SARS-COV-2 Omicron variants conformationally escape a rare quaternary antibody binding mode.

ABSTRACT: The ongoing evolution of SARS-CoV-2 into more easily transmissible and infectious variants has provided unprecedented insight into mutations enabling immune escape. Understanding how these mutations affect the dynamics of antibody-antigen interactions is crucial to the development of broadly protective antibodies and vaccines. Here we report the characterization of a potent neutralizing antibody (N3-1) identified from a COVID-19 patient during the first disease wave. Cryogenic electron microscopy revealed a quaternary binding mode that enables direct interactions with all three receptor-binding domains of the spike protein trimer, resulting in extraordinary avidity and potent neutralization of all major variants of concern until the emergence of Omicron. Structure-based rational design of

SUBMITTER: Goike J 

PROVIDER: S-EPMC10713552 | biostudies-literature | 2023 Dec

REPOSITORIES: biostudies-literature