ArticleProceedings of the National Academy of Sciences of the United States of America2004
A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 79 citations in OpenAlex.
- A Molecular and Structural Perspective on Bluetongue Virus Entry and Assembly.Pathogens (Basel, Switzerland) · 2026Review
- Structural determinants of rotavirus proteolytic activation.PLoS pathogens · 2025Article
- The effect of pH on the structure of Bluetongue virus VP5.The Journal of general virology · 2024Article
- Article
- Comparative Virus-Host Protein Interactions of the Bluetongue Virus NS4 Virulence Factor.Viruses · 2022Article
- Mechanisms of Cell Entry by dsRNA Viruses: Insights for Efficient Delivery of dsRNA and Tools for Improved RNAi-Based Pest Control.Frontiers in physiology · 2021Review
- Differential Localization of Structural and Non-Structural Proteins during the Bluetongue Virus Replication Cycle.Viruses · 2020Article
- Review
- Novel Function of Bluetongue Virus NS3 Protein in Regulation of the MAPK/ERK Signaling Pathway.Journal of virology · 2019Article
- Mapping the pH Sensors Critical for Host Cell Entry by a Complex Nonenveloped Virus.Journal of virology · 2019Article
- Elucidating virus entry using a tetracysteine-tagged virus.Methods (San Diego, Calif.) · 2017Review
- Atomic model of a nonenveloped virus reveals pH sensors for a coordinated process of cell entry.Nature structural & molecular biology · 2016Article
- The requirement of environmental acidification for Ibaraki virus infection to host cells.The Journal of veterinary medical science · 2016Article
- Trafficking of bluetongue virus visualized by recovery of tetracysteine-tagged virion particles.Journal of virology · 2014Article
- Structural constraints in the packaging of bluetongue virus genomic segments.The Journal of general virology · 2014Article
- Bluetongue virus capsid assembly and maturation.Viruses · 2014Review
- The molecular biology of Bluetongue virus replication.Virus research · 2014Review
- Cellular phosphoinositides and the maturation of bluetongue virus, a non-enveloped capsid virus.Virology journal · 2013Article
- Structural insight into African horsesickness virus infection.Journal of virology · 2012Article
- Surface display of rice stripe virus NSvc2 and analysis of its membrane fusion activity.Virologica Sinica · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The outer capsid layer of Bluetongue virus, a member of the nonenveloped Reoviridae family, is composed of two proteins, a receptor-binding protein, VP2, and a second protein, VP5, which shares structural features with class I fusion proteins of enveloped viruses. In the replication cycle of Bluetongue virus VP5 acts as a membrane permeabilization protein that mediates release of viral particles from endosomal compartments into the cytoplasm. Here, we show that VP5 can also act as a fusion protein and induce syncytium formation when it is fused to a transmembrane anchor and expressed on the cell surface. Fusion activity is strictly pH-dependent and is triggered by short exposure to low pH. No cell-cell fusion is observed at neutral pH. Deletion of the first 40 amino acids, which can fold into two amphipathic helices, abolishes fusion activity. Syncytium formation by VP5 is inhibited in the presence of VP2 when it is expressed in a membrane-anchored form. The data indicate an interaction between the outer capsid protein VP2 and VP5 and show that VP5 undergoes pH-dependent conformational changes that render it capable of interacting with cellular membranes. More importantly, our data show that a membrane permeabilization protein of a nonenveloped virus can evolve into a fusion protein by the addition of an appropriate transmembrane anchor. The results strongly suggest that the mechanism of membrane permeabilization by VP5 and membrane fusion by viral fusion proteins require similar structural features and conformational changes.
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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.