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Heat shock protein 70 enhances viral replication by stabilizing Senecavirus A nonstructural proteins L and 3D

文献类型： 外文期刊

作者： Hou, Lei 1 ; Zeng, Penghui 1 ; Wu, Zhi 1 ; Yang, Xiaoyu 1 ; Guo, Jinshuo 1 ; Shi, Yongyan 1 ; Song, Jiangwei 3 ; Zhou, Jianwei 1 ; 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.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： Hsp70; SVA L and 3D proteins; stability; Substrate binding domain (SBD); SVA replication

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) is an emerging pathogen that causes idiopathic vesicular infections in pig herds, posing a potential threat to their production performance. Heat shock protein 70 (Hsp70) is a molecular chaperone that plays an important role in host homeostasis under both physiological and stress conditions. However, the effects of Hsp70 on SVA infection and its underlying regulatory mechanisms remain unclear. Here, we confirmed that Hsp70 expression promotes SVA infection, as evidenced by the expression of viral proteins, viral titers, and the number of rSVA-eGFP-infected cells. This positive regulatory role of Hsp70 is mainly involved in post-entry stages of SVA. Viral proteins that interacted with Hsp70 were screened, and co-immunoprecipitation (co-IP) shows an interaction between Hsp70 and SVA L and 3D proteins. Subsequently, we determined that the expression of Hsp70 is beneficial for the stability of the SVA L and 3D proteins. Additionally, the substrate-binding domain (SBD) of Hsp70 plays an important role in the interaction between Hsp70 and SVA L or 3D proteins; and the deletion of this domain results in the loss of the stabilizing effect of Hsp70 on SVA L and 3D proteins and the positive regulatory effect of Hsp70 on SVA replication. These results reveal that Hsp70 promotes SVA infection by stabilizing viral L and 3D proteins and provides a strategy for preventing and controlling SVA infection.

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