National Natural Science Foundation of China (NSFC)
31672489
China
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE028583
United States
National Institutes of Health/National Institute of Dental and Craniofacial Research (NIH/NIDCR)
DE025567
United States
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)
AI094386
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM071940
United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR)
1S10RR23057
United States
National Institutes of Health/Office of the Director
1S10OD018111
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
U24GM116792
United States
National Science Foundation (NSF, United States)
DMR-1548924
United States
National Science Foundation (NSF, United States)
DBI-1338135
United States
Citation
Journal: Nat Commun / Year: 2022 Title: Multiple conformations of trimeric spikes visualized on a non-enveloped virus. Authors: Yinong Zhang / Yanxiang Cui / Jingchen Sun / Z Hong Zhou / 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 ...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.
In the structure databanks used in Yorodumi, some data are registered as the other names, "COVID-19 virus" and "2019-nCoV". Here are the details of the virus and the list of structure data.
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