Antibody-mediated disruption of the SARS-CoV-2 spike glycoprotein

Nat Commun. 2020 Oct 21;11(1):5337. doi: 10.1038/s41467-020-19146-5.

Abstract

The CR3022 antibody, selected from a group of SARS-CoV monoclonal antibodies for its ability to cross-react with SARS-CoV-2, has been examined for its ability to bind to the ectodomain of the SARS-CoV-2 spike glycoprotein. Using cryo-electron microscopy we show that antibody binding requires rearrangements in the S1 domain that result in dissociation of the spike.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Antibodies, Viral / immunology*
  • Betacoronavirus / immunology*
  • Binding Sites, Antibody / immunology*
  • COVID-19
  • Cell Line
  • Chlorocebus aethiops
  • Coronavirus Infections / virology
  • Cryoelectron Microscopy
  • Humans
  • Neutralization Tests
  • Pandemics
  • Pneumonia, Viral / virology
  • Protein Domains / immunology
  • SARS-CoV-2
  • Spike Glycoprotein, Coronavirus / immunology*
  • Vero Cells

Substances

  • Antibodies, Monoclonal
  • Antibodies, Viral
  • Spike Glycoprotein, Coronavirus
  • spike protein, SARS-CoV-2