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7WHN

Opened spike of Bombyx mori cytoplasmic polyhedrosis virus

Summary for 7WHN
Entry DOI10.2210/pdb7whn/pdb
EMDB information32505
DescriptorPPPDE domain-containing protein (1 entity in total)
Functional Keywordscell attachment, membrane penetration, viral protein
Biological sourceBombyx mori cypovirus 1
Total number of polymer chains1
Total formula weight140370.25
Authors
Zhang, Y.,Cui, Y.,Sun, J.,Zhou, Z.H. (deposition date: 2021-12-31, release date: 2022-02-02, Last modification date: 2025-07-02)
Primary citationZhang, Y.,Cui, Y.,Sun, J.,Zhou, Z.H.
Multiple conformations of trimeric spikes visualized on a non-enveloped virus.
Nat Commun, 13:550-550, 2022
Cited by
PubMed 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.
PubMed: 35087065
DOI: 10.1038/s41467-022-28114-0
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

240971

数据于2025-08-27公开中

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