Fig. 4: Antibody epitope, potency, breadth and escapability.
From: SARS-CoV-2 RBD antibodies that maximize breadth and resistance to escape
a, Multidimensional scaling projection of similarities in antibody binding-escape maps from the present (red) and previous (grey) studies. Pie charts illustrate the RBD subdomains where mutations confer escape (key, bottom left: RBM, residues 437–508; ACE2 contact, 4 Å cutoff). Structural projections of escape arrayed around the perimeter (colour bar, bottom right), with grey outlines tracing structural footprints. b–d, Projected epitope space from a annotated by antibody properties: SARS-CoV-2-neutralizing potency (b), sarbecovirus-binding breadth (c) and escape by natural SARS-CoV-2 mutants (d). For each property, antibodies are coloured such that purple reflects the most desirable antibody (colour bar, right): most potent neutralization (log10 scale), highest breadth, and lowest natural frequency of escape mutants (log10 scale). e, Relationship between SARS-CoV-2 neutralization potency and sarbecovirus breadth for antibodies described in this work and in a parallel study37 (S2X259). f, Relationship between functional epitope size and SARS-CoV-2 RBD binding affinity. g, Relationship between natural SARS-CoV-2 escape mutant frequency (Extended Data Fig. 3c) and sarbecovirus breadth.
