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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
Source PublicationFISH & SHELLFISH IMMUNOLOGY
Volume45Issue:2Pages:583-591
SubtypeArticle
AbstractC1q 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.
KeywordCrassostrea Gigas Innate Immunity Liposaccharide Cgc1qdc-1 Phagocytosis
DOI10.1016/j.fsi.2015.05.021
Indexed BySCI
Language英语
WOS IDWOS:000358626800044
Citation statistics
Cited Times:23[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/49671
Collection实验海洋生物学重点实验室
Affiliation1.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
First Author AffilicationKey Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
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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.
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