Mutation profiling, evolution analysis, molecular dynamics simulation, and functional characterization of Omicron sub-strains.

ABSTRACT: The ongoing mutation and evolution of SARS-CoV-2 have posed a severe threat to global health, and their functional impact remains to be further characterized. Here, we analyzed the selection pressure from 49 Omicron sub-strains at the gene and amino acid levels. We also examined the impact of mutations on the binding affinity between the receptor binding domain (RBD) and angiotensin-Converting Enzyme 2 (ACE2) and evaluated the immune escape ability of RBD responding to the monoclonal antibodies (mAbs) through molecular dynamics simulation on eight representative Omicron sub-variants (B.1.1.529, BA.2, XBB.1.5, BA.2.86, JN.1, KP.2, KP.3, and KP.3.1.1). We identified 12 positive selection mutation sites on the viral S protein, including 11 mutation sites in the N-terminal domain (NTD) and RBD

SUBMITTER: Gong T 

PROVIDER: S-EPMC12454883 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature