Porcine reproductive and respiratory syndrome virus Nsp4 cleaves ZAP to antagonize its antiviral activity
文献类型： 外文期刊
作者： Zhao, Yongxiang 1 ; Song, Zhongbao 1 ; Bai, Juan 1 ; Liu, Xuewei 1 ; Nauwynck, Hans 3 ; Jiang, Ping 1 ;
作者机构： 1.Nanjing Agr Univ, Coll Vet Med, Key Lab Anim Dis Diagnost & Immunol,Minist Agr, MOE Int Joint Collaborat Res Lab Anim Hlth & Food, Nanjing 210095, Peoples R China
2.Jiangsu Acad Agr Sci, Inst Vet Med, Key Lab Vet Biol Engn & Technol, Minist Agr, Nanjing 210014, Peoples R China
3.Univ Ghent, Fac Vet Med, Lab Virol, Salisburylaan 133, B-9820 Merelbeke, Belgium
4.Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou, Jiangsu, Peoples R China
5.Fujian Agr & Forestry Univ, Coll Anim Sci, Key Lab Fujian Taiwan Anim Pathogen Biol, Fuzhou 350002, Fujian, Peoples R China
关键词： PRRSV; Nsp4; Antagonize; ZAP; Antiviral activity
期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.293； 五年影响因子：3.599 ）
ISSN： 0378-1135
年卷期： 2020 年 250 卷
页码：
收录情况： SCI
摘要： Porcine reproductive and respiratory syndrome virus (PRRSV) is one of the most economically important pathogens impacting the global swine industry. PRRSV has been recognized to modulate the host immune response through a number of mechanisms. In our previous study, we found that over-expression of ZAP, a zinc finger antiviral protein of host, could suppress PRRSV replication, but how PRRSV escape the restriction of ZAP under natural conditions was still unknown. In this study, We found PRRSV infection significantly down-regulate the endogenous ZAP protein expression in Marc-145 cells. And PRRSV nonstructural protein 4 (Nsp4), a 3C-like serine proteinase, was screened to be responsible for ZAP reduction. Nsp4 could cleave ZAP, depending on its protease activity. The anti-PRRSV activity of ZAP was antagonized by Nsp4 in Marc-145 cells. In addition, we identified a unique amino acid, serine 180 of Nsp4 was required for efficient degradation of ZAP, and the mutation at residue 180 could decrease the ability of recombinant PRRSV to degrade ZAP. Those findings reveal a manner of PRRSV Nsp4 antagonizing the antiviral activity of ZAP, and shed light on a new strategy evolved by PRRSV to escape the host defense.
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