Antibodies are a potential therapy for severe acute respiratory syndrome
coronavirus 2 (SARS-CoV-2), but the risk of the virus evolving to escape them
remains unclear. Here we map how all mutations to the receptor binding domain
(RBD) of SARS-CoV-2 affect binding by the antibodies in the REGN-COV2 cocktail and
the antibody LY-CoV016. These complete maps uncover a single amino acid mutation
that fully escapes the REGN-COV2 cocktail, which consists of two antibodies,
REGN10933 and REGN10987, targeting distinct structural epitopes. The maps also
identify viral mutations that are selected in a persistently infected patient
treated with REGN-COV2 and during in vitro viral escape selections. Finally, the
maps reveal that mutations escaping the individual antibodies are already present
in circulating SARS-CoV-2 strains. These complete escape maps enable
interpretation of the consequences of mutations observed during viral
surveillance.
Disassembly of the ring‐type decameric structure of peroxiredoxin from
Aeropyrum pernix
K1 by amino acid mutation
