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Journal of General Virology header logo Journal of General Virology

Volume 104, Issue 9

ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection Open Access

Abstract

Hepatitis C virus (HCV) infects millions of people worldwide and is a leading cause of liver disease. Despite recent advances in antiviral therapies, viral resistance can limit drug efficacy and understanding the mechanisms that confer viral escape is important. We employ an unbiased interactome analysis to discover host binding partners of the HCV non-structural protein 5A (NS5A), a key player in viral replication and assembly. We identify ASPP2, apoptosis-stimulating protein of p53, as a new host co-factor that binds NS5A via its SH3 domain. Importantly, silencing ASPP2 reduces viral replication and spread. Our study uncovers a previously unknown role for ASPP2 to potentiate HCV RNA replication.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): ASPP2 , HCV , infection , liver cancer , NS5A and viral replication
Funding
This study was supported by the:
  • Medical Research Foundation (Award MR/R022011/1)
    • Principle Award Recipient: JaneMcKeating
  • NIHR Oxford Biomedical Research Centre
    • Principle Award Recipient: XinLu
© 2023 The Authors
  • This is an open-access article distributed under the terms of the Creative Commons Attribution License. This article was made open access via a Publish and Read agreement between the Microbiology Society and the corresponding author’s institution.
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2023-09-26
2025-01-15
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ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection
J. Gen. Virol. 104, 001895 (2023); https://doi.org/10.1099/jgv.0.001895
/content/journal/jgv/10.1099/jgv.0.001895
/content/journal/jgv/10.1099/jgv.0.001895
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