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Seneca valley virus 3C protease blocks EphA2-Mediated mTOR activation to facilitate viral replication

文献类型： 外文期刊

作者： Shi, Yongyan 1 ; Wu, Zhi 1 ; Zeng, Penghui 1 ; Song, Jiangwei 3 ; Guo, Jinshuo 1 ; Yang, Xiaoyu 1 ; Zhou, Jianwei 1 ; Liu, Jue 1 ; Hou, Lei 1 ;

作者机构： 1.Yangzhou Univ, Coll Vet Med, Yangzhou, Peoples R China

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

3.Beijing Acad Agr & Forestry Sci, Inst Anim Husb & Vet Med, Beijing Key Lab Prevent & Control Infect Dis Lives, Beijing, Peoples R China

4.Yangzhou Univ, Coll Vet Med, Dept Prevent Vet Med, 48 Wenhui Rd, Yangzhou 225009, Peoples R China

关键词： Seneca valley virus (SVV); Eph receptor A2 (EphA2); 3C protease(3C(pro)); Proteolysis; mTOR pathway

期刊名称：MICROBIAL PATHOGENESIS （ 影响因子：3.3； 五年影响因子：3.6 ）

ISSN： 0882-4010

年卷期： 2024 年 191 卷

页码：

收录情况： SCI

摘要： The Seneca Valley virus (SVV) is a recently discovered porcine pathogen that causes vesicular diseases and poses a significant threat to the pig industry worldwide. Erythropoietin-producing hepatoma receptor A2 (EphA2) is involved in the activation of the AKT/mTOR signaling pathway, which is involved in autophagy. However, the regulatory relationship between SVV and EphA2 remains unclear. In this study, we demonstrated that EphA2 is proteolysed in SVV-infected BHK-21 and PK-15 cells. Overexpression of EphA2 significantly inhibited SVV replication, as evidenced by decreased viral protein expression, viral titers, and viral load, suggesting an antiviral function of EphA2. Subsequently, viral proteins involved in the proteolysis of EphA2 were screened, and the SVV 3C protease (3C(pro)) was found to be responsible for this cleavage, depending on its protease activity. However, the protease activity sites of 3C(pro) did not affect the interactions between 3C(pro) and EphA2. We further determined that EphA2 overexpression inhibited autophagy by activating the mTOR pathway and suppressing SVV replication. Taken together, these results indicate that SVV 3C(pro) targets EphA2 for cleavage to impair its EphA2mediated antiviral activity and emphasize the potential of the molecular interactions involved in developing antiviral strategies against SVV infection.

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