ArticleProceedings of the National Academy of Sciences of the United States of America2021
Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers.
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Who cites it
125 citing papers in PubMed, 197 citations in OpenAlex.
- Glycosylation-modulated conformational diversity in neurotrophin receptors.Biophysical journal · 2026Article
- Exploring the diverse binding ability of SARS-CoV-2 variant RBDs to different antibody classes: a computational study.RSC advances · 2026Article
- Glycans Modulate the Adsorption of RBD Glycoproteins on Polarizable Surfaces.Journal of chemical information and modeling · 2026Article
- Cryo-EM structure of locked spike glycoprotein from bat SARS-like coronavirus WIV1, molecular dynamics and biophysics across host range.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Systems biology and microbiome innovations for personalized diabetic retinopathy management.NPJ systems biology and applications · 2025Review
- SARS-CoV-2 spike mutations alter structure and energetics to modulate ACE2 binding immune evasion and viral adaptation.Scientific reports · 2025Article
- Key β1-4 galactosylated glycan receptors of SARS-CoV-2 and its inhibitor from the galactosylated glycoproteins of bovine milk.Journal of advanced research · 2025Article
- Molecular dissection of the role of ACE2 in glucose homeostasis.Physiological reviews · 2025Review
- Membrane-wide screening identifies potential tissue-specific determinants of SARS-CoV-2 tropism.PLoS pathogens · 2025Article
- Role of N-linked glycosylation sites in human ACE2 in SARS-CoV-2 and hCoV-NL63 infection.Journal of virology · 2025Article
- Evolution of Antiviral Drug Resistance in SARS-CoV-2.Viruses · 2025Review
- A short intrinsically disordered region at KtrB's N-terminus facilitates allosteric regulation of KNature communications · 2025Article
- Molecular mechanisms of RaTG13 and SARS-CoV-2 RBD bound to Rhinolophus affinis bat ACE2.Protein science : a publication of the Protein Society · 2025Article
- A Reflection on the Use of Molecular Simulation to Respond to SARS-CoV-2 Pandemic Threats.The journal of physical chemistry letters · 2025Review
- Exploring the effects of N234 and N343 linked glycans to SARS CoV 2 spike protein pocket accessibility using Gaussian accelerated molecular dynamics simulations.Scientific reports · 2025Article
- Systematic Approach to Parametrization of Disaccharides for the Martini 3 Coarse-Grained Force Field.Journal of chemical information and modeling · 2025Article
- SARS-CoV-2 drug resistance and therapeutic approaches.Heliyon · 2025Review
- Viral Mimetic Bacterial Outer Membrane Vesicles for Targeting Angiotensin-Converting Enzyme 2.International journal of nanomedicine · 2025Article
- Integration of Experimental and Computational Methods to Characterize Glycoproteins.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Characterization of Site-Specific N- and O-Glycopeptides from Recombinant Spike and ACE2 Glycoproteins Using LC-MS/MS Analysis.International journal of molecular sciences · 2024Article
65 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Binding of the spike protein of SARS-CoV-2 to the human angiotensin-converting enzyme 2 (ACE2) receptor triggers translocation of the virus into cells. Both the ACE2 receptor and the spike protein are heavily glycosylated, including at sites near their binding interface. We built fully glycosylated models of the ACE2 receptor bound to the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Using atomistic molecular dynamics (MD) simulations, we found that the glycosylation of the human ACE2 receptor contributes substantially to the binding of the virus. Interestingly, the glycans at two glycosylation sites, N90 and N322, have opposite effects on spike protein binding. The glycan at the N90 site partly covers the binding interface of the spike RBD. Therefore, this glycan can interfere with the binding of the spike protein and protect against docking of the virus to the cell. By contrast, the glycan at the N322 site interacts tightly with the RBD of the ACE2-bound spike protein and strengthens the complex. Remarkably, the N322 glycan binds to a conserved region of the spike protein identified previously as a cryptic epitope for a neutralizing antibody. By mapping the glycan binding sites, our MD simulations aid in the targeted development of neutralizing antibodies and SARS-CoV-2 fusion inhibitors.
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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.