2. Academic Validation
  3. RSAD2 suppresses viral replication by interacting with the Senecavirus A 2 C protein

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

  • Vet Res. 2024 Sep 27;55(1):115. doi: 10.1186/s13567-024-01370-2.
Lei Hou # 1 2,  Zhi Wu # 3,  Penghui Zeng 4 5,  Xiaoyu Yang 4 5,  Yongyan Shi 4 5,  Jinshuo Guo 4 5,  Jianwei Zhou 4 5,  Jiangwei Song 6,  Jue Liu 7 8
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 Loudi Livestock, Aquaculture, and Agricultural Machinery Affairs Center, Loudi, China.
  • 4 College of Veterinary Medicine, Yangzhou University, Yangzhou, China.
  • 5 Jiangsu Co-Innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou, China.
  • 6 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.
  • 7 College of Veterinary Medicine, Yangzhou University, Yangzhou, China. liujue@263.net.
  • 8 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: 39334325 DOI: 10.1186/s13567-024-01370-2
Abstract

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.

Keywords

2 C protein; JAK-STAT pathway; RSAD2; SVA replication; interaction.

Figures
Products