A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri
文献类型：期刊论文
| 作者 | Zheng, Peilin1,2; Wang, Hao1; Zhao, Jianmin1; Song, Linsheng1; Qiu, Limei1; Dong, Chaohua3; Wang, Bo1,2; Gai, Yunchao1,2; Mu, Changkao1,2; Li, Chenghua1 |
| 刊名 | FISH & SHELLFISH IMMUNOLOGY
 |
| 出版日期 | 2008-03-01 |
| 卷号 | 24期号:3页码:286-293 |
| 关键词 | Chlamys Farreri Lectin Ca2++ Independent Staphylococcus Haemolyticus |
| ISSN号 | 1050-4648 |
| DOI | 10.1016/j.fsi.2007.11.014 |
| 文献子类 | Article |
| 英文摘要 | Lectins are a family of carbohydrate-recognition proteins which play crucial roles in innate immunity. In this study, a new lectin (CfLec-2) gene was cloned from Chlamys farreri by EST and RACE approaches. The full-length cDNA of CfLec-2 was composed of 708 bp, encoding a typical Long form carbohydrate-recognition domain of 130 residues. The deduced amino acid sequence showed high similarity to Brevican in Homo sapiens, C-type lectin-1 and lectin-2 in Anguilla japonica. The cDNA fragment encoding the mature peptide of CfLec-2 was recombined into plasmid pET-32a (+) and expressed in Escherichia coli Rosseta-Gami (DE3). The recombinant CfLec-2 (rCfLec-2) protein exhibited aggregative activity toward Staphylococcus haemolyticus, and the agglutination could be inhibited by D-mannose but not EDTA or D-galactose, indicating that CfLec-2 was a Ca2+ independent lectin. Moreover, rCfLec-2 could suppress the growth of E. coli TOP10F'. These results suggested that CfLec-2 was perhaps involved in the recognition and clearance of bacterial. pathogens in scallop. (C) 2007 Elsevier Ltd. All rights reserved.; Lectins are a family of carbohydrate-recognition proteins which play crucial roles in innate immunity. In this study, a new lectin (CfLec-2) gene was cloned from Chlamys farreri by EST and RACE approaches. The full-length cDNA of CfLec-2 was composed of 708 bp, encoding a typical Long form carbohydrate-recognition domain of 130 residues. The deduced amino acid sequence showed high similarity to Brevican in Homo sapiens, C-type lectin-1 and lectin-2 in Anguilla japonica. The cDNA fragment encoding the mature peptide of CfLec-2 was recombined into plasmid pET-32a (+) and expressed in Escherichia coli Rosseta-Gami (DE3). The recombinant CfLec-2 (rCfLec-2) protein exhibited aggregative activity toward Staphylococcus haemolyticus, and the agglutination could be inhibited by D-mannose but not EDTA or D-galactose, indicating that CfLec-2 was a Ca2+ independent lectin. Moreover, rCfLec-2 could suppress the growth of E. coli TOP10F'. These results suggested that CfLec-2 was perhaps involved in the recognition and clearance of bacterial. pathogens in scallop. (C) 2007 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:000254375200003 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5763]  |
| 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, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Ocean Univ China, Coll Marine Life Sci, Qingdao 266003, Peoples R China 4.Tianjin Agr Coll, Tianjin 300381, Peoples R China |
| 推荐引用方式 GB/T 7714 | Zheng, Peilin,Wang, Hao,Zhao, Jianmin,et al. A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri[J]. FISH & SHELLFISH IMMUNOLOGY,2008,24(3):286-293. |
| APA | Zheng, Peilin.,Wang, Hao.,Zhao, Jianmin.,Song, Linsheng.,Qiu, Limei.,...&Xing, Kezhi.(2008).A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri.FISH & SHELLFISH IMMUNOLOGY,24(3),286-293. |
| MLA | Zheng, Peilin,et al."A lectin (CfLec-2) aggregating Staphylococcus haemolyticus from scallop Chlamys farreri".FISH & SHELLFISH IMMUNOLOGY 24.3(2008):286-293. |
入库方式： OAI收割
来源：海洋研究所
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