Title : Structure, Function, and Antigenicity of the
SARS-CoV-2
Spike Glycoprotein
Abstract :
- 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