ArticleJournal of virology2010
Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- Comparative Analysis of Hepatitis C Virus NS5A Dynamics and Localization in Assembly-Deficient Mutants.Pathogens (Basel, Switzerland) · 2021Article
- Functional Study of the C-Terminal Part of the Hepatitis C Virus E1 Ectodomain.Journal of virology · 2018Article
- The role of PTEN - HCV core interaction in hepatitis C virus replication.Scientific reports · 2017Article
- Identification of Novel Functions for Hepatitis C Virus Envelope Glycoprotein E1 in Virus Entry and Assembly.Journal of virology · 2017Article
- Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A.PLoS pathogens · 2016Article
- Polyphenols Inhibit Hepatitis C Virus Entry by a New Mechanism of Action.Journal of virology · 2015Article
- Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Journal of virology · 2015Article
- HCV core protein and virus assembly: what we know without structures.Immunologic research · 2014Review
- Hepatitis C virus capsid protein and intracellular lipids interplay and its association with hepatic steatosis.Hepatitis monthly · 2014Article
- Inhibition of hepatitis C virus in chimeric mice by short synthetic hairpin RNAs: sequence analysis of surviving virus shows added selective pressure of combination therapy.Journal of virology · 2014Article
- Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Viruses · 2014Review
- HCV core residues critical for infectivity are also involved in core-NS5A complex formation.PloS one · 2014Article
- The antimalarial ferroquine is an inhibitor of hepatitis C virus.Hepatology (Baltimore, Md.) · 2013Article
- Hepatitis C virus replication and Golgi function in brefeldin a-resistant hepatoma-derived cells.PloS one · 2013Article
- Bidirectional lipid droplet velocities are controlled by differential binding strengths of HCV core DII protein.PloS one · 2013Article
- Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein.FEBS letters · 2012Article
- Strong correlation between liver and serum levels of hepatitis C virus core antigen and RNA in chronically infected patients.Journal of clinical microbiology · 2012Article
- Morphogenesis of infectious hepatitis C virus particles.Frontiers in microbiology · 2012Article
- Conserved glycine 33 residue in flexible domain I of hepatitis C virus core protein is critical for virus infectivity.Journal of virology · 2012Article
- A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus.Journal of virology · 2011Article
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Authors and funding
8 authors at 5 institutions in 1 country.
Funding
Abstract
A major function of the hepatitis C virus (HCV) core protein is the interaction with genomic RNA to form the nucleocapsid, an essential component of the virus particle. Analyses to identify basic amino acid residues of HCV core protein, important for capsid assembly, were initially performed with a cell-free system, which did not indicate the importance of these residues for HCV infectivity. The development of a cell culture system for HCV (HCVcc) allows a more precise analysis of these core protein amino acids during the HCV life cycle. In the present study, we used a mutational analysis in the context of the HCVcc system to determine the role of the basic amino acid residues of the core protein in HCV infectivity. We focused our analysis on basic residues located in two clusters (cluster 1, amino acids [aa]6 to 23; cluster 2, aa 39 to 62) within the N-terminal 62 amino acids of the HCV core protein. Our data indicate that basic residues of the first cluster have little impact on replication and are dispensable for infectivity. Furthermore, only four basic amino acids residues of the second cluster (R50, K51, R59, and R62) were essential for the production of infectious viral particles. Mutation of these residues did not interfere with core protein subcellular localization, core protein-RNA interaction, or core protein oligomerization. Moreover, these mutations had no effect on core protein envelopment by intracellular membranes. Together, these data indicate that R50, K51, R59, and R62 residues play a major role in the formation of infectious viral particles at a post-nucleocapsid assembly step.
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