ArticleNature microbiology2021
Bluetongue virus capsid protein VP5 perforates membranes at low endosomal pH during viral entry.
Article in Nature microbiology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 32 citations in OpenAlex.
- A Molecular and Structural Perspective on Bluetongue Virus Entry and Assembly.Pathogens (Basel, Switzerland) · 2026Review
- Bluetongue in the Mediterranean Basin: An Overview of Recent Hotspots and Advances in Vaccine Technologies.Microorganisms · 2026Review
- Viral Capsid-Membrane Interactions Propel Non-Brownian Movements of Non-enveloped Reoviruses during Entry.bioRxiv : the preprint server for biology · 2026Article
- Pathogen-Mediated Cell Fusion and Actin Cytoskeleton.Advances in experimental medicine and biology · 2026Review
- Functional diversity in GII.4 norovirus entry: HBGA binding and capsid clustering dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Bluetongue in ruminants: Global epidemiology, pathogenesis, and advances in diagnostic and control strategies within a One Health framework.Veterinary world · 2025Review
- Cholesterol-Dependent Membrane Deformation by Metastable Viral Capsids Facilitates Entry.ACS infectious diseases · 2024Article
- The effect of pH on the structure of Bluetongue virus VP5.The Journal of general virology · 2024Article
- Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to Ca2.PLoS pathogens · 2024Article
- Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes.Nature communications · 2024Article
- Molecular basis for the different PCV2 susceptibility of T-lymphoblasts in Landrace and Piétrain pigs.Veterinary research · 2024Article
- The rotavirus VP5*/VP8* conformational transition permeabilizes membranes to CabioRxiv : the preprint server for biology · 2023Article
- Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023Review
- Increased Clinical Signs and Mortality in IFNARPathogens (Basel, Switzerland) · 2023Article
- Identification of Orbivirus Non-Structural Protein 5 (NS5), Its Role and Interaction with RNA/DNA in Infected Cells.International journal of molecular sciences · 2023Article
- Recent advances in infectious disease research using cryo-electron tomography.Frontiers in molecular biosciences · 2023Review
- The Art of Viral Membrane Fusion and Penetration.Sub-cellular biochemistry · 2023Article
- Using cryoEM and cryoET to visualize membrane penetration of a non-enveloped virus.STAR protocols · 2022Article
- Non-enveloped virus membrane penetration: New advances leading to new insights.PLoS pathogens · 2022Article
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5 authors at 2 institutions in 2 countries.
Funding
Abstract
Bluetongue virus (BTV) is a non-enveloped virus and causes substantial morbidity and mortality in ruminants such as sheep. Fashioning a receptor-binding protein (VP2) and a membrane penetration protein (VP5) on the surface, BTV releases its genome-containing core (VP3 and VP7) into the host cell cytosol after perforation of the endosomal membrane. Unlike enveloped ones, the entry mechanisms of non-enveloped viruses into host cells remain poorly understood. Here we applied single-particle cryo-electron microscopy, cryo-electron tomography and structure-guided functional assays to characterize intermediate states of BTV cell entry in endosomes. Four structures of BTV at the resolution range of 3.4-3.9 Å show the different stages of structural rearrangement of capsid proteins on exposure to low pH, including conformational changes of VP5, stepwise detachment of VP2 and a small shift of VP7. In detail, sensing of the low-pH condition by the VP5 anchor domain triggers three major VP5 actions: projecting the hidden dagger domain, converting a surface loop to a protonated β-hairpin that anchors VP5 to the core and stepwise refolding of the unfurling domains into a six-helix stalk. Cryo-electron tomography structures of BTV interacting with liposomes show a length decrease of the VP5 stalk from 19.5 to 15.5 nm after its insertion into the membrane. Our structures, functional assays and structure-guided mutagenesis experiments combined indicate that this stalk, along with dagger domain and the WHXL motif, creates a single pore through the endosomal membrane that enables the viral core to enter the cytosol. Our study unveils the detailed mechanisms of BTV membrane penetration and showcases general methods to study cell entry of other non-enveloped viruses.
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