Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein.
The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result ... in dissociation of the spike.
Mesh Terms:
Animals, Antibodies, Monoclonal, Antibodies, Viral, Betacoronavirus, Binding Sites, Antibody, COVID-19, Cell Line, Chlorocebus aethiops, Coronavirus Infections, Cryoelectron Microscopy, Humans, Neutralization Tests, Pandemics, Pneumonia, Viral, Protein Domains, SARS-CoV-2, Spike Glycoprotein, Coronavirus, Vero Cells
Animals, Antibodies, Monoclonal, Antibodies, Viral, Betacoronavirus, Binding Sites, Antibody, COVID-19, Cell Line, Chlorocebus aethiops, Coronavirus Infections, Cryoelectron Microscopy, Humans, Neutralization Tests, Pandemics, Pneumonia, Viral, Protein Domains, SARS-CoV-2, Spike Glycoprotein, Coronavirus, Vero Cells
Nat Commun
Date: Oct. 21, 2020
PubMed ID: 33087721
View in: Pubmed Google Scholar
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