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...
Published in: | Fish & Shellfish Immunology |
---|---|
Main Authors: | , , , , , , |
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 |
id |
ftchinacasciocas:oai:ir.qdio.ac.cn:337002/49671 |
---|---|
record_format |
openpolar |
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 |
_version_ |
1766393461042315264 |