南方科技大学知识苑(SUSTech KC): TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes

题名	TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes
作者	Zhou, Jian 1 ; Zhou, Yuzheng 1; Wei, Xia-Fei 1; Fan, Lujie 1,2; Gao, Xiang1 ; Li, Yunfei 1 ; Wu, Yezi 1 ; Feng, Wei1 ; Shen, XiaoTong1 ; Liu, Lei 1 ; Xu, Gang 3; Zhang, Zheng 1
通讯作者	Liu, Lei; Xu, Gang; Zhang, Zheng
发表日期	2024-03-01
DOI	10.1002/jmv.29531
发表期刊	JOURNAL OF MEDICAL VIROLOGY 影响因子和分区
ISSN	0146-6615
EISSN	1096-9071
卷号	96 期号:3
摘要	The Nucleocapsid Protein (NP) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is not only the core structural protein required for viral packaging, but also participates in the regulation of viral replication, and its post-translational modifications such as phosphorylation have been shown to be an important strategy for regulating virus proliferation. Our previous work identified NP could be ubiquitinated, as confirmed by two independent studies. But the function of NP ubiquitination is currently unknown. In this study, we first pinpointed TRIM6 as the E3 ubiquitin ligase responsible for NP ubiquitination, binding to NP's CTD via its RING and B-box-CCD domains. TRIM6 promotes the K29-typed polyubiquitination of NP at K102, K347, and K361 residues, increasing its binding to viral genomic RNA. Consistently, functional experiments such as the use of the reverse genetic tool trVLP model and gene knockout of TRIM6 further confirmed that blocking the ubiquitination of NP by TRIM6 significantly inhibited the proliferation of SARS-CoV-2. Notably, the NP of coronavirus is relatively conserved, and the NP of SARS-CoV can also be ubiquitinated by TRIM6, indicating that NP could be a broad-spectrum anti-coronavirus target. These findings shed light on the intricate interaction between SARS-CoV-2 and the host, potentially opening new opportunities for COVID-19 therapeutic development.
关键词	nucleocapsid protein SARS-CoV-2 TRIM6 ubiquitination
相关链接	[来源记录]
收录类别	SCI
语种	英语
学校署名	第一 ; 通讯
资助项目	National Key Research and Development Program of China["2021YFA0910900","2021YFC2300100"] ; National Science Fund for Distinguished Young Scholars[82025022] ; National Natural Science Foundation of China["82151212","92369109"] ; China Postdoctoral Science Foundation[2023M731520] ; Guangdong Science and Technology Plan Project[2021B1212030010] ; Shenzhen Science and Technology Program[JCYJ20220818103017036] ; Natural Science Research Project of Anhui Educational Committee[2022AH030080]
WOS研究方向	Virology
WOS类目	Virology
WOS记录号	WOS:001275712800052
出版者	WILEY
ESI学科分类	MICROBIOLOGY
来源库	Web of Science
引用统计	被引频次[WOS]：2
成果类型	期刊论文
条目标识符	http://sustech.caswiz.com/handle/2SGJ60CL/804691
专题	南方科技大学医学院南方科技大学第一附属医院南方科技大学第二附属医院
作者单位	1.Southern Univ Sci & Technol, Shenzhen Peoples Hosp 3, Inst Hepatol,Affiliated Hosp 2, Sch Med,Natl Clin Res Ctr Infect Dis, Shenzhen, Guangdong, Peoples R China 2.Guangzhou Med Univ, Guangzhou Lab, Guangzhou, Peoples R China 3.Anhui Med Univ, Sch Basic Med Sci, Dept Microbiol, Hefei, Peoples R China
第一作者单位	南方科技大学医学院; 南方科技大学第二附属医院; 南方科技大学第一附属医院
通讯作者单位	南方科技大学医学院; 南方科技大学第二附属医院; 南方科技大学第一附属医院
第一作者的第一单位	南方科技大学医学院; 南方科技大学第二附属医院; 南方科技大学第一附属医院
推荐引用方式 GB/T 7714	Zhou, Jian,Zhou, Yuzheng,Wei, Xia-Fei,et al. TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes[J]. JOURNAL OF MEDICAL VIROLOGY,2024,96(3).
APA	Zhou, Jian.,Zhou, Yuzheng.,Wei, Xia-Fei.,Fan, Lujie.,Gao, Xiang.,...&Zhang, Zheng.(2024).TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes.JOURNAL OF MEDICAL VIROLOGY,96(3).
MLA	Zhou, Jian,et al."TRIM6 facilitates SARS-CoV-2 proliferation by catalyzing the K29-typed ubiquitination of NP to enhance the ability to bind viral genomes".JOURNAL OF MEDICAL VIROLOGY 96.3(2024).