ArticleThe journal of physical chemistry letters2022
Binding Interactions between Receptor-Binding Domain of Spike Protein and Human Angiotensin Converting Enzyme-2 in Omicron Variant.
Article in The journal of physical chemistry letters, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.
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Who cites it
44 citing papers in PubMed, 73 citations in OpenAlex.
- Scalable and sustainable manufacturing of functional DNA nanoassemblies via self-folding circular single-stranded DNA.Nature communications · 2026Article
- Glycans Modulate the Adsorption of RBD Glycoproteins on Polarizable Surfaces.Journal of chemical information and modeling · 2026Article
- Analysis of the Relationship Between the Charge Increment of the SARS-CoV-2 Spike Protein and Evolution.Viruses · 2025Article
- Carrageenans and the Carrageenan-Echinochrome Complex as Anti-SARS-CoV-2 Agents.International journal of molecular sciences · 2025Article
- Electronic Interactions Between the Receptor-Binding Domain of Omicron Variants and Angiotensin-Converting Enzyme 2: A Novel Amino Acid-Amino Acid Bond Pair Concept.Molecules (Basel, Switzerland) · 2025Article
- Structural and Energetic Insights into SARS-CoV-2 Evolution: Analysis of hACE2-RBD Binding in Wild-Type, Delta, and Omicron Subvariants.International journal of molecular sciences · 2025Article
- The Compensatory Effect of S375F on S371F Is Vital for Maintaining the Infectivity of SARS-CoV-2 Omicron Variants.Journal of medical virology · 2025Article
- Impact of COVID-19 on Ocular Surface Health: Infection Mechanisms, Immune Modulation, and Inflammatory Responses.Viruses · 2025Review
- Article
- Comprehensive N-glycosylation profiling of recombinant spike S1 protein from the wild-type SARS-CoV-2 and its variants.Frontiers in immunology · 2025Article
- Increased preference for lysine over arginine in spike proteins of SARS-CoV-2 BA.2.86 variant and its daughter lineages.PloS one · 2025Article
- Evaluation of Angiotensin-Converting Enzyme 2 ExpressionACS pharmacology & translational science · 2024Article
- Adsorption-Driven Deformation and Footprints of the RBD Proteins in SARS-CoV-2 Variants on Biological and Inanimate Surfaces.Journal of chemical information and modeling · 2024Article
- Interaction of Receptor-Binding Domain of the SARS-CoV-2 Omicron Variant with hACE2 and Actin.Cells · 2024Article
- Article
- Longitudinal analysis of genomic mutations in SARS-CoV-2 isolates from persistent COVID-19 patient.iScience · 2024Article
- SARS-CoV-2 Omicron Subvariants Do Not Differ Much in Binding Affinity to Human ACE2: A Molecular Dynamics Study.The journal of physical chemistry. B · 2024Article
- The Diverse Nature of the Molecular Interactions That Govern the COV-2 Variants' Cell Receptor Affinity Ranking and Its Experimental Variability.International journal of molecular sciences · 2024Article
- Three-Dimensional Structural Stability and Local Electrostatic Potential at Point Mutations in Spike Protein of SARS-CoV-2 Coronavirus.International journal of molecular sciences · 2024Article
- Deciphering the free energy landscapes of SARS-CoV-2 wild type and Omicron variant interacting with human ACE2.The Journal of chemical physics · 2024Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The emergence of new SARS-CoV-2 Omicron variant of concern (OV) has exacerbated the COVID-19 pandemic because of a large number of mutations in the spike protein, particularly in the receptor-binding domain (RBD), resulting in highly contagious and/or vaccine-resistant strains. Herein, we present a systematic analysis based on detailed molecular dynamics (MD) simulations in order to understand how the OV RBD mutations affect the ACE2 binding. We show that the OV RBD binds to ACE2 more efficiently and tightly predominantly because of strong electrostatic interactions, thereby promoting increased infectivity and transmissibility compared to other strains. Some of the OV RBD mutations are predicted to affect the antibody neutralization either through their role in the S-protein conformational changes, such as S371L, S373P, and S375F, or through changing its surface charge distribution, such as G339D, N440K, T478K, and E484A. Other mutations, such as K417N, G446S, and Y505H, decrease the ACE2 binding, whereas S447N, Q493R, G496S, Q498R, and N501Y tend to increase it.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.