ArticleJournal of virology2004
Unique features of hepatitis C virus capsid formation revealed by de novo cell-free assembly.
Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
32 citing papers in PubMed.
- Development of Virus-Like Particles (VLPs) for Hepatitis C Virus genotype 4: a novel approach for vaccine development in Egypt.BMC biotechnology · 2025Article
- SARS-CoV-2: lessons from both the history of medicine and from the biological behavior of other well-known viruses.Future microbiology · 2021Review
- Identification of an Antiretroviral Small Molecule That Appears To Be a Host-Targeting Inhibitor of HIV-1 Assembly.Journal of virology · 2021Article
- Synthesis and Assembly of Hepatitis B Virus-Like Particles in aFrontiers in bioengineering and biotechnology · 2020Article
- A User's Guide to Cell-Free Protein Synthesis.Methods and protocols · 2019Review
- Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation.Frontiers in molecular biosciences · 2019Article
- Role of cleavage at the core-E1 junction of hepatitis C virus polyprotein in viral morphogenesis.PloS one · 2017Article
- Design of virus-based nanomaterials for medicine, biotechnology, and energy.Chemical Society reviews · 2016Review
- 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
- Identification of novel RNA secondary structures within the hepatitis C virus genome reveals a cooperative involvement in genome packaging.Scientific reports · 2016Article
- Coordination of Hepatitis C Virus Assembly by Distinct Regulatory Regions in Nonstructural Protein 5A.PLoS pathogens · 2016Article
- Host-rabies virus protein-protein interactions as druggable antiviral targets.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Virion assembly and release.Current topics in microbiology and immunology · 2013Review
- hepatitis c Virus p7 is critical for capsid assembly and envelopment.PLoS pathogens · 2013Article
- Morphogenesis of infectious hepatitis C virus particles.Frontiers in microbiology · 2012Article
- Dimerization-driven interaction of hepatitis C virus core protein with NS3 helicase.The Journal of general virology · 2011Article
- 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
- Core as a novel viral target for hepatitis C drugs.Viruses · 2010Article
- Characterization of hepatitis C virus core protein multimerization and membrane envelopment: revelation of a cascade of core-membrane interactions.Journal of virology · 2009Article
- Assembly of immature HIV-1 capsids using a cell-free system.Methods in molecular biology (Clifton, N.J.) · 2009Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors.
Funding
Abstract
The assembly of hepatitis C virus (HCV) is poorly understood, largely due to the lack of mammalian cell culture systems that are easily manipulated and produce high titers of virus. This problem is highlighted by the inability of the recently established HCV replicon systems to support HCV capsid assembly despite high levels of structural protein synthesis. Here we demonstrate that up to 80% of HCV core protein synthesized de novo in cell-free systems containing rabbit reticulocyte lysate or wheat germ extracts assembles into HCV capsids. This contrasts with standard primate cell culture systems, in which almost no core assembles into capsids. Cell-free HCV capsids, which have a sedimentation value of approximately 100S, have a buoyant density (1.28 g/ml) on cesium chloride similar to that of HCV capsids from other systems. Capsids produced in cell-free systems are also indistinguishable from capsids isolated from HCV-infected patient serum when analyzed by transmission electron microscopy. Using these cell-free systems, we show that HCV capsid assembly is independent of signal sequence cleavage, is dependent on the N terminus but not the C terminus of HCV core, proceeds at very low nascent chain concentrations, is independent of intact membrane surfaces, and is partially inhibited by cultured liver cell lysates. By allowing reproducible and quantitative assessment of viral and cellular requirements for capsid formation, these cell-free systems make a mechanistic dissection of HCV capsid assembly possible.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.