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RSAD2 suppresses viral replication by interacting with the Senecavirus A 2 C protein

文献类型： 外文期刊

作者： Hou, Lei 1 ; Wu, Zhi 3 ; Zeng, Penghui 1 ; Yang, Xiaoyu 1 ; Shi, Yongyan 1 ; Guo, Jinshuo 1 ; Zhou, Jianwei 1 ; Song, Jiangwei 4 ; Liu, Jue 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.Loudi Livestock Aquaculture & Agr Machinery Affair, Loudi, Peoples R China

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

关键词： RSAD2; SVA replication; interaction; 2 C protein; JAK-STAT pathway

期刊名称：VETERINARY RESEARCH （ 影响因子：3.5； 五年影响因子：4.0 ）

ISSN： 0928-4249

年卷期： 2024 年 55 卷 1 期

页码：

收录情况： SCI

摘要： Senecavirus A (SVA), an emerging virus that causes blisters on the nose and hooves, reduces the production performance of pigs. RSAD2 is a radical S-adenosylmethionine (SAM) enzyme, and its expression can suppress various viruses due to its broad antiviral activity. However, the regulatory relationship between SVA and RSAD2 and the mechanism of action remain unclear. Here, we demonstrated that SVA infection increased RSAD2 mRNA levels, whereas RSAD2 expression negatively regulated viral replication, as evidenced by decreased viral VP1 protein expression, viral titres, and infected cell numbers. Viral proteins that interact with RSAD2 were screened, and the interaction between the 2 C protein and RSAD2 was found to be stronger than that between other proteins. Additionally, amino acids (aa) 43-70 of RSAD2 were crucial for interacting with the 2 C protein and played an important role in its anti-SVA activity. RSAD2 was induced by type I interferon (IFN-I) via Janus kinase signal transducer and activator of transcription (JAK-STAT), and had antiviral activity. Ruxolitinib, a JAK-STAT pathway inhibitor, and the knockdown of JAK1 expression substantially reduced RSAD2 expression levels and antiviral activity. Taken together, these results revealed that RSAD2 blocked SVA infection by interacting with the viral 2 C protein and provide a strategy for preventing and controlling SVA infection.

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