[PDF][PDF] Structure, function, and antigenicity of the SARS-CoV-2 spike glycoprotein

AC Walls, YJ Park, MA Tortorici, A Wall, AT McGuire… - Cell, 2020 - cell.com
Cell, 2020cell.com
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 S …
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.
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