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A tethered ligand assay to probe SARS-CoV-2:ACE2 interactions
Magnus S Bauer1,2,3, Sophia Gruber1,2, Adina Hausch1,2
1Department of Physics, LMU Munich, 80799 Munich, Germany.
The SARS-CoV-2 virus binds more stably to human ACE2 receptors than SARS-CoV-1, potentially offering a survival advantage. This finding aids in developing new therapies targeting viral attachment.
Area of Science:
- Virology
- Biophysics
- Immunology
Background:
- SARS-CoV-2 initiates infection by binding to the human ACE2 receptor.
- Mechanical stability of viral attachment is critical for fitness in the airways.
Purpose of the Study:
- To assess the force stability of the SARS-CoV-2 Receptor Binding Domain (RBD):ACE2 interaction.
- To compare the binding stability of SARS-CoV-2 and SARS-CoV-1.
Main Methods:
- Single-molecule force spectroscopy was used to mimic physiological forces like coughing and sneezing.
- The RBD:ACE2 interaction stability was tested under simulated physiological conditions.
Main Results:
- SARS-CoV-2 exhibited higher force stability in its binding to ACE2 compared to SARS-CoV-1.
- This enhanced binding stability may confer a fitness advantage to SARS-CoV-2.
Conclusions:
- The developed assay is sensitive to blocking agents that inhibit RBD:ACE2 binding.
- This method can be used to investigate the efficacy of neutralizing antibodies and other COVID-19 therapeutics.
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