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Seneca Valley virus 3C(pro) degrades heterogeneous nuclear ribonucleoprotein A1 to facilitate viral replication

文献类型： 外文期刊

作者： Song, Jiangwei 1 ; Wang, Dan 1 ; Quan, Rong 1 ; Liu, Jue 2 ;

作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Anim Husb & Vet Med, Beijing Key Lab Prevent & Control Infect Dis Live, Beijing, Peoples R China

2.Yangzhou Univ, Coll Vet Med, Yangzhou, Jiangsu, Peoples R China

3.Yangzhou Univ, Jiangsu Coinnovat Ctr Prevent & Control Important, Yangzhou, Jiangsu, Peoples R China

关键词： Seneca valley virus (SVV); hnRNP A1; degradation; 3C protease; replication

期刊名称：VIRULENCE （ 影响因子：5.428； 五年影响因子：6.735 ）

ISSN： 2150-5594

年卷期： 2021 年 12 卷 1 期

页码：

收录情况： SCI

摘要： Seneca Valley virus (SVV) is a recently-identified important pathogen that is closely related to idiopathic vesicular disease in swine. Infection of SVV has been shown to induce a variety of cellular factors and their activations are essential for viral replication, but whether heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) involved in SVV replication is unknown. The cytoplasmic redistribution of hnRNP A1 is considered to play an important role in the virus life cycle. Here, we demonstrated that SVV infection can promote redistribution of the nucleocytoplasmic shuttling RNA-binding protein hnRNP A1 to the cytoplasm from the nucleus, whereas hnRNP A1 remained mainly in the nucleus of mock-infected cells. siRNA-mediated knockdown of the gene encoding hnRNP A1 attenuated viral replication as evidenced by decreased viral protein expression and virus production, whereas its overexpression enhanced replication. Moreover, infection with SVV induced the degradation of hnRNP A1, and viral 3 C protease (3 C-pro) was found to be responsible for its degradation and translocation. Further studies demonstrated that 3 C-pro induced hnRNP A1 degradation through its protease activity, via the proteasome pathway. This degradation could be attenuated by a proteasome inhibitor (MG132) and inactivation of the conserved catalytic box in 3 C-pro. Taken together, these results presented here reveal that SVV 3 C protease targets cellular hnRNP A1 for its degradation and translocation, which is utilized by SVV to aid viral replication, thereby highlighting the control potential of strategies for infection of SVV.

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