ArticleProceedings of the National Academy of Sciences of the United States of America2021
Glycocalyx crowding with mucin mimetics strengthens binding of soluble and virus-associated lectins to host cell glycan receptors.
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 21 papers.
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Who cites it
21 citing papers in PubMed, 32 citations in OpenAlex.
- Mucins and Respiratory Virus Infection.Annual review of virology · 2026Review
- Chemically Masked aPD-L1-Sialidase Conjugate for Tumor-Specific Desialylation and Immunotherapy.Angewandte Chemie (International ed. in English) · 2026Article
- Multivalency influences virus dynamics at the glycocalyx: A study of glycosaminoglycan binding in HPV16 entry.Biophysical journal · 2026Article
- Diacetylene-Functionalized Glycan Mimetics for Receptor-Mediated Cluster Imprinting in Model Membranes.Macromolecular rapid communications · 2026Article
- Glycocalyx micro- and nanodomains in cell-cell and cell-matrix interactions revealed by enhanced click chemistry.Nature communications · 2026Article
- Glycocalyx at the host-virus interface: a double-edged sword in virus infection and tissue damage.Frontiers in molecular biosciences · 2026Review
- Membrane-Inserting α‑Lipid Polymers: Understanding Lipid Membrane Insertion and Effect on Membrane Fluidity.Chemistry of materials : a publication of the American Chemical Society · 2025Article
- Molecularly Defined Glycocalyx Models Reveal ABJACS Au · 2025Article
- ThePolymers · 2024Review
- Sialic acids in infection and their potential use in detection and protection against pathogens.RSC chemical biology · 2024Review
- Glycosylated extracellular mucin domains protect against SARS-CoV-2 infection at the respiratory surface.PLoS pathogens · 2023Article
- Antibody binding reports spatial heterogeneities in cell membrane organization.Nature communications · 2023Article
- Molecular Recognition of Glycan-Bearing Glycomacromolecules Presented at Membrane Surfaces by Lectins: An NMR View.ACS omega · 2023Article
- Catanionic Vesicles as a Facile Scaffold to Display Natural N-Glycan Ligands for Probing Multivalent Carbohydrate-Lectin Interactions.Bioconjugate chemistry · 2023Article
- Surface-Templated Glycopolymer Nanopatterns Transferred to Hydrogels for Designed Multivalent Carbohydrate-Lectin Interactions across Length Scales.Journal of the American Chemical Society · 2023Article
- Measuring the multifaceted roles of mucin-domain glycoproteins in cancer.Advances in cancer research · 2023Review
- Synthesis and biomedical applications of mucin mimic materials.Advanced drug delivery reviews · 2022Review
- Membrane attachment and fusion of HIV-1, influenza A, and SARS-CoV-2: resolving the mechanisms with biophysical methods.Biophysical reviews · 2022Review
- Polymers Inspired by Heparin and Heparan Sulfate for Viral Targeting.Macromolecules · 2022Review
- Cell surface photoengineering enables modeling of glycocalyx shedding dynamics.Chemical science · 2022Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Membrane-associated mucins protect epithelial cell surfaces against pathogenic threats by serving as nonproductive decoys that capture infectious agents and clear them from the cell surface and by erecting a physical barrier that restricts their access to target receptors on host cells. However, the mechanisms through which mucins function are still poorly defined because of a limited repertoire of tools available for tailoring their structure and composition in living cells with molecular precision. Using synthetic glycopolymer mimetics of mucins, we modeled the mucosal glycocalyx on red blood cells (RBCs) and evaluated its influence on lectin (SNA) and virus (H1N1) adhesion to endogenous sialic acid receptors. The glycocalyx inhibited the rate of SNA and H1N1 adhesion in a size- and density-dependent manner, consistent with the current view of mucins as providing a protective shield against pathogens. Counterintuitively, increasing the density of the mucin mimetics enhanced the retention of bound lectins and viruses. Careful characterization of SNA behavior at the RBC surface using a range of biophysical and imaging techniques revealed lectin-induced crowding and reorganization of the glycocalyx with concomitant enhancement in lectin clustering, presumably through the formation of a more extensive glycan receptor patch at the cell membrane. Our findings indicate that glycan-targeting pathogens may exploit the biophysical and biomechanical properties of mucins to overcome the mucosal glycocalyx barrier.
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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.