ArticleScientific reports2021
S494 O-glycosylation site on the SARS-CoV-2 RBD affects the virus affinity to ACE2 and its infectivity; a molecular dynamics study.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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18 citing papers in PubMed, 27 citations in OpenAlex.
- Glycan-binding properties of SARS-CoV-2 spike proteins: interactions with aminoglycoside antibiotics.Scientific reports · 2026Article
- The effect of cysteine oxidation on conformational changes of SARS-CoV-2 spike protein using atomistic simulations.Scientific reports · 2025Article
- O-glycosylation of SARS-CoV-2 spike protein by host O-glycosyltransferase strengthens its trimeric structure.Acta biochimica et biophysica Sinica · 2024Article
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- Efficient Expression inMolecules (Basel, Switzerland) · 2024Article
- Many Roles of Carbohydrates: A Computational Spotlight on the Coronavirus S Protein Binding.ACS applied bio materials · 2024Review
- Site-Specific O-glycosylation of SARS-CoV-2 Spike Protein and Its Impact on Immune and Autoimmune Responses.Cells · 2024Review
- Computational design and investigation of the monomeric spike SARS-CoV-2-ferritin nanocage vaccine stability and interactions.Frontiers in molecular biosciences · 2024Article
- Plant lectins as versatile tools to fight coronavirus outbreaks.Glycoconjugate journal · 2023Review
- Structural arrangement of the active back-to-back dimer in N-glycosylated ErbB receptors is regulated by heterodimerization.Molecular biology research communications · 2023Article
- Conformational Dynamics of the Receptor-Binding Domain of the SARS-CoV-2 Spike Protein.Biomedicines · 2022Article
- Exploring the Potential of Chemical Inhibitors for Targeting Post-translational Glycosylation of Coronavirus (SARS-CoV-2).ACS omega · 2022Review
- The structural role of SARS-CoV-2 genetic background in the emergence and success of spike mutations: The case of the spike A222V mutation.PLoS pathogens · 2022Article
- Implications of the Immune Polymorphisms of the Host and the Genetic Variability of SARS-CoV-2 in the Development of COVID-19.Viruses · 2022Review
- In silico design of refined ferritin-SARS-CoV-2 glyco-RBD nanoparticle vaccine.Frontiers in molecular biosciences · 2022Article
- Lentil lectin derived fromEmerging microbes & infections · 2021Article
- Glycosylation promotes the cancer regulator EGFR-ErbB2 heterodimer formation - molecular dynamics study.Journal of molecular modeling · 2021Article
- The glycosylation in SARS-CoV-2 and its receptor ACE2.Signal transduction and targeted therapy · 2021Review
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SARS-CoV-2 is a strain of Coronavirus family that caused the ongoing pandemic of COVID-19. Several studies showed that the glycosylation of virus spike (S) protein and the Angiotensin-Converting Enzyme 2 (ACE2) receptor on the host cell is critical for the virus infectivity. Molecular Dynamics (MD) simulations were used to explore the role of a novel mutated O-glycosylation site (D494S) on the Receptor Binding Domain (RBD) of S protein. This site was suggested as a key mediator of virus-host interaction. By exploring the dynamics of three O-glycosylated models and the control systems of unglcosylated S4944 and S494D complexes, it was shown that the decoration of S494 with elongated O-glycans results in stabilized interactions on the direct RBD-ACE2. Calculation of the distances between RBD and two major H1, H2 helices of ACE2 and the interacting pairs of amino acids in the interface showed that the elongated O-glycan maintains these interactions by forming several polar contacts with the neighbouring residues while it would not interfere in the direct binding interface. Relative binding free energy of RBD-ACE2 is also more favorable in the O-glycosylated models with longer glycans. The increase of RBD binding affinity to ACE2 depends on the size of attached O-glycan. By increasing the size of O-glycan, the RBD-ACE2 binding affinity will increase. Hence, this crucial factor must be taken into account for any further inhibitory approaches towards RBD-ACE2 interaction.
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