An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion
文献类型：期刊论文
| 作者 | Yang, Jialong1,2; Qiu, Limei1; Wei, Xiumei3; Wang, Leilei1,2; Wang, Lingling1; Zhou, Zhi1,2; Zhang, Huan1; Liu, Lin1,2; Song, Linsheng1 |
| 刊名 | DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
 |
| 出版日期 | 2010-12-01 |
| 卷号 | 34期号:12页码:1274-1282 |
| 关键词 | Chlamys Farreri C-type Lectin Innate Immunity Pattern Recognition Receptor Cellular Adhesion Evolution |
| ISSN号 | 0145-305X |
| DOI | 10.1016/j.dci.2010.07.004 |
| 文献子类 | Article |
| 英文摘要 | C-type lectins are a superfamily of Ca(2+) dependent carbohydrate-recognition proteins which play significant diverse roles in nonself-recognition and clearance of invaders. In the present study, a C-type lectin (CfLec-2) from Zhikong scallop Chlamys farreri was selected to investigate its functions in innate immunity. The mRNA expression of CfLec-2 in hemocytes was significantly up-regulated (P < 0.01) after scallops were stimulated by LPS. PGN or beta-glucan, and reached the highest expression level at 12h post-stimulation, which was 72.5-, 23.6- or 43.8-fold compared with blank group, respectively. The recombinant Cflec-2 (designated as rCfLec-2) could bind LPS, PGN, mannan and zymosan in vitro, but it could not bind beta-glucan. Immunofluorescence assay with polyclonal antibody specific for Cflec-2 revealed that CfLec-2 was mainly located in the mantle, kidney and gonad. Furthermore, rCfLec-2 could bind to the surface of scallop hemocytes, and then initiated cellular adhesion and recruited hemocytes to enhance their encapsulation in vitro, and this process could be specifically blocked by anti-rCfLec-2 serum. These results collectively suggested that CfLec-2 from the primitive deuterostome C. farreri could perform two distinct immune functions, pathogen recognition and cellular adhesion synchronously, while these functions were performed by collectins and selectins in vertebrates, respectively. The synchronous functions of pathogen recognition and cellular adhesion performed by CfLec-2 tempted us to suspect that CfLec-2 was an ancient form of C-type lectin, and apparently the differentiation of these two functions mediated by C-type lectins occurred after mollusk in phylogeny. (C) 2010 Elsevier Ltd. All rights reserved.; C-type lectins are a superfamily of Ca2+ dependent carbohydrate-recognition proteins which play significant diverse roles in nonself-recognition and clearance of invaders. In the present study, a C-type lectin (CfLec-2) from Zhikong scallop Chlamys farreri was selected to investigate its functions in innate immunity. The mRNA expression of CfLec-2 in hemocytes was significantly up-regulated (P < 0.01) after scallops were stimulated by LPS. PGN or beta-glucan, and reached the highest expression level at 12h post-stimulation, which was 72.5-, 23.6- or 43.8-fold compared with blank group, respectively. The recombinant Cflec-2 (designated as rCfLec-2) could bind LPS, PGN, mannan and zymosan in vitro, but it could not bind beta-glucan. Immunofluorescence assay with polyclonal antibody specific for Cflec-2 revealed that CfLec-2 was mainly located in the mantle, kidney and gonad. Furthermore, rCfLec-2 could bind to the surface of scallop hemocytes, and then initiated cellular adhesion and recruited hemocytes to enhance their encapsulation in vitro, and this process could be specifically blocked by anti-rCfLec-2 serum. These results collectively suggested that CfLec-2 from the primitive deuterostome C. farreri could perform two distinct immune functions, pathogen recognition and cellular adhesion synchronously, while these functions were performed by collectins and selectins in vertebrates, respectively. The synchronous functions of pathogen recognition and cellular adhesion performed by CfLec-2 tempted us to suspect that CfLec-2 was an ancient form of C-type lectin, and apparently the differentiation of these two functions mediated by C-type lectins occurred after mollusk in phylogeny. (C) 2010 Elsevier Ltd. All rights reserved. |
| 学科主题 | Immunology ; Zoology |
| URL标识 | 查看原文 |
| 语种 | 英语 |
| WOS记录号 | WOS:000283270700005 |
| 公开日期 | 2010-12-24 |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/5789]  |
| 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, Key Lab Expt Marine Biol, Inst Oceanol, Qingdao 266071, Peoples R China 2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China 3.Ocean Univ China, Lab Pathol & Immunol Aquat Anim, Qingdao 266003, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Jialong,Qiu, Limei,Wei, Xiumei,et al. An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2010,34(12):1274-1282. |
| APA | Yang, Jialong.,Qiu, Limei.,Wei, Xiumei.,Wang, Leilei.,Wang, Lingling.,...&Song, Linsheng.(2010).An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,34(12),1274-1282. |
| MLA | Yang, Jialong,et al."An ancient C-type lectin in Chlamys farreri (CfLec-2) that mediate pathogen recognition and cellular adhesion".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 34.12(2010):1274-1282. |
入库方式： OAI收割
来源：海洋研究所
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