ArticleCell2010
3.3 A cryo-EM structure of a nonenveloped virus reveals a priming mechanism for cell entry.
Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.
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Who cites it
164 citing papers in PubMed.
- Temperature-modulated persistent dsRNA phage infection selectively excludes superinfection and promotes generation of new viral variants.Microbiology spectrum · 2026Article
- Sialic acid serves as a functional receptor for grass carp reovirus.PLoS pathogens · 2025Article
- Progress in the development of an ultrafast pulsed ponderomotive phase plate for cryo-electron tomography.Structural dynamics (Melville, N.Y.) · 2025Article
- Heterogeneous Condensation on Simplified Viral Envelope Protein Structures.ACS applied materials & interfaces · 2025Article
- Characterization and Immune Functions of LcβLectin from Large Yellow Croaker (International journal of molecular sciences · 2025Article
- Autoproteolytic mechanism of CdiA toxin release reconstitutedJournal of bacteriology · 2024Article
- Liquid-liquid phase separation is essential for reovirus viroplasm formation and immune evasion.Journal of virology · 2024Article
- AI analysis of super-resolution microscopy: Biological discovery in the absence of ground truth.The Journal of cell biology · 2024Review
- Cryo-EM structures of Banna virus in multiple states reveal stepwise detachment of viral spikes.Nature communications · 2024Article
- Essential autoproteolysis of bacterial anti-σ factor RsgI for transmembrane signal transduction.Science advances · 2023Article
- An Aquareovirus Exploits Membrane-Anchored HSP70 To Promote Viral Entry.Microbiology spectrum · 2023Article
- The structure of a 12-segmented dsRNA reovirus: New insights into capsid stabilization and organization.PLoS pathogens · 2023Article
- An aquatic virus exploits the IL6-STAT3-HSP90 signaling axis to promote viral entry.PLoS pathogens · 2023Article
- Grass Carp Reovirus Induces Formation of Lipid Droplets as Sites for Its Replication and Assembly.mBio · 2022Article
- In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Atomic model of vesicular stomatitis virus and mechanism of assembly.Nature communications · 2022Article
- Cryo-EM structure-based selection of computed ligand poses enables design of MTA-synergic PRMT5 inhibitors of better potency.Communications biology · 2022Article
- AlphaFold2 and CryoEM: Revisiting CryoEM modeling in near-atomic resolution density maps.iScience · 2022Article
- Molecular Characterization of Outer Capsid Proteins VP5 and VP7 of Grass Carp Reovirus.Viruses · 2022Article
- Identification and establishment of type IV interferon and the characterization of interferon-υ including its class II cytokine receptors IFN-υR1 and IL-10R2.Nature communications · 2022Article
104 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors.
Funding
Abstract
To achieve cell entry, many nonenveloped viruses must transform from a dormant to a primed state. In contrast to the membrane fusion mechanism of enveloped viruses (e.g., influenza virus), this membrane penetration mechanism is poorly understood. Here, using single-particle cryo-electron microscopy, we report a 3.3 A structure of the primed, infectious subvirion particle of aquareovirus. The density map reveals side-chain densities of all types of amino acids (except glycine), enabling construction of a full-atom model of the viral particle. Our structure and biochemical results show that priming involves autocleavage of the membrane penetration protein and suggest that Lys84 and Glu76 may facilitate this autocleavage in a nucleophilic attack. We observe a myristoyl group, covalently linked to the N terminus of the penetration protein and embedded in a hydrophobic pocket. These results suggest a well-orchestrated process of nonenveloped virus entry involving autocleavage of the penetration protein prior to exposure of its membrane-insertion finger.
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