Fig. 2: Mutations that escape antibody binding are usually in the direct structural footprint. | Nature Communications

Fig. 2: Mutations that escape antibody binding are usually in the direct structural footprint.

From: Mapping mutations to the SARS-CoV-2 RBD that escape binding by different classes of antibodies

Fig. 2: Mutations that escape antibody binding are usually in the direct structural footprint.

a The total escape at each site is mapped onto the surface of the Fab-bound RBD, with white indicating no escape and red indicating the site with the most escape from that antibody. Sites where no mutations are tolerated for RBD folding or ACE2 binding are indicated in dark gray. For C105 and LY-CoV016, gray labels with dashed lines indicate example contact sites with no tolerated mutations. For C110, the general area where site 444 (unresolved in structure) would be located is indicated. b Total escape at each site in the RBD, with sites classified according to whether they are an antibody contact (within 4 Å), antibody-proximal (4 to 8 Å), antibody-distal (>8 Å), or unresolved in the Fab-spike trimer structure. The text indicates the number of sites in each structural category that are sites of strong escape, (n/total) shown in orange. See “Methods” for details and PDB accessions.

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