Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody
Chinese Academy of Sciences · Shanghai Institute of Materia Medica · +3 more institutions
Abstract
The severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) Omicron variant has become the dominant infective strain. We report the structures of the Omicron spike trimer on its own and in complex with angiotensin-converting enzyme 2 (ACE2) or an anti-Omicron antibody. Most Omicron mutations are located on the surface of the spike protein and change binding epitopes to many current antibodies. In the ACE2-binding site, compensating mutations strengthen receptor binding domain (RBD) binding to ACE2. Both the RBD and the apo form of the Omicron spike trimer are thermodynamically unstable. An unusual RBD-RBD interaction in the ACE2-spike complex supports the open conformation and further reinforces ACE2…
Citation impact
- FWCI
- 29.74
- Percentile
- 100%
- References
- 36
Authors
26- WYWanchao YinCorresponding
Chinese Academy of Sciences, Shanghai Institute of Materia Medica
- YXYouwei XuCorresponding
Chinese Academy of Sciences, Shanghai Institute of Materia Medica
- PXPeiyu XuCorresponding
Chinese Academy of Sciences, Shanghai Institute of Materia Medica
- XCXiaodan CaoCorresponding
Shanghai Genon Biological Products (China)
- CWCanrong WuCorresponding
Chinese Academy of Sciences, Shanghai Institute of Materia Medica
Topics & keywords
- Trimer
- Chemistry
- Antibody
- Spike (software development)
- Binding site
- Biophysics
- Epitope
- Crystallography
- Good health and well-being