A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas
Ubiquitination is an important post-translational protein modification and plays a crucial role in various processes such as cell cycle, signal transduction, and transcriptional regulation. In the present study, a novel ubiquitin (Ub)-protein ligase E3 (designed as CgE3Rv1) was identified from Crass...
Published in: | Developmental & Comparative Immunology |
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Language: | English |
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2016
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Online Access: | http://ir.qdio.ac.cn/handle/337002/131017 https://doi.org/10.1016/j.dci.2016.02.027 |
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ftchinacasciocas:oai:ir.qdio.ac.cn:337002/131017 2023-05-15T15:57:55+02:00 A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas Cheng, Qi Wang, Hao Jiang, Shuai Wang, Lingling Xin, Lusheng Liu, Conghui Jia, Zhihao Song, Linsheng Zhu, Beiwei 2016-07-01 http://ir.qdio.ac.cn/handle/337002/131017 https://doi.org/10.1016/j.dci.2016.02.027 英语 eng DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY Cheng, Qi,Wang, Hao,Jiang, Shuai,et al. A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2016,60:180-190. http://ir.qdio.ac.cn/handle/337002/131017 doi:10.1016/j.dci.2016.02.027 Crassostrea Gigas Ubiquitination Immune Response Lipopolysaccharide Stimulation Ub-protein Ligase E3 Article 期刊论文 2016 ftchinacasciocas https://doi.org/10.1016/j.dci.2016.02.027 2022-06-27T05:37:39Z Ubiquitination is an important post-translational protein modification and plays a crucial role in various processes such as cell cycle, signal transduction, and transcriptional regulation. In the present study, a novel ubiquitin (Ub)-protein ligase E3 (designed as CgE3Rv1) was identified from Crassostrea gigas, and its ubiquitination regulation in the immune response against lipopolysaccharide (LPS) stimulation was investigated. The open reading frame of CgE3Rv1 gene was of 1455 bp encoding a polypeptide of 484 amino acids with the predicted molecular mass of 54.89 kDa. There were two transmembrane regions and a RING-variant (RINGv) domain identified in CgE3Rv1. CgE3Rv1 shared similar C4HC3 zinc-finger like motif with those RINGv domain Ub-protein ligases E3s identified from vertebrates and invertebrates, and it was closely clustered with the membrane-associated RING-CH2 (MARCH2) Ub-protein ligases E3s in the phylogenetic tree. The mRNA transcript of CgE3Rv1 was highest expressed in gonads and hemolymph (p < 0.05), and its mRNA expression level in hemocytes was significantly increased at 6 h (p < 0.01) after the stimulation of LPS, while the up-regulated mRNA expression was significantly decreased (p < 0.01) after acetylcholine stimulation. No significant changes of CgE3Rv1 expression were observed after peptidoglycan or mannan stimulation. Immunohistochemistry and in situ hybridization assays revealed that CgE3Rv1 protein and mRNA were dominantly distributed in the gonad. In the hemocytes, CgE3Rv1 was mainly located around the nucleus, and slightly distributed in the cytoplasm and on the cell membrane. Recombinant CgE3Rv1 RINGv domain protein (rCgE3Rv1-RINGv) was confirmed to activate the Ub reaction system in vitro with the aid of Ub-activating enzyme El and Ub-conjugating enzyme E2. These results demonstrated that CgE3Rv1 was an Ub-protein ligase E3, which was involved in the immune response against LPS and the interaction with cell surface signal molecules of neuroendocrine-immune system in ... Article in Journal/Newspaper Crassostrea gigas Pacific oyster Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR Pacific Developmental & Comparative Immunology 60 180 190 |
institution |
Open Polar |
collection |
Institute of Oceanology, Chinese Academy of Sciences: IOCAS-IR |
op_collection_id |
ftchinacasciocas |
language |
English |
topic |
Crassostrea Gigas Ubiquitination Immune Response Lipopolysaccharide Stimulation Ub-protein Ligase E3 |
spellingShingle |
