Fig. 1. Potency, escapability, and breadth of a panel of RBD antibodies.

a, SARS-CoV-2 neutralization potency (authentic virus [n=3] and spike-pseudotyped VSV particles [n = 3 to 8] on Vero E6 cells), Fab:RBD binding affinities measured by SPR [n = 2 to 4], and epitope classifications. Additional details in Extended Data Table 1. b,c, Deep mutational scanning maps of mutations that escape binding by antibodies targeting the core RBD (b) or the receptor-binding motif (c). Letter height indicates that mutation’s strength of escape from antibody binding. Letters colored by effect on folded RBD expression (b) or ACE2 binding affinity (c)²⁶. Relative “functional epitope size” and “escapability” are tabulated at right, scaling from 0 (no escape mutations) to 1 (largest epitope/most escapable antibody). Heatmaps, bottom, illustrate variability among sarbecovirus or SARS-CoV-2 sequences. d, Antibody binding to a pan-sarbecovirus RBD panel. Heatmap illustrates binding from FACS-based selections (scale bar, bottom left). Asterisks, reduced-affinity binding in secondary binding assays (Extended Data Fig. 4a–f).