Scanning the RBD-ACE2 molecular interactions in Omicron variant

The emergence of new SARS-CoV-2 variants poses a threat to the human population where it is difficult to assess the severity of a particular variant of the virus. Spike protein and specifically its receptor binding domain (RBD) which makes direct interaction with the ACE2 receptor of the human has shown prominent amino acid substitutions in most of the Variants of Concern. Here, by using all-atom molecular dynamics simulations we compare the interaction of Wild-type RBD/ACE2 receptor complex with that of the latest Omicron variant of the virus. We observed a very interesting diversification of the charge, dynamics and energetics of the protein complex formed upon mutations. These results would help us in understanding the molecular basis of binding of the Omicron variant with that of SARS-CoV-2 Wild-type. (c) 2022 Elsevier Inc. All rights reserved.

Automated summary

The emergence of new SARS-CoV-2 variants poses a threat to the human population, and assessing their severity is challenging. This study compares the interaction of the wild-type and the latest Omicron variant using molecular dynamics simulations, revealing diverse changes in the properties of the mutated protein complex. These findings enhance our understanding of the binding mechanism between the Omicron variant and the wild-type SARS-CoV-2.