Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition

Greaney, Allison J.; Starr, Tyler N.; Gilchuk, Pavlo; Zost, Seth J.; Binshtein, Elad; Loes, Andrea N.; Hilton, Sarah K.; Huddleston, John; Eguia, Rachel; Crawford, Katharine H. D.; Dingens, Adam S.; Nargi, Rachel S.; Sutton, Rachel E.; Suryadevara, Naveenchandra; Rothlauf, Paul W.; Liu, Zhuoming; Whelan, Sean P. J.; Carnahan, Robert H.; Crowe, James E.; Bloom, Jesse D.

doi:10.1016/j.chom.2020.11.007

articleCell Host & MicrobeNov 19, 2020HYBRID OA

Complete Mapping of Mutations to the SARS-CoV-2 Spike Receptor-Binding Domain that Escape Antibody Recognition

AJAllison J. Greaney TNTyler N. Starr PGPavlo Gilchuk SJSeth J. Zost EBElad Binshtein

University of Washington · Fred Hutch Cancer Center · +4 more institutions

PubMed

Indexed incrossrefpubmed

Abstract

Antibodies targeting the SARS-CoV-2 spike receptor-binding domain (RBD) are being developed as therapeutics and are a major contributor to neutralizing antibody responses elicited by infection. Here, we describe a deep mutational scanning method to map how all amino-acid mutations in the RBD affect antibody binding and apply this method to 10 human monoclonal antibodies. The escape mutations cluster on several surfaces of the RBD that broadly correspond to structurally defined antibody epitopes. However, even antibodies targeting the same surface often have distinct escape mutations. The complete escape maps predict which mutations are selected during viral growth in the presence of single antibodies. They…

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Topics & keywords

Topics

Keywords

Spike Protein
Biology
Spike (software development)
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2)
Coronavirus disease 2019 (COVID-19)
Antibody
Virology
Mutation

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