Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
| A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS | |
Jiang, Shuai1; Li, Hui1 ; Zhang, Daoxiang1; Zhang, Huan1; Wang, Lingling1; Sun, Jinsheng3; Song, Linsheng2
| |
| 2015-08-01 | |
| 发表期刊 | FISH & SHELLFISH IMMUNOLOGY
 |
| 卷号 | 45期号:2页码:583-591 |
| 文章类型 | Article |
| 摘要 | C1q proteins serve as pattern recognition receptors and involve in the pathogen recognition and complement pathway activation. In the present study, a novel C1q domain containing protein from Crassostrea gigas (designated CgC1qDC-1) was isolated by liposaccharide-Sepharose 6B affinity chromatography. The coding sequence of CgC1 qDC-1 gene was determined by performing a homologous search of eight tryptic peptides identified by IVIALDI-TOF/TOF-MS against the genome of C. gigas. The coding sequence of CgC1qDC-1 was of 387 bp encoding a polypeptide of 128 amino acids containing a typical globular C1q domain. The globular C1q domain possessed eight beta strands with a jelly-roll topology structure, which was similar to the structure of human gC1q domain. The mRNA transcripts of CgC1 qDC-1 were dominantly expressed in mantle and hemocytes, while low expressed in hepatopancreas, gonad, gill and muscle. The expression level of CgC1qDC-1 increased drastically at 6 h after Vibrio splendidus stimulation, and then gradually fell to the normal level at about 24 h. ELISA assay quantified that CgC1qDC-1 bound to LPS with high binding affinity (Kd = 0.09 x 10(-6) M). Moreover, CgC1qDC-1 significantly enhanced the phagocytosis of oyster hemocytes towards Gram-negative bacteria Escherichia con and V. splendidus. These results collectively indicated that CgC1qDC-1 could serve as pattern recognition receptor and opsonin in the innate immune response against invading Gram-negative bacteria. (C) 2015 Elsevier Ltd. All rights reserved. |
| 关键词 | Crassostrea Gigas Innate Immunity Liposaccharide Cgc1qdc-1 Phagocytosis |
| DOI | 10.1016/j.fsi.2015.05.021 |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000358626800044 |
| 引用统计 | |
| 文献类型 | 期刊论文 |
| 条目标识符 | http://ir.qdio.ac.cn/handle/337002/49671 |
| 专题 | 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.Dalian Ocean Univ, Dalian 116023, Peoples R China 3.Tianjin Key Lab Anim & Plant Resistance, Tianjin 300387, 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 | Jiang, Shuai,Li, Hui,Zhang, Daoxiang,et al. A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS[J]. FISH & SHELLFISH IMMUNOLOGY,2015,45(2):583-591. |
| APA | Jiang, Shuai.,Li, Hui.,Zhang, Daoxiang.,Zhang, Huan.,Wang, Lingling.,...&Song, Linsheng.(2015).A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS.FISH & SHELLFISH IMMUNOLOGY,45(2),583-591. |
| MLA | Jiang, Shuai,et al."A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS".FISH & SHELLFISH IMMUNOLOGY 45.2(2015):583-591. |
| 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 C1 q domain contai（1791KB） | 期刊论文 | 出版稿 | 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