Method: Recombinant proteins for RBD and its mutants (A435S, F342L, G476S, K458R, N354D, V367F, V483A, W436R), SARS-CoV S1, HCoV-HKU1 S1, and MERS-CoV RBD were commercial products (Sino Biological).
Discussion: For instance, V367F, W436R, and D364Y were reported to increase the binding affinity for ACE2, which might accelerate viral spread further perpetuating the pandemic.
In silico binding profile characterization of SARS-CoV-2 spike protein and its mutants bound to human ACE2 receptor.
Result: The simulation results suggested that all the three mutants (N354D/D364Y, V367F and W436R) can enhance the binding between spike RBD and hACE2, which agrees with the experiment.
Discussion: V367F, W436R and N354D/D364Y, had more potent binding affinities than the prototype, and the findings agreed with the KD and EC50 values measured by different methods by ACRO biosystem (https://www.acrobiosystems.com).
Discussion: The trend of the measured binding affinities was: prototype < W436R < N354D/D364Y < PMID: 34379353
2021
Biotechnology journal
Discussion: Interestingly, the mutations Discussion: Then, the RBD sequence between SARS-CoV-2 and SARS-CoV was compared and we found that the W436R and R408I are same in both, which suggested that the binding to these sites couldn't distinguish SARS-CoV-2 and SARS-CoV.
Discussion: Therefore, the convalescent patients or vaccine immunized people without antibody to block the mutant virus may still have the possibility of SARS-COV-2 infection with W436R and R408I mutation.
Discussion: While the sequence of HTS0483 is totally different with the other 3 antibodies which may partially explain why only HTS0483 could blocking the entry of the mutants W436R and R408I.
A bioluminescent and homogeneous SARS-CoV-2 spike RBD and hACE2 interaction assay for antiviral screening and monitoring patient neutralizing antibody levels.
SARS_CoV_2 mutation literature information.
PMID: 
2021
Nature communications
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