Recent emerging SARS-CoV-2 variant from the United Kingdom (B.1.1.7) is spreading worldwide at an alarming rate.
•
The B.1.1.7 strain consists of six mutations, and three residue deletions on the spike protein (S-protein).
•
One of the notable mutations in the B.1.1.7 variant is the P681H, which is a substitution of proline (P) to histidine (H) on the S-protein "PRRAR" furin cleavage site.
•
The P618H mutation on B.1.1.7 variant resulted in a conformational change in the furin cleavage, subsequently increasing the binding affinity of furin to the S-protein.
•
The S-protein B.1.1.7 variant may enhance viral entry to the host cell causing higher infectivity.
Abstract
The B.1.1.7 SARS-CoV-2 strain that has emerged in the UK in early December presents seven mutations and three deletions on S-protein structure that could lead to a more infective strain. The P681H mutation in the “PRRAR” furin cleavage site might affect the binding affinity to furin enzyme and hence its infectivity.
Therefore, in this study, various structural bioinformatics approaches were used to model the S-protein structure with the B.1.1.7 variant amino acid substitutions and deletions. In addition to modelling the binding of furin to the cleavage site of the wild-type and the B.1.1.7 variant.
Conclusively the B.1.1.7 variant resulted in dynamic stability, conformational changes and variations in binding energies in the S-protein structure, resulting in a more favourable binding of furin enzyme to the SARS-CoV-2 S-protein.
