ArticleNature communications2022
Multiple conformations of trimeric spikes visualized on a non-enveloped virus.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed, 11 citations in OpenAlex.
- Insect cypoviruses: advances in structural characterization, evolutionary genomics, and host interaction dynamics.Archives of virology · 2026Review
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- Crystal structure and nucleic acid binding mode of CPV NSP9: implications for viroplasm in Reovirales.Nucleic acids research · 2024Article
- Molecular Mechanism of pH-Induced Protrusion Configuration Switching in Piscine Betanodavirus Implies a Novel Antiviral Strategy.ACS infectious diseases · 2024Article
- Interaction between Bombyx mori Cytoplasmic Polyhedrosis Virus NSP8 and BmAgo2 Inhibits RNA Interference and Enhances Virus Proliferation.Microbiology spectrum · 2023Article
- Integration of Cypoviruses into polyhedrin matrix.Nanoscale advances · 2023Article
- Asymmetric reconstruction of the aquareovirus core at near-atomic resolution and mechanism of transcription initiation.Protein & cell · 2023Article
- A New Cypovirus-1 Strain as a Promising Agent for Lepidopteran Pest Control.Microbiology spectrum · 2023Article
- Viral inactivation by light.eLight · 2022Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Many viruses utilize trimeric spikes to gain entry into host cells. However, without in situ structures of these trimeric spikes, a full understanding of this dynamic and essential process of viral infections is not possible. Here we present four in situ and one isolated cryoEM structures of the trimeric spike of the cytoplasmic polyhedrosis virus, a member of the non-enveloped Reoviridae family and a virus historically used as a model in the discoveries of RNA transcription and capping. These structures adopt two drastically different conformations, closed spike and opened spike, which respectively represent the penetration-inactive and penetration-active states. Each spike monomer has four domains: N-terminal, body, claw, and C-terminal. From closed to opened state, the RGD motif-containing C-terminal domain is freed to bind integrins, and the claw domain rotates to expose and project its membrane insertion loops into the cellular membrane. Comparison between turret vertices before and after detachment of the trimeric spike shows that the trimeric spike anchors its N-terminal domain in the iris of the pentameric RNA-capping turret. Sensing of cytosolic S-adenosylmethionine (SAM) and adenosine triphosphate (ATP) by the turret triggers a cascade of events: opening of the iris, detachment of the spike, and initiation of endogenous transcription.
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