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Published on: August 12, 2021
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Experimental Evidence for Enhanced Receptor Binding by Rapidly Spreading SARS-CoV-2 Variants
Charlie Laffeber1, Kelly de Koning1, Roland Kanaar1
1Department of Molecular Genetics, Oncode Institute, Erasmus MC Cancer Institute, Erasmus University Medical Center, 3000 CA Rotterdam, the Netherlands.
Journal of Molecular Biology
|May 23, 2021
Summary
New SARS-CoV-2 variants show mutations in the spike protein that affect binding to human ACE2 receptors. Some mutations enhance binding, impacting viral transmission and immune evasion, highlighting the need for global genomic surveillance.
Area of Science:
- Virology
- Molecular Biology
- Genomics
Background:
- New SARS-CoV-2 variants possess multiple spike protein mutations.
- These mutations occur at the receptor binding domain (RBD) interface with human ACE2 (hACE2).
Purpose of the Study:
- To experimentally characterize the impact of specific SARS-CoV-2 mutations on RBD binding affinity to hACE2.
- To understand the combined effects of mutations found in different SARS-CoV-2 lineages.
Main Methods:
- Experimental determination of binding affinity between mutated RBDs and hACE2.
- Comparison of binding affinities for wild-type RBD, N501Y, E484K, K417N, and combinations thereof.
Main Results:
- N501Y mutation significantly increases RBD binding affinity (7-fold) to hACE2.
- E484K slightly enhances affinity, while K417N reduces it.
- The triple mutant (B.1.351) shows increased binding (3-fold) but less than N501Y alone; E484K/N501Y double mutant exhibits stronger binding than N501Y.
Conclusions:
- Mutations independently affect SARS-CoV-2 receptor binding affinity.
- The functional characterization of viral mutations is crucial for understanding viral evolution and spread.
- Global viral genome surveillance is essential for tracking and managing emerging variants.
