Nanometer-resolution in situ structure of the SARS-CoV-2 postfusion spike protein.
The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates membrane fusion to allow entry of the viral genome into host cells. To understand its detailed entry mechanism and develop a specific entry inhibitor, in situ structural information on the SARS-CoV-2 spike protein in different states is urgent. ... Here, by using cryo-electron tomography, we observed both prefusion and postfusion spikes in ?-propiolactone-inactivated SARS-CoV-2 virions and solved the in situ structure of the postfusion spike at nanometer resolution. Compared to previous reports, the six-helix bundle fusion core, the glycosylation sites, and the location of the transmembrane domain were clearly resolved. We observed oligomerization patterns of the spikes on the viral membrane, likely suggesting a mechanism of fusion pore formation.
Mesh Terms:
Amino Acid Motifs, Animals, Chlorocebus aethiops, Cryoelectron Microscopy, Electron Microscope Tomography, Glycosylation, Protein Domains, Protein Multimerization, SARS-CoV-2, Spike Glycoprotein, Coronavirus, Vero Cells
Amino Acid Motifs, Animals, Chlorocebus aethiops, Cryoelectron Microscopy, Electron Microscope Tomography, Glycosylation, Protein Domains, Protein Multimerization, SARS-CoV-2, Spike Glycoprotein, Coronavirus, Vero Cells
Proc Natl Acad Sci U S A
Date: Nov. 30, 2021
PubMed ID: 34782481
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