This analysis reveals mutation patterns and their effects on receptor binding affinity in Omicron variants, suggesting implications for immune response.
Key Points
The binding affinity of SARS-CoV-2 variants increased, particularly in B.1.1.529 and BA.2.86, due to accumulated mutations.
Twelve positive selection mutation sites were identified in the S protein, mostly within the N-terminal domain and receptor binding domain.
Molecular dynamics simulation evaluated how mutations affect immune escape from monoclonal antibodies in Omicron sub-variants.
Findings indicate that specific mutations may enhance receptor binding, thus contributing to the evolution and infectivity of these variants.