The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP)
文献类型：期刊论文
| 作者 | Lu, Baojing1; Xie, Li3,4; Zheng, Zhenhua3; Miao, Yuanjiu3; Liu, Yan3; Zhang, Yuan3; Zheng, Caishang3; Ke, Xianliang3; Hu, Qinxue2; Wang, Hanzhong3 |
| 刊名 | JOURNAL OF GENERAL VIROLOGY
 |
| 出版日期 | 2018 |
| 卷号 | 99期号:1页码:73-85 |
| 关键词 | 3C enterovirus A71 zinc finger antiviral protein cleavage |
| ISSN号 | 0022-1317 |
| DOI | 10.1099/jgv.0.000982 |
| 英文摘要 | Enterovirus A71 (EV-A71) is a positive-strand RNA virus that causes hand-foot-mouth disease and neurological complications in children and infants. Although the underlying mechanisms remain to be further defined, impaired immunity is thought to play an important role. The host zinc-finger antiviral protein (ZAP), an IFN-stimulated gene product, has been reported to specifically inhibit the replication of certain viruses. However, whether ZAP restricts the infection of enteroviruses remains unknown. Here, we report that EV-A71 infection upregulates ZAP mRNA in RD and HeLa cells. Moreover, ZAP overexpression rendered 293T cells resistant to EV-A71 infection, whereas siRNA-mediated depletion of endogenous ZAP enhanced EV-A71 infection. The EV-A71 infection stimulated site-specific proteolysis of two ZAP isoforms, leading to the accumulation of a 40 kDa N-terminal ZAP fragment in virus-infected cells. We further revealed that the 3C protease (3Cpro) of EV-A71 mediates ZAP cleavage, which requires protease activity. Furthermore, ZAP variants with single amino acid substitutions at Gln-369 were resistant to 3Cpro cleavage, implying that Gln-369 is the sole cleavage site in ZAP. Moreover, although ZAP overexpression inhibited EV-A71 replication, the cleaved fragments did not show this effect. Our results indicate that an equilibrium between ZAP and enterovirus 3Cpro controls viral infection. The findings in this study suggest that viral 3Cpro mediated ZAP cleavage may represent a mechanism to escape host antiviral responses. |
| 资助项目 | National Natural Science Foundation of China (NSFC)[81371811] ; National Natural Science Foundation of China (NSFC)[81401658] |
| WOS研究方向 | Biotechnology & Applied Microbiology ; Virology |
| 语种 | 英语 |
| WOS记录号 | WOS:000431016500009 |
| 出版者 | MICROBIOLOGY SOC |
| 源URL | [http://202.127.146.157/handle/2RYDP1HH/5109]  |
| 专题 | 中国科学院武汉植物园 |
| 通讯作者 | Hu, Qinxue; Wang, Hanzhong |
| 作者单位 | 1.Anhui Med Univ, Sch Basic Med Sci, Dept Microbiol, Hefei 230032, Anhui, Peoples R China 2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430071, Hubei, Peoples R China 3.Chinese Acad Sci, Wuhan Inst Virol, Ctr Emerging Infect Dis, CAS Key Lab Special Pathogens & Biosafety, Wuhan, Hubei, Peoples R China 4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lu, Baojing,Xie, Li,Zheng, Zhenhua,et al. The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP)[J]. JOURNAL OF GENERAL VIROLOGY,2018,99(1):73-85. |
| APA | Lu, Baojing.,Xie, Li.,Zheng, Zhenhua.,Miao, Yuanjiu.,Liu, Yan.,...&Wang, Hanzhong.(2018).The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP).JOURNAL OF GENERAL VIROLOGY,99(1),73-85. |
| MLA | Lu, Baojing,et al."The 3C protease of enterovirus A71 counteracts the activity of host zinc-finger antiviral protein (ZAP)".JOURNAL OF GENERAL VIROLOGY 99.1(2018):73-85. |
入库方式： OAI收割
来源：武汉植物园
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