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-Structure paper
Title | Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein. |
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Journal, issue, pages | Cell, Vol. 181, Issue 2, Page 281-292.e6, Year 2020 |
Publish date | Apr 16, 2020 |
Authors | Alexandra C Walls / Young-Jun Park / M Alejandra Tortorici / Abigail Wall / Andrew T McGuire / David Veesler / |
PubMed 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- ...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/S 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. |
External links | Cell / PubMed:32155444 / PubMed Central |
Methods | EM (single particle) |
Resolution | 2.8 - 3.2 Å |
Structure data | EMDB-21452, PDB-6vxx: EMDB-21457, PDB-6vyb: |
Chemicals | ChemComp-NAG: |
Source |
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Keywords | VIRAL PROTEIN / Coronavirus / SARS-CoV-2 / SARS-CoV / spike glycoprotein / fusion protein / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID |