Your browser doesn't support javascript.
loading
ASPP2 binds to hepatitis C virus NS5A protein via an SH3 domain/PxxP motif-mediated interaction and potentiates infection.
Smirnov, Artem; Magri, Andrea; Lotz, Rebecca; Han, Xiaoyue; Yin, Chunhong; Harris, Mark; Osterburg, Christian; Dötsch, Volker; McKeating, Jane A; Lu, Xin.
Affiliation
  • Smirnov A; Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, UK.
  • Magri A; Department of Experimental Medicine, TOR, University of Rome "Tor Vergata", Rome 00133, Italy.
  • Lotz R; Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7FZ, UK.
  • Han X; Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.
  • Yin C; Ludwig Institute for Cancer Research, Nuffield Department of Clinical Medicine, University of Oxford, Oxford OX3 7DQ, UK.
  • Harris M; School of Molecular and Cellular Biology, Faculty of Biological Sciences, and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
  • Osterburg C; Present address: State Key Laboratory of Virology, Wuhan Institute of Virology, Chinese Academy of Sciences, Wuhan, PR China.
  • Dötsch V; School of Molecular and Cellular Biology, Faculty of Biological Sciences, and Astbury Centre for Structural Molecular Biology, University of Leeds, Leeds, UK.
  • McKeating JA; Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.
  • Lu X; Institute of Biophysical Chemistry and Center for Biomolecular Magnetic Resonance, Goethe University, Frankfurt, Germany.
J Gen Virol ; 104(9)2023 09.
Article in En | MEDLINE | ID: mdl-37750869
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.
Subject(s)
Key words
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Hepatitis C / Hepacivirus Type of study: Prognostic_studies Limits: Humans Language: En Journal: J Gen Virol Year: 2023 Document type: Article Affiliation country: United kingdom
Fulltext
Add to My VHL
Print
XML
PubMed Links
Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Hepatitis C / Hepacivirus Type of study: Prognostic_studies Limits: Humans Language: En Journal: J Gen Virol Year: 2023 Document type: Article Affiliation country: United kingdom