ArticleFASEB journal : official publication of the Federation of American Societies for Experimental Biology2018
Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins.
Article in FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 2018. 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, 35 citations in OpenAlex.
- One-Step Microfluidic Manufactured Fucose-Decorated Sweetosomes Choose the Time and the Road for Their Intracellular Journey to Cancer Treatment.Advanced healthcare materials · 2026Article
- Intestinal Mucin Glycosylation: Structural Regulation, Homeostasis Maintenance and Disease Association.Biomolecules · 2025Review
- Targeting pattern recognition receptors for cancer therapy: Mechanisms and strategies.Acta pharmaceutica Sinica. B · 2025Review
- A Narrative Review on the Multifaceted Roles of Galectins in Host-Pathogen Interactions DuringInternational journal of molecular sciences · 2025Review
- The role of glycan-lectin interactions in the tumor microenvironment: immunosuppression regulators of colorectal cancer.American journal of cancer research · 2025Review
- The Dectin-1 and Dectin-2 clusters: C-type lectin receptors with fundamental roles in immunity.EMBO reports · 2024Review
- Article
- B3galt5 functions as a PXR target gene and regulates obesity and insulin resistance by maintaining intestinal integrity.Nature communications · 2024Article
- Human gut microbes express functionally distinct endoglycosidases to metabolize the same N-glycan substrate.Nature communications · 2024Article
- Dectin-1 as a therapeutic target for inflammatory bowel disease.Advances in pharmacology (San Diego, Calif.) · 2024Review
- Galectin 3 enhances platelet aggregation and thrombosis via Dectin-1 activation: a translational study.European heart journal · 2022Article
- The Role of C-Type Lectin Receptor Signaling in the Intestinal Microbiota-Inflammation-Cancer Axis.Frontiers in immunology · 2022Review
- Mechanism of Mucin Recognition by Lectins: A Thermodynamic Study.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Article
- Trefoil Factor Family (TFF) Peptides and Their Links to Inflammation: A Re-evaluation and New Medical Perspectives.International journal of molecular sciences · 2021Review
- Safety and Modulatory Effects of Humanized Galacto-Oligosaccharides on the Gut Microbiome.Frontiers in nutrition · 2021Article
- Intestinal epithelial glycosylation in homeostasis and gut microbiota interactions in IBD.Nature reviews. Gastroenterology & hepatology · 2020Review
- Could Galectin 3 Be a Good Prognostic Factor in Endometrial Cancer?Diagnostics (Basel, Switzerland) · 2020Article
- Structural basis of mammalian high-mannose N-glycan processing by human gut Bacteroides.Nature communications · 2020Article
- Biological and Technical Challenges in Unraveling the Role of N-Glycans in Immune Receptor Regulation.Frontiers in chemistry · 2020Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
Intestinal mucins trigger immune responses upon recognition by dendritic cells via protein-carbohydrate interactions. We used a combination of structural, biochemical, biophysical, and cell-based approaches to decipher the specificity of the interaction between mucin glycans and mammalian lectins expressed in the gut, including galectin (Gal)-3 and C-type lectin receptors. Gal-3 differentially recognized intestinal mucins with different O-glycosylation profiles, as determined by mass spectrometry (MS). Modification of mucin glycosylation, via chemical treatment leading to a loss of terminal glycans, promoted the interaction of Gal-3 to poly- N-acetyllactosamine. Specific interactions were observed between mucins and mouse dendritic cell-associated lectin (mDectin)-2 or specific intercellular adhesion molecule-grabbing nonintegrin-related-1 (SIGN-R1), but not mDectin-1, using a cell-reporter assay, as also confirmed by atomic force spectroscopy. We characterized the N-glycosylation profile of mouse colonic mucin (Muc)-2 by MS and showed that the interaction with mDectin-2 was mediated by high-mannose N-glycans. Furthermore, we observed Gal-3 binding to the 3 C-type lectins by force spectroscopy. We showed that mDectin-1, mDectin-2, and SIGN-R1 are decorated by N-glycan structures that can be recognized by the carbohydrate recognition domain of Gal-3. These findings provide a structural basis for the role of mucins in mediating immune responses and new insights into the structure and function of major mammalian lectins.-Leclaire, C., Lecointe, K., Gunning, P. A., Tribolo, S., Kavanaugh, D. W., Wittmann, A., Latousakis, D., MacKenzie, D. A., Kawasaki, N., Juge, N. Molecular basis for intestinal mucin recognition by galectin-3 and C-type lectins.
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Registered trials
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