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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.
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https://hal-pasteur.archives-ouvertes.fr/pasteur-02546518
Contributor : Maria-Alejandra Tortorici <>
Submitted on : Saturday, April 18, 2020 - 3:43:22 AM
Last modification on : Friday, April 24, 2020 - 1:47:32 AM

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Alexandra Walls, Young-Jun Park, M. Alejandra Tortorici, Abigail Wall, Andrew Mcguire, et al.. Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. Cell, Elsevier, 2020, 181 (2), pp.281-292.e6. ⟨10.1016/j.cell.2020.02.058⟩. ⟨pasteur-02546518⟩

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