Allosteric effects of CDR-H3 mutations modulate binding and neutralization of a conserved SARS-CoV-2 RBD-targeting antibody
Comparing wild-type XG83 and modified MuXG83 shows how allosteric tuning affects antibody-antigen compatibility in developing variations like Omicron, and indicates that non-epitope (potentially allosteric) changes to CDRH3 are also important while investigating potential development and neutralization before advancement.