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Research Article
Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
Antoni Wrobel
Francis Crick Institute
Corresponding Author
Donald Benton
Francis Crick Institute
Corresponding Author
Steven Gamblin
Francis Crick Institute
Corresponding Author
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The CR3022 antibody, selected from a group of SARS-CoV-1 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 electron cryo-microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.
Keywords
SARS-CoV-2, cryoEM, Structural Biology, Virology
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This is a preprint. It has not completed peer review.
Research Article
Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein
Antoni Wrobel
Francis Crick Institute
Corresponding Author
Donald Benton
Francis Crick Institute
Corresponding Author
Steven Gamblin
Francis Crick Institute
Corresponding Author
Badges
Prescreen
This manuscript passed our Prescreen assessment
Complete author information
Appropriate declaration statements
Potential risks to human health
Prescreen
History
CURRENT STATUS: Posted
Version 1
Posted 05 Jun, 2020
Published
On 21 Oct, 2020
No community comments so far
Metrics
Comments: 0
PDF Downloads: ...
HTML Views: ...
License:
This work is licensed under a CC BY 4.0 License. Read Full License
View the published version here.
The CR3022 antibody, selected from a group of SARS-CoV-1 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 electron cryo-microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.
Figure 1
Figure 2