6VXX

Structure of the SARS-CoV-2 spike glycoprotein (closed state)

Summary for 6VXX

• Entry DOI: 10.2210/pdb6vxx/pdb
• EMDB information: 21452 21457
• Descriptor: Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: coronavirus, sars-cov-2, sars-cov, spike glycoprotein, fusion protein, structural genomics, seattle structural genomics center for infectious disease, ssgcid, viral protein
• Biological source: Severe acute respiratory syndrome coronavirus 2 (2019-nCoV)
• Total number of polymer chains: 3
• Total formula weight: 438264.27

Authors

Walls, A.C.,Park, Y.J.,Tortorici, M.A.,Wall, A.,Seattle Structural Genomics Center for Infectious Disease (SSGCID),McGuire, A.T.,Veesler, D. (deposition date: 2020-02-25, release date: 2020-03-11, Last modification date: 2024-11-06)

Primary citation

Walls, A.C.,Park, Y.J.,Tortorici, M.A.,Wall, A.,McGuire, A.T.,Veesler, D.
Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein.
Cell, 181:281-, 2020

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-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.

PubMed: 32155444
DOI: 10.1016/j.cell.2020.02.058

Experimental method

ELECTRON MICROSCOPY (2.8 Å)