ArticleJournal of virology2012
Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Anti-Hepatitis C Virus Activity of Uridine Derivatives of 2-Deoxy Sugars.Molecules (Basel, Switzerland) · 2018Article
- Novel Uridine Glycoconjugates, Derivatives of 4-Aminophenyl 1-Thioglycosides, as Potential Antiviral Compounds.Molecules (Basel, Switzerland) · 2018Article
- The role of PTEN - HCV core interaction in hepatitis C virus replication.Scientific reports · 2017Article
- 17,β-estradiol inhibits hepatitis C virus mainly by interference with the release phase of its life cycle.Liver international : official journal of the International Association for the Study of the Liver · 2017Article
- Exploration of acetanilide derivatives of 1-(ω-phenoxyalkyl)uracils as novel inhibitors of Hepatitis C Virus replication.Scientific reports · 2016Article
- Coevolution analysis of Hepatitis C virus genome to identify the structural and functional dependency network of viral proteins.Scientific reports · 2016Article
- Intrinsic disorder mediates hepatitis C virus core-host cell protein interactions.Protein science : a publication of the Protein Society · 2015Article
- HCV core protein and virus assembly: what we know without structures.Immunologic research · 2014Review
- HCV core residues critical for infectivity are also involved in core-NS5A complex formation.PloS one · 2014Article
- A Metabolomics Profiling Study in Hand-Foot-and-Mouth Disease and Modulated Pathways of Clinical Intervention Using Liquid Chromatography/Quadrupole Time-of-Flight Mass Spectrometry.Evidence-based complementary and alternative medicine : eCAM · 2013Article
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Authors and funding
7 authors.
Funding
Abstract
Hepatitis C virus core protein forms the viral nucleocapsid and plays a critical role in the formation of infectious particles. In this study, we demonstrate that the highly conserved residue G33, located within domain 1 of the core protein, is important for the production of cell culture-infectious virus (HCVcc). Alanine substitution at this position in the JFH1 genome did not alter viral RNA replication but reduced infectivity by ∼2 logs. Virus production by this core mutant could be rescued by compensatory mutations located immediately upstream and downstream of the original G33A mutation. The examination of the helix-loop-helix motif observed in the core protein structure (residues 15 to 41; Protein Data Bank entry 1CWX) indicated that the residues G33 and F24 are in close contact with each other, and that the G33A mutation induces a steric clash with F24. Molecular simulations revealed that the compensatory mutations increase the helix-loop-helix flexibility, allowing rescue of the core active conformation required for efficient virus production. Taken together, these data highlight the plasticity of core domain 1 conformation and illustrate the relationship between its structural tolerance to mutations and virus infectivity.
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