ArticlePLoS biology2023
Structures of the Hepaci-, Pegi-, and Pestiviruses envelope proteins suggest a novel membrane fusion mechanism.
Article in PLoS biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 19 citations in OpenAlex.
- A structure-aware generative AI framework for revealing functional relationships in protein families.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structure-based design of stable recombinant hepatitis C virus E1E2 heterodimers.Nature communications · 2026Article
- Mapping Determinants of Hepatitis C Virus E1/E2 Transmembrane Interactions Using Intergenotypic Chimeras.Viruses · 2026Article
- Generation of a HiBiT-expressing recombinant rat hepacivirus supporting both in vivo and in vitro infection.PLoS pathogens · 2026Article
- Recent advances in the inference of deep viral evolutionary history.Journal of virology · 2025Review
- In vivo and in vitro recombinant systems of a novel variant demonstrate cross-reactive neutralization for the HCV model virus, Norway rat hepacivirus.PLoS pathogens · 2025Article
- A proteome-wide structural systems approach reveals insights into protein families of all human herpesviruses.Nature communications · 2024Article
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- Visualizing intermediate stages of viral membrane fusion by cryo-electron tomography.Trends in biochemical sciences · 2024Review
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- Article
- Determinants of pegivirus persistence, cross-species infection, and adaptation in the laboratory mouse.PLoS pathogens · 2024Article
- AlphaFold and Protein Folding: Not Dead Yet! The Frontier Is Conformational Ensembles.Annual review of biomedical data science · 2024Review
- A ~40-kb flavi-like virus does not encode a known error-correcting mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- GB Virus B and Hepatitis C Virus, Distantly Related Hepaciviruses, Share an Entry Factor, Claudin-1.Journal of virology · 2023Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Enveloped viruses encode specialised glycoproteins that mediate fusion of viral and host membranes. Discovery and understanding of the molecular mechanisms of fusion have been achieved through structural analyses of glycoproteins from many different viruses, and yet the fusion mechanisms of some viral genera remain unknown. We have employed systematic genome annotation and AlphaFold modelling to predict the structures of the E1E2 glycoproteins from 60 viral species in the Hepacivirus, Pegivirus, and Pestivirus genera. While the predicted structure of E2 varied widely, E1 exhibited a very consistent fold across genera, despite little or no similarity at the sequence level. Critically, the structure of E1 is unlike any other known viral glycoprotein. This suggests that the Hepaci-, Pegi-, and Pestiviruses may possess a common and novel membrane fusion mechanism. Comparison of E1E2 models from various species reveals recurrent features that are likely to be mechanistically important and sheds light on the evolution of membrane fusion in these viral genera. These findings provide new fundamental understanding of viral membrane fusion and are relevant to structure-guided vaccinology.
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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.