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A hinge glycan regulates spike bending and impacts coronavirus infectivity

ABSTRACT: Analysis of the structures and distributions of native spike conformations on vitrified human coronavirus NL63 (HCoV-NL63) virions without chemical fixation by cryogenic electron tomography (cryoET) and subtomogram averaging, along with site-specific glycan composition and occupancy determined by mass spectroscopy

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Cercopithecus Aethiops (green Monkey) (grivet)

SUBMITTER: Peng Zhao

LAB HEAD: Lance Wells

PROVIDER: PXD039247 | Pride | 2024-01-26

REPOSITORIES: Pride

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Structural insights into the modulation of coronavirus spike tilting and infectivity by hinge glycans.

Chmielewski David D Wilson Eric A EA Pintilie Grigore G Zhao Peng P Chen Muyuan M Schmid Michael F MF Simmons Graham G Wells Lance L Jin Jing J Singharoy Abhishek A Chiu Wah W

Nature communications 20231107 1

Coronavirus spike glycoproteins presented on the virion surface mediate receptor binding, and membrane fusion during virus entry and constitute the primary target for vaccine and drug development. How the structure dynamics of the full-length spikes incorporated in viral lipid envelope correlates with the virus infectivity remains poorly understood. Here we present structures and distributions of native spike conformations on vitrified human coronavirus NL63 (HCoV-NL63) virions without chemical ...[more]

PMID: 37935678

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