Crassostrea Gigas Ubiquitination Immune Response Lipopolysaccharide Stimulation Ub-protein Ligase E3 Cheng, Qi Wang, Hao Jiang, Shuai Wang, Lingling Xin, Lusheng Liu, Conghui Jia, Zhihao Song, Linsheng Zhu, Beiwei A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
topic_facet |
Crassostrea Gigas Ubiquitination Immune Response Lipopolysaccharide Stimulation Ub-protein Ligase E3 |
description |
Ubiquitination is an important post-translational protein modification and plays a crucial role in various processes such as cell cycle, signal transduction, and transcriptional regulation. In the present study, a novel ubiquitin (Ub)-protein ligase E3 (designed as CgE3Rv1) was identified from Crassostrea gigas, and its ubiquitination regulation in the immune response against lipopolysaccharide (LPS) stimulation was investigated. The open reading frame of CgE3Rv1 gene was of 1455 bp encoding a polypeptide of 484 amino acids with the predicted molecular mass of 54.89 kDa. There were two transmembrane regions and a RING-variant (RINGv) domain identified in CgE3Rv1. CgE3Rv1 shared similar C4HC3 zinc-finger like motif with those RINGv domain Ub-protein ligases E3s identified from vertebrates and invertebrates, and it was closely clustered with the membrane-associated RING-CH2 (MARCH2) Ub-protein ligases E3s in the phylogenetic tree. The mRNA transcript of CgE3Rv1 was highest expressed in gonads and hemolymph (p < 0.05), and its mRNA expression level in hemocytes was significantly increased at 6 h (p < 0.01) after the stimulation of LPS, while the up-regulated mRNA expression was significantly decreased (p < 0.01) after acetylcholine stimulation. No significant changes of CgE3Rv1 expression were observed after peptidoglycan or mannan stimulation. Immunohistochemistry and in situ hybridization assays revealed that CgE3Rv1 protein and mRNA were dominantly distributed in the gonad. In the hemocytes, CgE3Rv1 was mainly located around the nucleus, and slightly distributed in the cytoplasm and on the cell membrane. Recombinant CgE3Rv1 RINGv domain protein (rCgE3Rv1-RINGv) was confirmed to activate the Ub reaction system in vitro with the aid of Ub-activating enzyme El and Ub-conjugating enzyme E2. These results demonstrated that CgE3Rv1 was an Ub-protein ligase E3, which was involved in the immune response against LPS and the interaction with cell surface signal molecules of neuroendocrine-immune system in ... |
format |
Article in Journal/Newspaper |
author |
Cheng, Qi Wang, Hao Jiang, Shuai Wang, Lingling Xin, Lusheng Liu, Conghui Jia, Zhihao Song, Linsheng Zhu, Beiwei |
author_facet |
Cheng, Qi Wang, Hao Jiang, Shuai Wang, Lingling Xin, Lusheng Liu, Conghui Jia, Zhihao Song, Linsheng Zhu, Beiwei |
author_sort |
Cheng, Qi |
title |
A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
title_short |
A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
title_full |
A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
title_fullStr |
A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
title_full_unstemmed |
A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas |
title_sort |
novel ubiquitin-protein ligase e3 functions as a modulator of immune response against lipopolysaccharide in pacific oyster, crassostrea gigas |
publishDate |
2016 |
url |
http://ir.qdio.ac.cn/handle/337002/131017 https://doi.org/10.1016/j.dci.2016.02.027 |
geographic |
Pacific |
geographic_facet |
Pacific |
genre |
Crassostrea gigas Pacific oyster |
genre_facet |
Crassostrea gigas Pacific oyster |
op_relation |
DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY Cheng, Qi,Wang, Hao,Jiang, Shuai,et al. A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas[J]. DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,2016,60:180-190. http://ir.qdio.ac.cn/handle/337002/131017 doi:10.1016/j.dci.2016.02.027 |
op_doi |
https://doi.org/10.1016/j.dci.2016.02.027 |
container_title |
Developmental & Comparative Immunology |
container_volume |
60 |
container_start_page |
180 |
op_container_end_page |
190 |
_version_ |
1766393618142068736 |