ArticleThe Journal of biological chemistry2012
Hepatitis C virus NS5B and host cyclophilin A share a common binding site on NS5A.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- A novel dimerization site in non-structural protein 5A of hepatitis C virus regulates viral replication fitness.PLoS pathogens · 2026Article
- Cyclophilin inhibition as a strategy for the treatment of human disease.Frontiers in pharmacology · 2024Review
- Cyclophilins and Their Roles in Hepatitis C Virus and Flavivirus Infections: Perspectives for Novel Antiviral Approaches.Pathogens (Basel, Switzerland) · 2021Review
- Hepatitis C Virus Replication.Cold Spring Harbor perspectives in medicine · 2020Review
- Cyclophilin A allows the allosteric regulation of a structural motif in the disordered domain 2 of NS5A and thereby fine-tunes HCV RNA replication.The Journal of biological chemistry · 2019Article
- Phosphorylated tyrosine 93 of hepatitis C virus nonstructural protein 5A is essential for interaction with host c-Src and efficient viral replication.The Journal of biological chemistry · 2019Article
- NMR and circular dichroism data for domain 2 of the HCV NS5A protein phosphorylated by the Casein Kinase II.Data in brief · 2018Article
- Interaction study between HCV NS5A-D2 and NS5B usingJournal of biomolecular NMR · 2018Article
- NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B.The Journal of biological chemistry · 2017Article
- Long Non-coding RNAs in Hepatitis C Virus-Infected Cells.Frontiers in microbiology · 2017Review
- Entangled in a membranous web: ER and lipid droplet reorganization during hepatitis C virus infection.Current opinion in cell biology · 2016Review
- Infection Counter: Automated Quantification of in Vitro Virus Replication by Fluorescence Microscopy.Viruses · 2016Article
- NMR Meets Tau: Insights into Its Function and Pathology.Biomolecules · 2016Review
- Chaperones in hepatitis C virus infection.World journal of hepatology · 2016Review
- Characterization of the Anti-HCV Activities of the New Cyclophilin Inhibitor STG-175.PloS one · 2016Article
- The Disordered Region of the HCV Protein NS5A: Conformational Dynamics, SH3 Binding, and Phosphorylation.Biophysical journal · 2015Article
- The yin and yang of hepatitis C: synthesis and decay of hepatitis C virus RNA.Nature reviews. Microbiology · 2015Review
- Combination of pharmacophore hypothesis and molecular docking to identify novel inhibitors of HCV NS5B polymerase.Molecular diversity · 2015Article
- Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Protein science : a publication of the Protein Society · 2015Article
- Resistance patterns associated with HCV NS5A inhibitors provide limited insight into drug binding.Viruses · 2014Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Nonstructural protein 5B (NS5B) is essential for hepatitis C virus (HCV) replication as it carries the viral RNA-dependent RNA polymerase enzymatic activity. HCV replication occurs in a membrane-associated multiprotein complex in which HCV NS5A and host cyclophilin A (CypA) have been shown to be present together with the viral polymerase. We used NMR spectroscopy to perform a per residue level characterization of the molecular interactions between the unfolded domains 2 and 3 of NS5A (NS5A-D2 and NS5A-D3), CypA, and NS5B(Δ21). We show that three regions of NS5A-D2 (residues 250-262 (region A), 274-287 (region B), and 306-333 (region C)) interact with NS5B(Δ21), whereas NS5A-D3 does not. We show that both NS5B(Δ21) and CypA share a common binding site on NS5A that contains residues Pro-306 to Glu-323. No direct molecular interaction has been detected by NMR spectroscopy between HCV NS5B(Δ21) and host CypA. We show that cyclosporine A added to a sample containing NS5B(Δ21), NS5A-D2, and CypA specifically inhibits the interaction between CypA and NS5A-D2 without altering the one between NS5A-D2 and NS5B(Δ21). A high quality heteronuclear NMR spectrum of HCV NS5B(Δ21) has been obtained and was used to characterize the binding site on the polymerase of NS5A-D2. Moreover these data highlight the potential of using NMR of NS5B(Δ21) as a powerful tool to characterize in solution the interactions of the HCV polymerase with all kinds of molecules (proteins, inhibitors, RNA). This work brings new insights into the comprehension of the molecular interplay between NS5B, NS5A, and CypA, three essentials proteins for HCV replication.
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