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Structural Basis for Human Receptor Recognition by SARS-CoV-2 Omicron Variant BA.1
Qibin Geng1,2, Ke Shi3, Gang Ye1,2
1Department of Veterinary and Biomedical Sciences, University of Minnesotagrid.17635.36, Saint Paul, Minnesota, USA.
Journal of Virology
|March 28, 2022
Summary
The Omicron variant
Area of Science:
- Virology
- Structural Biology
- Molecular Biology
Background:
- The Omicron variant of SARS-CoV-2 efficiently infects the respiratory tract, despite low ACE2 expression.
- The spike protein's Receptor-Binding Domain (RBD) is crucial for ACE2 recognition and viral tropism.
Purpose of the Study:
- To investigate the enhanced ACE2 binding affinity of the Omicron RBD.
- To elucidate the structural basis of Omicron's mutations affecting ACE2 interaction.
Main Methods:
- Biochemical assays to measure ACE2 binding affinity.
- X-ray crystallography to determine the Omicron RBD-ACE2 complex structure.
Main Results:
- Omicron RBD (BA.1) exhibits stronger binding to ACE2 than the Wuhan strain RBD.
- Crystal structure reveals significant rearrangements at the RBD/ACE2 interface due to Omicron mutations.
- Individual mutations' effects on ACE2 binding were quantified.
Conclusions:
- Enhanced ACE2 binding by Omicron RBD may facilitate respiratory tract infection.
- Structural insights explain Omicron's altered receptor recognition and tissue tropism.
- Findings contribute to understanding SARS-CoV-2 evolution and Omicron's infectivity.
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