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Evolutionary and structural analysis elucidates mutations on SARS-CoV2 spike protein with altered human ACE2 binding
1Amity Institute of Biotechnology, Amity University, Kolkata, 700135, India.
Biochemical and Biophysical Research Communications
|February 19, 2021
Summary
Scientists identified key SARS-CoV-2 variants affecting spike protein binding to human ACE2. Some variants like V367F and S494P show increased binding affinity, potentially impacting viral entry and transmission.
Area of Science:
- Virology
- Molecular Biology
- Evolutionary Biology
Background:
- The spike protein's receptor-binding domain (RBD) is crucial for SARS-CoV-2 entry into host cells by binding to human ACE2.
- Understanding viral evolution and its impact on spike protein function is vital for pandemic response.
Purpose of the Study:
- To identify SARS-CoV-2 spike protein variants that emerged during the pandemic.
- To evaluate the binding affinity of these RBD variants with human ACE2.
Main Methods:
- Evolutionary analysis of 2178 SARS-CoV-2 genomes to identify variants under selection.
- Protein-protein docking and binding free energy calculations to assess ACE2 binding efficacy.
- Pan-proteomic analysis to identify mutations.
Main Results:
- Five RBD variants (A348T, V367F, G476S, V483A, S494P) were identified under strong positive selection.
- A348T, G476S, and V483A showed reduced ACE2 binding affinity compared to the Wuhan strain.
- V367F and S494P variants exhibited increased binding affinity to human ACE2 due to enhanced hydrogen bonding and interfacial complementarity.
Conclusions:
- Specific SARS-CoV-2 RBD variants significantly alter binding affinity to human ACE2.
- Variants like V367F and S494P with enhanced binding may have implications for viral transmissibility and pathogenesis.
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