Structural and functional impact by SARS-CoV-2 Omicron spike mutations.

ABSTRACT: The Omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), bearing an unusually high number of mutations, has become a dominant strain in many countries within several weeks. We report here structural, functional, and antigenic properties of its full-length spike (S) protein with a native sequence in comparison with those of previously prevalent variants. Omicron S requires a substantially higher level of host receptor ACE2 for efficient membrane fusion than other variants, possibly explaining its unexpected cellular tropism. Mutations not only remodel the antigenic structure of the N-terminal domain of the S protein but also alter the surface of the receptor-binding domain in a way not seen in other variants, consistent with its remarkable resistance to neutraliz

SUBMITTER: Zhang J 

PROVIDER: S-EPMC8995406 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature