ArticleFrontiers in chemistry2021
Galectin-4 N-Terminal Domain: Binding Preferences Toward A and B Antigens With Different Peripheral Core Presentations.
Article in Frontiers in chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Human Milk Oligosaccharides Multivalently Presented on Defined Synthetic Neo-Glycoproteins Are Nanomolar Ligands of Tandem-Repeat Galectins.Biomacromolecules · 2025Article
- Exploring galectin interactions with human milk oligosaccharides and blood group antigens identifies BGA6 as a functional galectin-4 ligand.The Journal of biological chemistry · 2024Article
- The impact of glycosylation on the structure, function, and interactions of CD14.Glycobiology · 2024Article
- Insights into the recognition of hypermucoviscousFrontiers in immunology · 2024Article
- Oligosaccharide Ligands of Galectin-4 and Its Subunits: Multivalency Scores Highly.Molecules (Basel, Switzerland) · 2023Article
- Galectin-4 levels in hospitalized versus non-hospitalized subjects with obesity: the Malmö Preventive Project.Cardiovascular diabetology · 2022Article
- The Synthesis of Blood Group Antigenic A Trisaccharide and Its Biotinylated Derivative.Molecules (Basel, Switzerland) · 2021Article
- SelectiveAngewandte Chemie (International ed. in English) · 2021Article
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7 authors.
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Abstract
The tandem-repeat Galectin-4 (Gal-4) contains two different domains covalently linked through a short flexible peptide. Both domains have been shown to bind preferentially to A and B histo blood group antigens with different affinities, although the binding details are not yet available. The biological relevance of these associations is unknown, although it could be related to its attributed role in pathogen recognition. The presentation of A and B histo blood group antigens in terms of peripheral core structures differs among tissues and from that of the antigen-mimicking structures produced by pathogens. Herein, the binding of the N-terminal domain of Gal-4 toward a group of differently presented A and B oligosaccharide antigens in solution has been studied through a combination of NMR, isothermal titration calorimetry (ITC), and molecular modeling. The data presented in this paper allow the identification of the specific effects that subtle chemical modifications within this antigenic family have in the binding to the N-terminal domain of Gal-4 in terms of affinity and intermolecular interactions, providing a structural-based rationale for the observed trend in the binding preferences.
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