Structural insights into antibody-mediated neutralization of SARS-CoV-2
Abstract
In less than a year, researchers have uncovered structure–function details for many of the proteins encoded by SARS-CoV-2. We report structures that reveal how monoclonal neutralizing antibodies bind spike to prevent infection. One such monoclonal antibody, BG10–19, targets a highly-conserved, proteoglycan epitope on the SARS-CoV-2 RBD, which sits outside of mutated residue positions found in all circulating variants of concern (i.e. alpha, beta, gamma, delta, kappa, and lambda). In addition, BG10–19 bridges adjacent RBDs and locks the spike trimer in a completely closed conformation to potently neutralize SARSCoV-2 and heterologous SARS-like coronaviruses. Thus, BG10–19 is a candidate antibody therapeutic to combat continuing SARS-CoV-2 antigenic drift and represents an attractive epitope for pan-sarbecovirus vaccine design.
Additional Information
© The Author(s) 2021. Published by Oxford University Press. This article is published and distributed under the terms of the Oxford University Press, Standard Journals Publication Model (https://academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model). Published: 27 January 2022.Additional details
- Eprint ID
- 114351
- DOI
- 10.1093/glycob/cwab121
- Resolver ID
- CaltechAUTHORS:20220415-214637408
- Created
-
2022-04-18Created from EPrint's datestamp field
- Updated
-
2022-04-18Created from EPrint's last_modified field
- Caltech groups
- COVID-19, Division of Biology and Biological Engineering (BBE)