β-(1→3)-Glucans can be found as structural polysaccharides in cereals, in algae or as exo-polysaccharides secreted on the surfaces of mushrooms or fungi. Research has now established that β-(1→3)-glucans can trigger different immune responses and act as efficient immunostimulating agents. They constitute prevalent sources of carbons for microorganisms after subsequent recognition by digesting enzymes. Nevertheless, mechanisms associated with both roles are not yet clearly understood. This review focuses on the variety of elucidated molecular interactions that involve these natural or synthetic polysaccharides and their receptors, i.e., Dectin-1, CR3, glycolipids, langerin and carbohydrate-binding modules.
Keywords:
β-(1→3)-glucans; Dectin-1; CR3; glycolipids; langerin; CBM
β-(1→3)-Glucans are homopolymers of glucose where each unit is linked to the next by a β-(1→3) bond. They are known to interact with various receptors in humans, invertebrates or microorganisms. Such recognition triggered various responses like immune cascade or digestion. Strangely, most receptors that specifically recognize β-(1→3)-glucans share common characteristics and some show great homology. The mechanisms involved in immunological and inflammatory responses induced by β-glucans or the degradation of β-glucans are complex. They may depend on several factors: characteristics of the β-(1→3)-glucan (molecular weight, degree of branc
This 2015 Molecules review examined the molecular interactions between β-(1→3)-glucans and their cellular receptors, providing detailed mechanistic insight into β-glucan immune recognition.
Molecular docking and interaction studies revealed how β-(1→3)-glucan chains interact with Dectin-1, complement receptor 3, and scavenger receptors at the atomic level. Branching degree, molecular conformation, and chain length all influence receptor binding affinity and downstream immune activation. Soluble versus particulate forms of β-glucan engage different receptor combinations.
Atomic-level receptor interaction data provides the structural basis for understanding AP-glucan's immunostimulatory potency. The specific β-1,3/1,6 branching of AP-glucan predicts strong Dectin-1 engagement, validating its position as a highly bioactive β-glucan preparation.
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Legentil, Laurent; Paris, Franck; Ballet, Caroline; Trouvelot, Sophie; Daire, Xavier; Vetvicka, Vaclav; Ferrières, Vincent. Molecular Interactions of β-(1→3)-Glucans with Their Receptors. Molecules. 2015. DOI: 10.3390/molecules20069745.
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