A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS

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...

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Published in:Fish & Shellfish Immunology
Main Authors: Jiang, Shuai, Li, Hui, Zhang, Daoxiang, Zhang, Huan, Wang, Lingling, Sun, Jinsheng, Song, Linsheng
Format: Article in Journal/Newspaper
Language:English
Published: 2015
Subjects:
Online Access:http://ir.qdio.ac.cn/handle/337002/49671
https://doi.org/10.1016/j.fsi.2015.05.021
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spelling ftchinacasciocas:oai:ir.qdio.ac.cn:337002/49671 2023-05-15T15:57:46+02:00 A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS Jiang, Shuai Li, Hui Zhang, Daoxiang Zhang, Huan Wang, Lingling Sun, Jinsheng Song, Linsheng 2015-08-01 http://ir.qdio.ac.cn/handle/337002/49671 https://doi.org/10.1016/j.fsi.2015.05.021 英语 eng FISH & SHELLFISH IMMUNOLOGY 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. http://ir.qdio.ac.cn/handle/337002/49671 doi:10.1016/j.fsi.2015.05.021 Crassostrea Gigas Innate Immunity Liposaccharide Cgc1qdc-1 Phagocytosis Article 期刊论文 2015 ftchinacasciocas https://doi.org/10.1016/j.fsi.2015.05.021 2022-06-27T05:37:17Z 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. Article in Journal/Newspaper Crassostrea gigas Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Fish & Shellfish Immunology 45 2 583 591
institution Open Polar
collection Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR
op_collection_id ftchinacasciocas
language English
topic Crassostrea Gigas
Innate Immunity
Liposaccharide
Cgc1qdc-1
Phagocytosis
spellingShingle Crassostrea Gigas
Innate Immunity
Liposaccharide
Cgc1qdc-1
Phagocytosis
Jiang, Shuai
Li, Hui
Zhang, Daoxiang
Zhang, Huan
Wang, Lingling
Sun, Jinsheng
Song, Linsheng
A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
topic_facet Crassostrea Gigas
Innate Immunity
Liposaccharide
Cgc1qdc-1
Phagocytosis
description 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.
format Article in Journal/Newspaper
author Jiang, Shuai
Li, Hui
Zhang, Daoxiang
Zhang, Huan
Wang, Lingling
Sun, Jinsheng
Song, Linsheng
author_facet Jiang, Shuai
Li, Hui
Zhang, Daoxiang
Zhang, Huan
Wang, Lingling
Sun, Jinsheng
Song, Linsheng
author_sort Jiang, Shuai
title A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
title_short A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
title_full A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
title_fullStr A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
title_full_unstemmed A C1 q domain containing protein from Crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to LPS
title_sort c1 q domain containing protein from crassostrea gigas serves as pattern recognition receptor and opsonin with high binding affinity to lps
publishDate 2015
url http://ir.qdio.ac.cn/handle/337002/49671
https://doi.org/10.1016/j.fsi.2015.05.021
genre Crassostrea gigas
genre_facet Crassostrea gigas
op_relation FISH & SHELLFISH IMMUNOLOGY
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.
http://ir.qdio.ac.cn/handle/337002/49671
doi:10.1016/j.fsi.2015.05.021
op_doi https://doi.org/10.1016/j.fsi.2015.05.021
container_title Fish & Shellfish Immunology
container_volume 45
container_issue 2
container_start_page 583
op_container_end_page 591
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