The SARS-CoV-2 spike reversibly samples an open-trimer conformation exposing novel epitopes.

ABSTRACT: Current COVID-19 vaccines and many clinical diagnostics are based on the structure and function of the SARS-CoV-2 spike ectodomain. Using hydrogen-deuterium exchange monitored by mass spectrometry, we have uncovered that, in addition to the prefusion structure determined by cryo-electron microscopy, this protein adopts an alternative conformation that interconverts slowly with the canonical prefusion structure. This new conformation-an open trimer-contains easily accessible receptor-binding domains. It exposes the conserved trimer interface buried in the prefusion conformation, thus exposing potential epitopes for pan-coronavirus antibody and ligand recognition. The population of this state and kinetics of interconversion are modulated by temperature, receptor binding, antibody binding, an

SUBMITTER: Costello SM 

PROVIDER: S-EPMC9007726 | biostudies-literature | 2022 Mar

REPOSITORIES: biostudies-literature