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A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas
Cheng, Qi1,4; Wang, Hao3; Jiang, Shuai3; Wang, Lingling2,3; Xin, Lusheng3; Liu, Conghui3; Jia, Zhihao3; Song, Linsheng2; Zhu, Beiwei1,4
2016-07-01
Source PublicationDEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY
Volume60Pages:180-190
SubtypeArticle
AbstractUbiquitination 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 oysters. (C) 2016 Elsevier Ltd. All rights reserved.
KeywordCrassostrea Gigas Ubiquitination Immune Response Lipopolysaccharide Stimulation Ub-protein Ligase E3
DOI10.1016/j.dci.2016.02.027
Indexed BySCI
Language英语
WOS IDWOS:000374613800018
Citation statistics
Document Type期刊论文
Version出版稿
Identifierhttp://ir.qdio.ac.cn/handle/337002/131017
Collection实验海洋生物学重点实验室
Affiliation1.Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China
2.Dalian Ocean Univ, Minist Agr, Key Lab Mariculture & Stock Enhancement North Chi, Dalian 116023, Peoples R China
3.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
4.Natl Engn Res Ctr Seafood, Dalian 116034, Peoples R China
Recommended Citation
GB/T 7714
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.
APA Cheng, Qi.,Wang, Hao.,Jiang, Shuai.,Wang, Lingling.,Xin, Lusheng.,...&Zhu, Beiwei.(2016).A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas.DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY,60,180-190.
MLA Cheng, Qi,et al."A novel ubiquitin-protein ligase E3 functions as a modulator of immune response against lipopolysaccharide in Pacific oyster, Crassostrea gigas".DEVELOPMENTAL AND COMPARATIVE IMMUNOLOGY 60(2016):180-190.
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