bioRxivBiophysics
Molecular Insights into the Differential Dynamics of SARS-CoV-2 Variants of Concern (VOCs)
Abstract
Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) has affected the lives and livelihood of millions of individuals around the world. It has mutated several times after its first inception, with an estimated two mutations occurring every month. Although we have been successful in developing vaccines against the virus, emergence of variants has enabled it to escape therapy. Few of the generated variants are also reported to be more infectious than the wild-type (WT). In this study, we analyze the attributes of all RBD/ACE2 complexes for the reported VOCs, namely, Alpha, Beta, Gamma, and Delta through computer simulations. Results indicate differences in orientation and binding energies of the VOCs from the WT. Overall, it was observed that electrostatic interactions play a major role in the binding of the complexes. Detailed residue level energetics revealed that the most prominent changes in interaction energies were seen particularly at the mutated residues which were present at RBD/ACE2 interface. We found that the Delta variant is one of the most tightly bound variants of SARS-CoV-2 with dynamics similar to WT. High binding affinity of RBD towards ACE2 is indicative of an increase in the viral transmission and infectivity. The details presented in our study would prove extremely useful for the design and development of effective therapeutic strategies for the emerging variants of the virus.
- organism: virus
- assay: structural biology
- research focus: host-pathogen & immune response
- approach: statistical model
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- SARS-CoV-2 variants impact RBD conformational dynamics and ACE2 accessibility
M. F. Valerio, L. Borges-Araujo, … C. M. Soares·bioRxiv·Nov 30, 2021
- Decomposition of the SARS-CoV-2-ACE2 interface reveals a common trend among emerging viral variants
Eileen Socher, Marcus Conrad, … Philipp Arnold·Journal of Cellular BiochemistryPeer-reviewed·Sep 13, 2021
- Subtle changes at the RBD/hACE2 interface during SARS-CoV2 variant evolution: a molecular dynamics study
Aria Gheeraert, Vincent Leroux, … Laurent Chaloin·BiomoleculesPeer-reviewed·Apr 7, 2025
- Scanning the RBD-ACE2 molecular interactions in Omicron variant
S. L. Rath, A. K. Padhi, N. Mandal·bioRxiv·Dec 12, 2021
- Binding of Human ACE2 and RBD of Omicron Enhanced by Unique Interaction Patterns Among SARS-CoV-2 Variants of Concern
- Mutations on RBD of SARS-CoV-2 Omicron variant result in stronger binding to human ACE2 receptor
Cecylia S. Lupala, Yongjin Ye, … Haiguang Liu·Biochemical and Biophysical Research CommunicationsPeer-reviewed·Dec 24, 2021