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

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

  • Vet Res. 2024 Dec 18;55(1):158. doi: 10.1186/s13567-024-01414-7.
Lei Hou # 1 2,  Penghui Zeng # 3 4,  Zhi Wu 3 4,  Xiaoyu Yang 3 4,  Jinshuo Guo 3 4,  Yongyan Shi 3 4,  Jiangwei Song 5,  Jianwei Zhou 3 4,  Jue Liu 6 7
Affiliations

Affiliations

  • 1 College of Veterinary Medicine, Yangzhou University, Yangzhou, China. hlbj09@163.com.
  • 2 Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou, China. hlbj09@163.com.
  • 3 College of Veterinary Medicine, Yangzhou University, Yangzhou, China.
  • 4 Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou, China.
  • 5 Beijing Key Laboratory for Prevention and Control of Infectious Diseases in Livestock and Poultry, Institute of Animal Husbandry and Veterinary Medicine, Beijing Academy of Agriculture and Forestry Sciences, Beijing, China.
  • 6 College of Veterinary Medicine, Yangzhou University, Yangzhou, China. liujue@263.net.
  • 7 Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou, China. liujue@263.net.
  • # Contributed equally.
PMID: 39695881 DOI: 10.1186/s13567-024-01414-7
Abstract

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.

Keywords

Hsp70; SVA L and 3D proteins; SVA replication; Substrate binding domain (SBD); stability.

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