Structural analysis of spike proteins from SARS-CoV-2 variants of concern highlighting their functional alterations: Supplementary figure

Aim: Mutations in the SARS-CoV-2 spike (S) protein have dramatically changed the transmissibility and

pathogenicity of the virus. Therefore, we studied the binding affinity of Omicron spike-receptor binding

domain (S-RBD) with human ACE2 receptor. Materials & methods: We used pyDockWEB and HADDOCK

2.4 docking for our study. Results: Computational docking indicated higher binding affinity of Omicron SRBD

as comparedwithwild-type SARS-CoV-2 and Delta S-RBD with ACE2. Interface analysis suggested four

mutated residues of Omicron S-RBD for its enhanced binding. We also showed decreased binding affinity

of Omicron and Delta S-RBDs with monoclonal antibodies. Conclusion: Compared with wild-type SARSCoV-

2, Omicron S-RBD exhibit higher binding with ACE2 and lower affinity against monoclonal antibodies.