Accéder au contenu
MilliporeSigma

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.

Cell (2020-03-11)
Alexandra C Walls, Young-Jun Park, M Alejandra Tortorici, Abigail Wall, Andrew T McGuire, David Veesler
RÉSUMÉ

The emergence of SARS-CoV-2 has resulted in >90,000 infections and >3,000 deaths. Coronavirus spike (S) glycoproteins promote entry into cells and are the main target of antibodies. We show that SARS-CoV-2 S uses ACE2 to enter cells and that the receptor-binding domains of SARS-CoV-2 S and SARS-CoV S bind with similar affinities to human ACE2, correlating with the efficient spread of SARS-CoV-2 among humans. We found that the SARS-CoV-2 S glycoprotein harbors a furin cleavage site at the boundary between the S1/S2 subunits, which is processed during biogenesis and sets this virus apart from SARS-CoV and SARS-related CoVs. We determined cryo-EM structures of the SARS-CoV-2 S ectodomain trimer, providing a blueprint for the design of vaccines and inhibitors of viral entry. Finally, we demonstrate that SARS-CoV S murine polyclonal antibodies potently inhibited SARS-CoV-2 S mediated entry into cells, indicating that cross-neutralizing antibodies targeting conserved S epitopes can be elicited upon vaccination.

MATÉRIAUX
Référence du produit
Marque
Description du produit

Sigma-Aldrich
SARS-COV-2-Spike-RBD epitope (450-469), 95% (HPLC), lyophilized powder
Sigma-Aldrich
SARS-COV-2-Spike-RBD epitope (370-394), ≥95% (HPLC), lyophilized powder
Sigma-Aldrich
SARS-COV-2-Spike-RBD epitope (480-499), ≥95% (HPLC), lyophilized powder
Sigma-Aldrich
Anti-SARS-COV-2-Spike-RBD region Peroxidase conjugated antibody produced in rabbit