Fig. 3: Structure complexes formed between YB9-258 and SARS-CoV-2 spikes reveal an antibody-antigen interface involving point changes introduced by somatic hypermutation. | Nature Communications

Fig. 3: Structure complexes formed between YB9-258 and SARS-CoV-2 spikes reveal an antibody-antigen interface involving point changes introduced by somatic hypermutation.

From: Somatically hypermutated antibodies isolated from SARS-CoV-2 Delta infected patients cross-neutralize heterologous variants

Fig. 3: Structure complexes formed between YB9-258 and SARS-CoV-2 spikes reveal an antibody-antigen interface involving point changes introduced by somatic hypermutation.The alternative text for this image may have been generated using AI.

a Omicron BA.1 spike (S-6P) in complex with YB9-258 Fab in different stoichiometries and conformations. b Wildtype spike (S-6P) in complex with YB9-258 Fab and R1-32 Fab. c S1 of disintegrated wildtype spike in complex with YB9-258 Fab and R1-32 Fab. Structures in a–c are low-pass filtered to 15 Å to reveal flexible regions (also see Supplementary Fig. 5). d Epitope of YB9-258 Fab on RBD of wildtype spike. CDR loops are indicated, selected interacting residues between RBD and antibody are shown and indicated. Somatically hypermutated residues are highlighted in yellow and sidechains of the ones involved in interaction are shown with changes indicated (also see Supplementary Fig. 7). Dashed lines indicate hydrogen bonds. Highly buried RBD residues (BSA > 30 Å) are colored blue.

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