ArticleJournal of virology2005
Identification of residues in the hepatitis C virus core protein that are critical for capsid assembly in a cell-free system.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 27 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed.
- Cell-Free Gene Expression: Methods and Applications.Chemical reviews · 2025Review
- Selective Depletion of ZAP-Binding CpG Motifs in HCV Evolution.Pathogens (Basel, Switzerland) · 2022Article
- Activation of the CaViruses · 2022Article
- Hepatitis C Virus Uses Host Lipids to Its Own Advantage.Metabolites · 2021Review
- Nanosized Particles Assembled by a Recombinant Virus Protein Are Able to Encapsulate Negatively Charged Molecules and Structured RNA.Polymers · 2021Article
- Identification of an Antiretroviral Small Molecule That Appears To Be a Host-Targeting Inhibitor of HIV-1 Assembly.Journal of virology · 2021Article
- The acidic domain of the hepatitis C virus NS4A protein is required for viral assembly and envelopment through interactions with the viral E1 glycoprotein.PLoS pathogens · 2019Article
- Biochemical and biophysical characterization of cell-free synthesized Rift Valley fever virus nucleoprotein capsids enables in vitro screening to identify novel antivirals.Biology direct · 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
- A rapid, low-cost quantitative diagnostic method for hepatitis C virus infection using capillary zone electrophoresis.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2014Article
- Relationship between humoral response against hepatitis C virus and disease overcome.SpringerPlus · 2014Article
- HCV core residues critical for infectivity are also involved in core-NS5A complex formation.PloS one · 2014Article
- Host-rabies virus protein-protein interactions as druggable antiviral targets.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Morphogenesis of infectious hepatitis C virus particles.Frontiers in microbiology · 2012Article
- Article
- A genetic interaction between the core and NS3 proteins of hepatitis C virus is essential for production of infectious virus.Journal of virology · 2011Article
- Novel mutations in a tissue culture-adapted hepatitis C virus strain improve infectious-virus stability and markedly enhance infection kinetics.Journal of virology · 2011Article
- Article
- Identification of basic amino acids at the N-terminal end of the core protein that are crucial for hepatitis C virus infectivity.Journal of virology · 2010Article
Corrections and comments
- Erratum issued
Authors and funding
3 authors.
Funding
Abstract
Significant advances have been made in understanding hepatitis C virus (HCV) replication through development of replicon systems. However, neither replicon systems nor standard cell culture systems support significant assembly of HCV capsids, leaving a large gap in our knowledge of HCV virion formation. Recently, we established a cell-free system in which over 60% of full-length HCV core protein synthesized de novo in cell extracts assembles into HCV capsids by biochemical and morphological criteria. Here we used mutational analysis to identify residues in HCV core that are important for capsid assembly in this highly reproducible cell-free system. We found that basic residues present in two clusters within the N-terminal 68 amino acids of HCV core played a critical role, while the uncharged linker domain between them was not. Furthermore, the aspartate at position 111, the region spanning amino acids 82 to 102, and three serines that are thought to be sites of phosphorylation do not appear to be critical for HCV capsid formation in this system. Mutation of prolines important for targeting of core to lipid droplets also failed to alter HCV capsid assembly in the cell-free system. In addition, wild-type HCV core did not rescue assembly-defective mutants. These data constitute the first systematic and quantitative analysis of the roles of specific residues and domains of HCV core in capsid formation.
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