期刊
SCIENCE
卷 375, 期 6583, 页码 864-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abn8652
关键词
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资金
- National Institute of Allergy and Infectious Diseases [DP1AI158186, HHSN272201700059C]
- Pew Biomedical Scholars Award
- Investigators in the Pathogenesis of Infectious Disease Awards from the Burroughs Wellcome Fund
- Fast Grants
- NIH [S10OD032290]
- University of Washington Arnold and Mabel Beckman Cryo-EM Center
- Wellcome Trust [209407/Z/17/Z]
- ALS-ENABLE program - National Institute of General Medical Sciences [DE-AC02-05CH11231, P30 GM124169-01]
The SARS-CoV-2 Omicron variant evades antibody-mediated immunity and exhibits enhanced affinity for host cells due to accumulation of spike mutations and remodeling of interactions with the ACE2 receptor.
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant of concern evades antibody-mediated immunity that comes from vaccination or infection with earlier variants due to accumulation of numerous spike mutations. To understand the Omicron antigenic shift, we determined cryo-electron microscopy and x-ray crystal structures of the spike protein and the receptor-binding domain bound to the broadly neutralizing sarbecovirus monoclonal antibody (mAb) S309 (the parent mAb of sotrovimab) and to the human ACE2 receptor. We provide a blueprint for understanding the marked reduction of binding of other therapeutic mAbs that leads to dampened neutralizing activity. Remodeling of interactions between the Omicron receptor-binding domain and human ACE2 likely explains the enhanced affinity for the host receptor relative to the ancestral virus.
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