Trim14 inhibits hepatitis c virus infection by spry domain-dependent targeted degradation of the viral ns5a protein | |
Wang, Shanshan1,2,3,4,5; Chen, Yongzhi6,7; Li, Chunfeng3,4,5; Wu, Yaoxing1,2; Guo, Lei1,2; Peng, Changwei1,2; Huang, Yueping1,2; Cheng, Genhong3,4,5,6,8; Qin, F. Xiao-Feng1,2,3,4,5 | |
刊名 | Scientific reports
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2016-08-31 | |
卷号 | 6页码:12 |
ISSN号 | 2045-2322 |
DOI | 10.1038/srep32336 |
通讯作者 | Qin, f. xiao-feng(fqin1@foxmail.com) |
英文摘要 | Tripartite motif 14 (trim14) was reported to function as a mitochondrial signaling adaptor in mediating innate immune responses. however, the involvement of trim14 in host defense against viral infection and molecular mechanisms remain unclear. here, we demonstrated that enforced expression of trim14 could potently inhibit the infection and replication of hcv in hepatocytes, whereas trim14 knockout cells became more susceptible to hcv infection. interestingly, further experiments revealed that such anti-hcv activity was independent of activating the nf-kappa b or interferon pathways but required the c-terminal spry domain of no signaling capacity. in searching for mechanisms how trim14 exerts its antiviral function we found that trim14 interacted with hcv encoded non-structural protein ns5a and could strongly induce its degradation dependent on the ns5a1 subdomain. interestingly extensive domain mapping analyses revealed that ns5a degradation was mediated by the highly conserved spry domain of trim14, which might involve the k48 ubiquitination pathway. collectively, our work uncovered a new mechanism responsible for host defense against hcv infection, and could potentially aid the development of novel anti-hcv therapeutics. |
WOS关键词 | PATTERN-RECOGNITION RECEPTORS ; ZINC-BINDING DOMAIN ; DISTINCT MECHANISMS ; ANTIVIRAL RESPONSE ; INNATE IMMUNITY ; REPLICATION ; EXPRESSION ; EFFECTORS ; PATHWAYS ; FAMILY |
WOS研究方向 | Science & Technology - Other Topics |
WOS类目 | Multidisciplinary Sciences |
语种 | 英语 |
出版者 | NATURE PUBLISHING GROUP |
WOS记录号 | WOS:000382240400001 |
内容类型 | 期刊论文 |
URI标识 | http://www.corc.org.cn/handle/1471x/2375389 |
专题 | 中国科学院大学 |
通讯作者 | Qin, F. Xiao-Feng |
作者单位 | 1.Sun Yat Sen Univ, Sch Life Sci, Key Lab Gene Engn, Minist Educ, Guangzhou 510275, Guangdong, Peoples R China 2.Sun Yat Sen Univ, Sch Life Sci, State Key Lab Biocontrol, Guangzhou 510275, Guangdong, Peoples R China 3.Chinese Acad Med Sci, Inst Basic Med Sci, Ctr Syst Med, Beijing 100005, Peoples R China 4.Peking Union Med Coll, Beijing 100005, Peoples R China 5.Suzhou Inst Syst Med, Suzhou 215123, Jiangsu, Peoples R China 6.Chinese Acad Sci, Inst Biophys, CAS Key Lab Infect & Immun, Beijing, Peoples R China 7.Univ Chinese Acad Sci, Beijing, Peoples R China 8.Univ Calif Los Angeles, Dept Microbiol Immunol & Mol Genet, Los Angeles, CA 90095 USA |
推荐引用方式 GB/T 7714 | Wang, Shanshan,Chen, Yongzhi,Li, Chunfeng,et al. Trim14 inhibits hepatitis c virus infection by spry domain-dependent targeted degradation of the viral ns5a protein[J]. Scientific reports,2016,6:12. |
APA | Wang, Shanshan.,Chen, Yongzhi.,Li, Chunfeng.,Wu, Yaoxing.,Guo, Lei.,...&Qin, F. Xiao-Feng.(2016).Trim14 inhibits hepatitis c virus infection by spry domain-dependent targeted degradation of the viral ns5a protein.Scientific reports,6,12. |
MLA | Wang, Shanshan,et al."Trim14 inhibits hepatitis c virus infection by spry domain-dependent targeted degradation of the viral ns5a protein".Scientific reports 6(2016):12. |
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