ArticleThe Journal of general virology2011
The subcellular localization of the hepatitis C virus non-structural protein NS2 is regulated by an ion channel-independent function of the p7 protein.
Article in The Journal of general virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
What it found
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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.
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Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Advances in Viroporin Function and Structure: A Comparative Analysis of Alphavirus 6K with Well-Characterized Viroporins.Viruses · 2025Review
- Requirement of a functional ion channel for Sindbis virus glycoprotein transport, CPV-II formation, and efficient virus budding.PLoS pathogens · 2022Article
- Hepatitis C Virus p7 Induces Membrane Permeabilization by Interacting with Phosphatidylserine.International journal of molecular sciences · 2020Article
- Palmitoylation of Hepatitis C Virus NS2 Regulates Its Subcellular Localization and NS2-NS3 Autocleavage.Journal of virology · 2019Article
- Article
- The amino-terminus of the hepatitis C virus (HCV) p7 viroporin and its cleavage from glycoprotein E2-p7 precursor determine specific infectivity and secretion levels of HCV particle types.PLoS pathogens · 2017Article
- Classical swine fever virus nonstructural protein p7 modulates infectious virus production.Scientific reports · 2017Article
- Hepatitis C Virus-Induced Rab32 Aggregation and Its Implications for Virion Assembly.Journal of virology · 2017Article
- Release of Infectious Hepatitis C Virus from Huh7 Cells Occurs via a trans-Golgi Network-to-Endosome Pathway Independent of Very-Low-Density Lipoprotein Secretion.Journal of virology · 2016Article
- Targeting the Channel Activity of Viroporins.Advances in protein chemistry and structural biology · 2016Review
- Identification of a lead like inhibitor of the hepatitis C virus non-structural NS2 autoprotease.Antiviral research · 2015Article
- Review
- Review
- Detergent-resistant membrane association of NS2 and E2 during hepatitis C virus replication.Journal of virology · 2015Article
- Computational Docking Study of p7 Ion Channel from HCV Genotype 3 and Genotype 4 and Its Interaction with Natural Compounds.PloS one · 2015Article
- NS2 is dispensable for efficient assembly of hepatitis C virus-like particles in a bipartite trans-encapsidation system.The Journal of general virology · 2014Article
- The elusive function of the hepatitis C virus p7 protein.Virology · 2014Review
- The intraviral protein interaction network of hepatitis C virus.Molecular & cellular proteomics : MCP · 2014Article
- Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release.Hepatology (Baltimore, Md.) · 2014Article
- Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The hepatitis C virus (HCV) p7 ion channel and non-structural protein 2 (NS2) are both required for efficient assembly and release of nascent virions, yet precisely how these proteins are able to influence this process is unclear. Here, we provide both biochemical and cell biological evidence for a functional interaction between p7 and NS2. We demonstrate that in the context of a genotype 1b subgenomic replicon the localization of NS2 is affected by the presence of an upstream p7 with its cognate signal peptide derived from the C terminus of E2 (SPp7). Immunofluorescence analysis revealed that the presence of SPp7 resulted in the targeting of NS2 to sites closely associated with viral replication complexes. In addition, biochemical analysis demonstrated that, in the presence of SPp7, a significant proportion of NS2 was found in a detergent (Triton X-100)-insoluble fraction, which also contained a marker of detergent resistant rafts. In contrast, in replicons lacking p7, NS2 was entirely detergent soluble and the altered localization was lost. Furthermore, we found that serine 168 within NS2 was required for its localization adjacent to replication complexes, but not for its accumulation in the detergent-insoluble fraction. NS2 physically interacted with NS5A and this interaction was dependent on both p7 and serine 168 within NS2. Mutational and pharmacological analyses demonstrated that these effects were not a consequence of p7 ion channel function, suggesting that p7 possesses an alternative function that may influence the coordination of virus genome replication and particle assembly.
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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.