ArticleJournal of molecular biology2021
Subtle Influence of ACE2 Glycan Processing on SARS-CoV-2 Recognition.
Article in Journal of molecular biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 75 citations in OpenAlex.
- Species- and variant-specific ACE2 compatibility shapes SARS-CoV-2 spillover potential in North American cervids.Nature communications · 2026Article
- 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
- Comprehensive analysis of SARS-CoV-2 Spike evolution: epitope classification and immune escape prediction.Virus evolution · 2025Article
- Viral Mimetic Bacterial Outer Membrane Vesicles for Targeting Angiotensin-Converting Enzyme 2.International journal of nanomedicine · 2025Article
- Characterization of biotinylated human ACE2 and SARS-CoV-2 Omicron BA.4/5 spike protein reference materials.Analytical and bioanalytical chemistry · 2024Article
- N-glycosylation of the SARS-CoV-2 spike protein at Asn331 and Asn343 is involved in spike-ACE2 binding, virus entry, and regulation of IL-6.Microbiology and immunology · 2024Article
- Role of N-linked glycosylation in porcine reproductive and respiratory syndrome virus (PRRSV) infection.The Journal of general virology · 2024Article
- Many Roles of Carbohydrates: A Computational Spotlight on the Coronavirus S Protein Binding.ACS applied bio materials · 2024Review
- Microfluidic Diffusion Sizing Applied to the Study of Natural Products and Extracts That Modulate the SARS-CoV-2 Spike RBD/ACE2 Interaction.Molecules (Basel, Switzerland) · 2023Article
- Biophysical evolution of the receptor-binding domains of SARS-CoVs.Biophysical journal · 2023Article
- Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.PLoS pathogens · 2023Article
- Site specific N- and O-glycosylation mapping of the spike proteins of SARS-CoV-2 variants of concern.Scientific reports · 2023Article
- Regulation of angiotensin-converting enzyme 2 isoforms by type 2 inflammation and viral infection in human airway epithelium.Mucosal immunology · 2023Article
- Plant lectins as versatile tools to fight coronavirus outbreaks.Glycoconjugate journal · 2023Review
- Identification of host receptors for viral entry and beyond: a perspective from the spike of SARS-CoV-2.Frontiers in microbiology · 2023Review
- Glycosylation in SARS-CoV-2 variants: A path to infection and recovery.Biochemical pharmacology · 2022Review
- The Role of Host Cell Glycans on Virus Infectivity: The SARS-CoV-2 Case.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2022Article
- Site Specific N- and O-glycosylation mapping of the Spike Proteins of SARS-CoV-2 Variants of Concern.Research square · 2022Article
- Direct discrimination of cell surface glycosylation signatures using a single pH-responsive boronic acid-functionalized polymer.Chemical science · 2022Article
- ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner.Communications biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The severity of SARS-CoV-2 infection is highly variable and yet the molecular basis for this effect remains elusive. One potential contribution are differences in the glycosylation of target human cells, particularly as SARS-CoV-2 has the capacity to bind sialic acid which is a common, and highly variable, terminal modification of glycans. The viral spike glycoprotein (S) of SARS-CoV-2 and the human cellular receptor, angiotensin-converting enzyme 2 (ACE2) are both densely glycosylated. We therefore sought to investigate whether the glycosylation state of ACE2 impacts the interaction with SARS-CoV-2 viral spike. We generated a panel of engineered ACE2 glycoforms which were analyzed by mass spectrometry to reveal the site-specific glycan modifications. We then probed the impact of ACE2 glycosylation on S binding and revealed a subtle sensitivity with hypersialylated or oligomannose-type glycans slightly impeding the interaction. In contrast, deglycosylation of ACE2 did not influence SARS-CoV-2 binding. Overall, ACE2 glycosylation does not significantly influence viral spike binding. We suggest that any role of glycosylation in the pathobiology of SARS-CoV-2 will lie beyond its immediate impact of receptor glycosylation on virus binding.
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Registered trials
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.