Cell
Volume 181, Issue 2, 16 April 2020, Pages 281-292.e6
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Article
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

https://doi.org/10.1016/j.cell.2020.02.058Get rights and content
open access

Highlights

  • SARS-CoV-2 uses ACE2 to enter target cells

  • SARS-CoV-2 and SARS-CoV bind with similar affinities to ACE2

  • Structures of SARS-CoV-2 spike glycoprotein in two conformations

  • SARS-CoV polyclonal antibodies inhibit SARS-CoV-2 spike-mediated entry into cells

Summary

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.

Keywords

coronavirus
SARS-CoV-2
SARS-CoV
spike glycoprotein
antibodies
neutralizing antibodies
viral receptor
cryo-EM

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These authors contributed equally

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