期刊
CELL
卷 181, 期 2, 页码 281-+出版社
CELL PRESS
DOI: 10.1016/j.cell.2020.02.058
关键词
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资金
- National Institute of General Medical Sciences [R01GM120553]
- National Institute of Allergy and Infectious Diseases [HHSN272201700059C]
- Pew Biomedical Scholars Award
- Burroughs Wellcome Fund
- Washington Research Foundation
- Pasteur Institute
- University of Washington Arnold and Mabel Beckman cryoEM center
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-1/S-2 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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