |
| 卷号 | 30期号:3页码:836-844 |
| 关键词 | Argopecten Irradians Innate Immunity Pattern Recognition Receptor C-type Lectin Microbial Agglutinating Activity |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2011.01.005 |
| 文献子类 | Article |
| 英文摘要 | C-type lectins are a superfamily of proteins that can bind pathogen-associated molecular patterns (PAMPs) and microorganisms through the recognition of carbohydrates, thus they are directly involved in innate defense mechanisms as part of the acute-phase response to infection. In this study, the cDNA of a novel C-type lectin (designated as AiCTL-7) was cloned from bay scallop Argopecten irradians by expression sequence tag (EST) analysis and rapid amplification of cDNA ends (RACE) approach. The full-length cDNA of AiCTL-7 was of 651 bp containing a 525 bp open reading frame which encoded a signal peptide of 15 residues and a conserved carbohydrate-recognition domain (CRD) of 174 residues with the EPD and WSD motifs instead of the invariant EPN and WND motifs for determining the carbohydrate-binding specificity and constructing Ca2+-binding site 2 in vertebrates. The deduced amino acid sequence of AiCTL-7 CRD shared homology not only with the CRDs of C-type lectins in mollusks, but also with the fish lectin CRDs. The mRNA transcripts of AiCTL-7 were mainly detected in the tissue of hepatopancreas and also marginally detectable in kidney, gonad, hemocytes, heart and adductor of health scallop. After challenge with fungi Pichia pastoris GS115 and Gram-negative bacteria Listonella anguillarum, the relative expression level of AiCTL-7 was up-regulated significantly in hepatopancreas and hemocytes. The CRD of AiCTL-7 was recombined and expressed in Escherichia coli, and the recombinant protein (rAiCTL-7) aggregated P. pastoris remarkably in a Ca2+-dependent manner, and this agglutination could be inhibited by D-mannose, but not by D-galactose or beta-1,3-glucan. However, rAiCTL-7 displayed no obvious agglutinating activity against L anguillarum. These results collectively indicated that AiCTL-7 was involved in the primitive acute-phase response to microbial invasion as an important pattern recognition receptor (PRR) in the innate immune system of scallops. (C) 2011 Elsevier Ltd. All rights reserved.; C-type lectins are a superfamily of proteins that can bind pathogen-associated molecular patterns (PAMPs) and microorganisms through the recognition of carbohydrates, thus they are directly involved in innate defense mechanisms as part of the acute-phase response to infection. In this study, the cDNA of a novel C-type lectin (designated as AiCTL-7) was cloned from bay scallop Argopecten irradians by expression sequence tag (EST) analysis and rapid amplification of cDNA ends (RACE) approach. The full-length cDNA of AiCTL-7 was of 651 bp containing a 525 bp open reading frame which encoded a signal peptide of 15 residues and a conserved carbohydrate-recognition domain (CRD) of 174 residues with the EPD and WSD motifs instead of the invariant EPN and WND motifs for determining the carbohydrate-binding specificity and constructing Ca(2+)-binding site 2 in vertebrates. The deduced amino acid sequence of AiCTL-7 CRD shared homology not only with the CRDs of C-type lectins in mollusks, but also with the fish lectin CRDs. The mRNA transcripts of AiCTL-7 were mainly detected in the tissue of hepatopancreas and also marginally detectable in kidney, gonad, hemocytes, heart and adductor of health scallop. After challenge with fungi Pichia pastoris GS115 and Gram-negative bacteria Listonella anguillarum, the relative expression level of AiCTL-7 was up-regulated significantly in hepatopancreas and hemocytes. The CRD of AiCTL-7 was recombined and expressed in Escherichia coli, and the recombinant protein (rAiCTL-7) aggregated P. pastoris remarkably in a Ca(2+)-dependent manner, and this agglutination could be inhibited by D-mannose, but not by D-galactose or beta-1,3-glucan. However, rAiCTL-7 displayed no obvious agglutinating activity against L anguillarum. These results collectively indicated that AiCTL-7 was involved in the primitive acute-phase response to microbial invasion as an important pattern recognition receptor (PRR) in the innate immune system of scallops. (C) 2011 Elsevier Ltd. All rights reserved. |
| 学科主题 | Fisheries ; Immunology ; Marine & Freshwater Biology ; Veterinary Sciences |
| URL标识 | 查看原文 |
| 语种 | 英语 |
| WOS记录号 | WOS:000288888500011 |
| 公开日期 | 2012-07-03 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/11756]  |
| 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.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Kong, Pengfei,Wang, Lingling,Zhang, Huan,et al. A novel C-type lectin from bay scallop Argopecten irradians (AiCTL-7) agglutinating fungi with mannose specificity[J]. FISH & SHELLFISH IMMUNOLOGY,2011,30(3):836-844. |
| APA | Kong, Pengfei.,Wang, Lingling.,Zhang, Huan.,Song, Xiaoyan.,Zhou, Zhi.,...&Song, Linsheng.(2011).A novel C-type lectin from bay scallop Argopecten irradians (AiCTL-7) agglutinating fungi with mannose specificity.FISH & SHELLFISH IMMUNOLOGY,30(3),836-844. |
| MLA | Kong, Pengfei,et al."A novel C-type lectin from bay scallop Argopecten irradians (AiCTL-7) agglutinating fungi with mannose specificity".FISH & SHELLFISH IMMUNOLOGY 30.3(2011):836-844. |
入库方式： OAI收割
来源：海洋研究所
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