Fig. 5: Escape maps predict mutations that are selected during viral growth in the presence of monoclonal antibodies.

a Mutations selected when chimeric VSV encoding the SARS-CoV-2 spike was grown in the presence of each of the three indicated antibodies by Weisblum et al.⁷. Each point represents a different amino-acid mutation, with the x axis indicating how strongly the mutation escapes antibody binding (measured in the current study) and the y axis indicating how well the mutant binds to ACE2 (measured in Starr et al.³²). The red diamonds indicate the mutations selected in VSV-spike by Weisblum et al., the gray circles indicate all other amino-acid mutations accessible by a single-nucleotide change, and the gold x’s indicate amino-acid mutations that require multiple nucleotide changes to the codon. b Logo plots showing the effects of only single-nucleotide accessible amino-acid mutations on antibody binding. Mutations selected in VSV-spike virus by Weisblum et al. are colored red. c The correlation of the effects of mutations on antibody binding measured in the current study and effects on viral neutralization previously measured by Weisblum et al.⁷ using chimeric VSV (top) or lentiviral particles (bottom). The x axis shows the escape fraction measured in the current study, and the y axis shows the fold change in inhibitory concentration 50% (IC50) for viral neutralization caused by that mutation, such that larger numbers correspond to greater reductions in neutralization sensitivity. For effects of all antibody- and plasma-binding-escape mutations on ACE2 binding and RBD expression, see Fig. S4. For each mutation’s escape fraction compared to fold-change IC₅₀ against each monoclonal antibody or polyclonal plasma tested in Weisblum et al.⁷, see Fig. S6.