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Structure paper

TitleMultiple conformations of trimeric spikes visualized on a non-enveloped virus.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 550, Year 2022
Publish dateJan 27, 2022
AuthorsYinong Zhang / Yanxiang Cui / Jingchen Sun / Z Hong Zhou /
PubMed AbstractMany 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 ...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.
External linksNat Commun / PubMed:35087065 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 4.1 Å
Structure data

32504

7whm

EMDB-32504, PDB-7whm:
Closed spike of Bombyx mori cytoplasmic polyhedrosis virus
Method: EM (single particle) / Resolution: 2.7 Å

32505

7whn

EMDB-32505, PDB-7whn:
Opened spike of Bombyx mori cytoplasmic polyhedrosis virus
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-32506:
5-fold vertex of Bombyx mori cytoplasmic polyhedrosis virus formed by trimeric spike and pentameric turret
Method: EM (single particle) / Resolution: 4.1 Å

32507

7whp

EMDB-32507, PDB-7whp:
Pentameric turret of Bombyx mori cytoplasmic polyhedrosis virus after spike detaches.
Method: EM (single particle) / Resolution: 3.7 Å

EMDB-32508:
Detached spike from Bombyx mori cytoplasmic polyhedrosis virus particle
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-SAM:
S-ADENOSYLMETHIONINE

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • bombyx mori cypovirus 1
KeywordsVIRAL PROTEIN / Cell attachment / Membrane penetration / Capping enzyme

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