ArticlePLoS computational biology2012
The p7 protein of hepatitis C virus forms structurally plastic, minimalist ion channels.
Article in PLoS computational biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Lipid-driven alignment and binding of p7 dimers in early oligomer assembly.PLoS computational biology · 2025Article
- Lipid-Driven Alignment and Binding of p7 Dimers in Early Oligomer Assembly.bioRxiv : the preprint server for biology · 2025Article
- Highly versatile small virus-encoded proteins in cellular membranes: A structural perspective on how proteins' inherent conformational plasticity couples with host membranes' properties to control cellular processes.Journal of structural biology: X · 2025Article
- Activation of the CaViruses · 2022Article
- Viroporins: Structure, function, and their role in the life cycle of SARS-CoV-2.The international journal of biochemistry & cell biology · 2022Review
- Electrophysiological Properties from Computations at a Single Voltage: Testing Theory with Stochastic Simulations.Entropy (Basel, Switzerland) · 2021Article
- Article
- Review
- Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features.Scientific reports · 2019Article
- Emerging Diversity in Lipid-Protein Interactions.Chemical reviews · 2019Review
- All-atom virus simulations.Current opinion in virology · 2018Review
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
- The Unusual Transmembrane Partition of the Hexameric Channel of the Hepatitis C Virus.Structure (London, England : 1993) · 2018Article
- Symmetric dimeric adamantanes for exploring the structure of two viroporins: influenza virus M2 and hepatitis C virus p7.Drug design, development and therapy · 2018Article
- 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
- Coupling neutron reflectivity with cell-free protein synthesis to probe membrane protein structure in supported bilayers.Scientific reports · 2017Article
- Validity of the Electrodiffusion Model for Calculating Conductance of Simple Ion Channels.The journal of physical chemistry. B · 2017Article
- Viral channel forming proteins--How to assemble and depolarize lipid membranes in silico.Biochimica et biophysica acta · 2016Review
- Ion Channel Function and Cross-Species Determinants in Viral Assembly of Nonprimate Hepacivirus p7.Journal of virology · 2016Article
- The N-terminal Helical Region of the Hepatitis C Virus p7 Ion Channel Protein Is Critical for Infectious Virus Production.PLoS pathogens · 2015Article
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Authors and funding
4 authors.
Funding
Abstract
Hepatitis C virus (HCV) p7 is a membrane-associated oligomeric protein harboring ion channel activity. It is essential for effective assembly and release of infectious HCV particles and an attractive target for antiviral intervention. Yet, the self-assembly and molecular mechanism of p7 ion channelling are currently only partially understood. Using molecular dynamics simulations (aggregate time 1.2 µs), we show that p7 can form stable oligomers of four to seven subunits, with a bias towards six or seven subunits, and suggest that p7 self-assembles in a sequential manner, with tetrameric and pentameric complexes forming as intermediate states leading to the final hexameric or heptameric assembly. We describe a model of a hexameric p7 complex, which forms a transiently-open channel capable of conducting ions in simulation. We investigate the ability of the hexameric model to flexibly rearrange to adapt to the local lipid environment, and demonstrate how this model can be reconciled with low-resolution electron microscopy data. In the light of these results, a view of p7 oligomerization is proposed, wherein hexameric and heptameric complexes may coexist, forming minimalist, yet robust functional ion channels. In the absence of a high-resolution p7 structure, the models presented in this paper can prove valuable as a substitute structure in future studies of p7 function, or in the search for p7-inhibiting drugs.
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