ArticleFrontiers in cell and developmental biology2021
N439K Variant in Spike Protein Alter the Infection Efficiency and Antigenicity of SARS-CoV-2 Based on Molecular Dynamics Simulation.
Article in Frontiers in cell and developmental biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 35 citations in OpenAlex.
- Modeling the Mutational Effects on Biochemical Phenotypes of SARS-CoV-2 Using Molecular Fields.Biomolecules · 2025Article
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- Current Updates on Variants of SARS-CoV- 2: Systematic Review.Health science reports · 2024Review
- COVID-19 mutations: An overview.World journal of methodology · 2024Review
- Unveiling Inter- and Intra-Patient Sequence Variability with a Multi-Sample Coronavirus Target Enrichment Approach.Viruses · 2024Article
- COVID-19 Variants and Vaccine Development.Viruses · 2024Review
- N123I mutation in the ALV-J receptor-binding domain region enhances viral replication ability by increasing the binding affinity with chNHE1.PLoS pathogens · 2024Article
- Atomistic insights into the binding of SARS-CoV-2 spike receptor binding domain with the human ACE2 receptor: The importance of residue 493.Journal of molecular graphics & modelling · 2023Article
- Early detection and improved genomic surveillance of SARS-CoV-2 variants from deep sequencing data.iScience · 2022Article
- Tracking the molecular evolution and transmission patterns of SARS-CoV-2 lineage B.1.466.2 in Indonesia based on genomic surveillance data.Virology journal · 2022Article
- MutCov: A pipeline for evaluating the effect of mutations in spike protein on infectivity and antigenicity of SARS-CoV-2.Computers in biology and medicine · 2022Article
- An engineered bispecific human monoclonal antibody against SARS-CoV-2.Nature immunology · 2022Article
- Impact of mutations in SARS-COV-2 spike on viral infectivity and antigenicity.Briefings in bioinformatics · 2022Article
- Article
- Article
- A Detailed Overview of Immune Escape, Antibody Escape, Partial Vaccine Escape of SARS-CoV-2 and Their Emerging Variants With Escape Mutations.Frontiers in immunology · 2022Review
- Structural and functional insights into the spike protein mutations of emerging SARS-CoV-2 variants.Cellular and molecular life sciences : CMLS · 2021Review
- Predicting Mutational Effects on Receptor Binding of the Spike Protein of SARS-CoV-2 Variants.Journal of the American Chemical Society · 2021Article
- Computational prediction of the effect of amino acid changes on the binding affinity between SARS-CoV-2 spike RBD and human ACE2.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Role of SARS-CoV-2 and ACE2 variations in COVID-19.Biomedical journal · 2021Review
Corrections and comments
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Authors and funding
13 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), causing an outbreak of coronavirus disease 2019 (COVID-19), has been undergoing various mutations. The analysis of the structural and energetic effects of mutations on protein-protein interactions between the receptor binding domain (RBD) of SARS-CoV-2 and angiotensin converting enzyme 2 (ACE2) or neutralizing monoclonal antibodies will be beneficial for epidemic surveillance, diagnosis, and optimization of neutralizing agents. According to the molecular dynamics simulation, a key mutation N439K in the SARS-CoV-2 RBD region created a new salt bridge with Glu329 of hACE2, which resulted in greater electrostatic complementarity, and created a weak salt bridge with Asp442 of RBD. Furthermore, the N439K-mutated RBD bound hACE2 with a higher affinity than wild-type, which may lead to more infectious. In addition, the N439K-mutated RBD was markedly resistant to the SARS-CoV-2 neutralizing antibody REGN10987, which may lead to the failure of neutralization. The results show consistent with the previous experimental conclusion and clarify the structural mechanism under affinity changes. Our methods will offer guidance on the assessment of the infection efficiency and antigenicity effect of continuing mutations in SARS-CoV-2.
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