A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
文献类型:期刊论文
作者 | Jiang, Shuai1; Li, Hui1![]() |
刊名 | FISH & SHELLFISH IMMUNOLOGY
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出版日期 | 2015-08-01 |
卷号 | 45期号:2页码:583-591 |
关键词 | Crassostrea gigas Innate immunity Liposaccharide CgC1qDC-1 Phagocytosis |
英文摘要 | 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. |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000358626800044 |
源URL | [http://ir.qdio.ac.cn/handle/337002/49671] ![]() |
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.Dalian Ocean Univ, Dalian 116023, Peoples R China 3.Tianjin Key Lab Anim & Plant Resistance, Tianjin 300387, Peoples R China |
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. |
入库方式: OAI收割
来源:海洋研究所
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