ArticleProceedings of the National Academy of Sciences of the United States of America2009
The 3-dimensional structure of a hepatitis C virus p7 ion channel by electron microscopy.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers.
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Who cites it
82 citing papers in PubMed.
- 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
- Protein-driven membrane remodeling: Molecular perspectives from Flaviviridae infections.Biophysical journal · 2023Review
- The envelope proteins from SARS-CoV-2 and SARS-CoV potently reduce the infectivity of human immunodeficiency virus type 1 (HIV-1).Retrovirology · 2022Article
- SARS-CoV-2 Envelope Protein Forms Clustered Pentamers in Lipid Bilayers.Biochemistry · 2022Article
- Requirement of a functional ion channel for Sindbis virus glycoprotein transport, CPV-II formation, and efficient virus budding.PLoS pathogens · 2022Article
- 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
- Identification of a novel class of cyclic penta-peptides against hepatitis C virus as p7 channel blockers.Computational and structural biotechnology journal · 2022Article
- Lagovirus Non-structural Protein p23: A Putative Viroporin That Interacts With Heat Shock Proteins and Uses a Disulfide Bond for Dimerization.Frontiers in microbiology · 2022Article
- Review
- Inhibitor Development against p7 Channel in Hepatitis C Virus.Molecules (Basel, Switzerland) · 2021Article
- Article
- Review
- Porcine deltacoronavirus (PDCoV) modulates calcium influx to favor viral replication.Virology · 2020Article
- Critical Effect of the Detergent:Protein Ratio on the Formation of the Hepatitis C Virus p7 Channel.Biochemistry · 2019Review
- Hepatitis C virus sequence divergence preserves p7 viroporin structural and dynamic features.Scientific reports · 2019Article
- Re-evaluating the p7 viroporin structure.Nature · 2018Article
- The Good, the Bad, and the Shocking: The Multiple Roles of Dengue Virus Nonstructural Protein 1 in Protection and Pathogenesis.Annual review of virology · 2018Review
- Adaptive mutation F772S-enhanced p7-NS4A cooperation facilitates the assembly and release of hepatitis C virus and is associated with lipid droplet enlargement.Emerging microbes & infections · 2018Article
- Perturbations of Native Membrane Protein Structure in Alkyl Phosphocholine Detergents: A Critical Assessment of NMR and Biophysical Studies.Chemical reviews · 2018Review
22 more citing papers are in PubMed but not listed here.
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9 authors.
Funding
Abstract
Infection with the hepatitis C virus (HCV) has a huge impact on global health putting more than 170 million people at risk of developing severe liver disease. The HCV encoded p7 ion channel is essential for the production of infectious viruses. Despite a growing body of functional data, little is known about the 3-dimensional (3D) structure of the channel. Here, we present the 3D structure of a full-length viroporin, the detergent-solubilized hexameric 42 kDa form of the HCV p7 ion channel, as determined by single-particle electron microscopy using the random conical tilting approach. The reconstruction of such a small protein complex was made possible by a combination of high-contrast staining, the symmetry, and the distinct structural features of the channel. The orientation of the p7 monomers within the density was established using immunolabeling with N and C termini specific F(ab) fragments. The density map at a resolution of approximately 16 A reveals a flower-shaped protein architecture with protruding petals oriented toward the ER lumen. This broadest part of the channel presents a comparatively large surface area providing potential interaction sites for cellular and virally encoded ER resident proteins.
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