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Abstract

Swine acute diarrhoea syndrome coronavirus (SADS-CoV) is an enveloped, single-stranded positive-sense RNA virus that causes acute diarrhoea and death in piglets, resulting in significant economic losses to the pig farming industry. Studying the interaction patterns between SADS-CoV and host proteins can provide guidance for the development of antiviral drugs. In previous work, we identified 289 host proteins interacting with the SADS-CoV M protein through glutathione S-transferase pull down combined with LC-MS/MS. Here, we focus on prohibitin (PHB), which is associated with the stability of mitochondrial function in cells, and demonstrate that there is a physical interaction and cellular co-localization relationship between the SADS-CoV M protein and PHB protein. Additionally, SADS-CoV-mediated infection has a strong correlation with PHB expression, and regulating PHB expression dose-dependently antagonizes SADS-CoV replication. Moreover, we discovered that PHB has an antagonistic effect on apoptosis induced by SADS-CoV infection. Overall, this work helps to elucidate the role of the PHB protein in the SADS-CoV life cycle, providing a potential target for antiviral research.

Funding
This study was supported by the:
  • Natural Science Foundation of Guangdong Province (Award 2020A1515010220)
    • Principal Award Recipient: JingyunMa
  • Science and Technology Program of Guangzhou City of China (Award 201904010433)
    • Principal Award Recipient: JingyunMa
  • Guangdong Major Project of Basic and Applied Basic Research (Award 2020B0301030007)
    • Principal Award Recipient: JingyunMa
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/content/journal/jgv/10.1099/jgv.0.002073
2025-02-11
2026-01-17

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