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Intestinal glycan receptors are a heterogeneous group of glycan-binding proteins (lectins) expressed by cells in the gut, including epithelial cells and immune cells. These receptors recognize and bind diverse carbohydrate structures (N- and O-linked glycans) present on mucins, microbial surfaces, and host glycoproteins. The interaction between glycan receptors and their ligands orchestrates mucosal immunity, barrier function, and the spatial organization of the gut microbiota. Aberrant glycosylation and altered expression of these receptors are implicated in the pathogenesis of inflammatory bowel disease, susceptibility to gastrointestinal infections, and even cancer. Therapeutic targeting of these receptors is an area of ongoing research, though their immense structural diversity and dynamic regulation present significant challenges.
Binding inhibition: blocking glycan-receptor interactions between host and microbes or between immune cells. Modulation of glycosylation: altering the structure of glycans to affect immune signaling, microbial adhesion, or epithelial integrity. Immune activation/inhibition: therapeutic lectins or antagonists may modulate immune signaling pathways.
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