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

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posted on 2022-08-02, 09:18 authored by Kundan Solanki, Sajjan Rajpoot, Ashutosh Kumar, Kam Y J Zhang, Tomokazu Ohishi, Nik Hirani, Khandu Wadhonkar, Pramod Patidar, Qiuwei Pan, Mirza S Baig

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.


This work is supported by Cumulative Professional Development Allowance (CPDA) and Research Development Fund (RDF) from the Indian Institute of Technology Indore (IITI) to MS Baig.


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