ArticleBiomolecules2021
Mutations of SARS-CoV-2 RBD May Alter Its Molecular Structure to Improve Its Infection Efficiency.
Article in Biomolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- An inverse-protein-folding pre-trained model for predicting the mutational effects in protein-protein interactions.iScience · 2026Article
- SARS-CoV-2 spike mutations alter structure and energetics to modulate ACE2 binding immune evasion and viral adaptation.Scientific reports · 2025Article
- Mechanistic insights into the orthogonal functionality of an AHL-mediated quorum-sensing circuit inSynthetic and systems biotechnology · 2025Article
- Insights into the role of dynamical features in protein complex formation: The case of SARS-CoV-2 spike binding with ACE2.Computational and structural biotechnology journal · 2025Article
- Deep learning for discriminating non-trivial conformational changes in molecular dynamics simulations of SARS-CoV-2 spike-ACE2.Scientific reports · 2024Article
- Dynamics of SARS-CoV-2 Seroprevalence in a Large US population Over a Period of 12 Months.medRxiv : the preprint server for health sciences · 2023Article
- Article
- Digestive system infection by SARS‑CoV‑2: Entry mechanism, clinical symptoms and expression of major receptors (Review).International journal of molecular medicine · 2023Review
- Structure, dynamics and free energy studies on the effect of point mutations on SARS-CoV-2 spike protein binding with ACE2 receptor.PloS one · 2023Article
- Article
- Host adaptation of codon usage in SARS-CoV-2 from mammals indicates potential natural selection and viral fitness.Archives of virology · 2022Article
- SARS-CoV-2 Delta Variant: Interplay between Individual Mutations and Their Allosteric Synergy.Biomolecules · 2022Article
- Identification of Doxorubicin as Repurposing Inhibitory Drug for MERS-CoV PLpro.Molecules (Basel, Switzerland) · 2022Article
- Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2.Protein science : a publication of the Protein Society · 2022Article
- Mutation informatics: SARS-CoV-2 receptor-binding domain of the spike protein.Drug discovery today · 2022Review
- Computational Dissection of the Role of Trp305 in the Regulation of the Death-Associated Protein Kinase-Calmodulin Interaction.Biomolecules · 2022Article
- Spike protein of SARS-CoV-2 variants: a brief review and practical implications.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2022Review
- Impact of SARS-CoV-2 RBD Mutations on the Production of a Recombinant RBD Fusion Protein in Mammalian Cells.Biomolecules · 2022Article
- Understanding gilteritinib resistance to FLT3-F691L mutation through an integrated computational strategy.Journal of molecular modeling · 2022Article
- Review
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2 authors.
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Abstract
The receptor-binding domain (RBD) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) mediates the viral-host interaction and is a target for most neutralizing antibodies. Nevertheless, SARS-CoV-2 RBD mutations pose a threat due to their role in host cell entry via the human angiotensin-converting enzyme 2 receptor that might strengthen SARS-CoV-2 infectivity, viral load, or resistance against neutralizing antibodies. To understand the molecular structural link between RBD mutations and infectivity, the top five mutant RBDs (i.e., N501Y, E484K L452R, S477N, and N439K) were selected based on their recorded case numbers. These mutants along with wild-type (WT) RBD were studied through all-atom molecular dynamics (MD) simulations of 100 ns. The principal component analysis and the free energy landscape were used too. Interestingly, N501Y, N439K, and E484K mutations were observed to increase the rigidity in some RBD regions while increasing the flexibility of the receptor-binding motif (RBM) region, suggesting a compensation of the entropy penalty. However, S477N and L452R RBDs were observed to increase the flexibility of the RBM region while maintaining similar flexibility in other RBD regions in comparison to WT RBD. Therefore, both mutations (especially S477N) might destabilize the RBD structure, as loose conformation compactness was observed. The destabilizing effect of S477N RBD was consistent with previous work on S477N mutation. Finally, the free energy landscape results showed that mutations changed WT RBD conformation while local minima were maintained for all mutant RBDs. In conclusion, RBD mutations definitely impact the WT RBD structure and conformation as well as increase the binding affinity to angiotensin-converting enzyme receptor.
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