Structural analysis of spike proteins from SARS-CoV-2 variants of concern highlighting their functional alterations
Future virology
; 2022.
Article
in English
| EuropePMC | ID: covidwho-1970897
ABSTRACT
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 S-RBD as compared with wild-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 SARS-CoV-2, Omicron S-RBD exhibit higher binding with ACE2 and lower affinity against monoclonal antibodies.
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Collection:
Databases of international organizations
Database:
EuropePMC
Topics:
Variants
Language:
English
Journal:
Future virology
Year:
2022
Document Type:
Article
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