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Porcine epidemic diarrhea virus E protein suppresses RIG-I signaling-mediated interferon- ? production

文献类型： 外文期刊

作者： Zheng, Liang 1 ; Wang, Xianhe 3 ; Guo, Dexuan 3 ; Cao, Jinglong 3 ; Cheng, Lixin 3 ; Li, Xingzhi 3 ; Zou, Dehua 3 ; Zhang 1 ;

作者机构： 1.HeiLongJiang BaYi Agr Univ, Coll Anim Sci & Vet Med, Daqing 163319, Peoples R China

2.Chinese Acad Agr Sci, Harbin Vet Res Inst, State Key Lab Vet Biotechnol, Harbin 150069, Peoples R China

3.HeiLongJiang BaYi Agr Univ, Coll Life Sci & Technol, Daqing 163319, Peoples R China

4.HeiLongJiang BaYi Agr Univ, Biotechnol Ctr, Daqing 163319, Peoples R China

5.Harbin Med Univ, Affiliated Hosp 5, Dept Nephrol, Daqing 163319, Peoples R China

6.HeiLongJiang BaYi Agr Univ, Coll Sci, Daqing 163319, Peoples R China

7.HeiLongJiang Acad Agr Sci, Branch Anim Husb & Vet, Qiqihar 161005, Peoples R China

关键词： Porcine epidemic diarrhea virus; E protein; RIG-I signaling; IFN-? suppression; Innate immune evasion

期刊名称：VETERINARY MICROBIOLOGY （ 影响因子：3.03； 五年影响因子：2.923 ）

ISSN： 0378-1135

年卷期： 2021 年 254 卷

页码：

收录情况： SCI

摘要： Porcine epidemic diarrhea virus (PEDV) encodes many multifunctional proteins that inhibit host innate immune response during virus infection. As one of important structural proteins, PEDV E protein has been found to block the production of type I interferon (IFN) in virus life cycle, but little is known about this process that E protein subverts host innate immune. Thus, in this present study, we initiated the construction of eukaryotic expression vectors to express PEDV E protein. Subsequently, cellular localization analysis was performed and the results showed that the majority of PEDV E protein distributed at cytoplasm and localized in endoplasmic reticulum (ER). Over-expression of PEDV E protein significantly inhibited poly(I:C)-induced IFN-? and IFN-stimulated genes (ISGs) productions. We also found that PEDV E protein remarkably suppressed the protein expression of RIG-I signaling-associated molecules, but all their corresponding mRNA levels remained unaffected and unchanged. Furthermore, PEDV E protein obviously interfered with the translocation of IRF3 from cytoplasm to nucleus through direct interaction with IRF3, which is crucial for the IFN-? production induced by poly(I:C). Taken together, our results suggested that PEDV E protein acts as an IFN-? antagonist through suppression of the RIG-I-mediated signaling. This study will pave the way for the further investigation into the molecular mechanisms by which PEDV E protein evades host innate immune response.

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