The accumulation of numerous mutations in emerging SARS-CoV-2 variants contributes to viral escape from immune response, necessitating an assessment of the effectiveness of known antibodies and consideration of their modification.

The study modeled the receptor binding domain (RBD) of Wild-type and XBB.1.5 virus variants complexed with native and modified STE90-C11 antibodies.

 

The most stabilizing set of substitutions:

V2I, A24E, V29F, R71M, V99F, A100F, D101Y in the heavy chain of antibody.

A25F, S31Y, A50W, S56E, N92H, S93E, and P95E in the light chain of antibody.

 

The accumulation of mutations in the spike protein of emerging SARS-CoV-2 variants can poten- tially reduce the affinity of neutralizing antibodies. However, modifying amino acid sequences of antibody chains offers a promising strategy to re-establish efficient binding to the Spike protein, thereby enabling the adaptation of antibodies in response to the virus’s evolutionary changes.