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Intestinal epithelial surface and mucosal glycan structures are complex carbohydrate chains attached to proteins and lipids that form the glycocalyx and the mucus layer of the gastrointestinal tract (Tailford et al., 2015, Mucin glycan foraging in the human gut microbiome). These structures, primarily composed of O-glycans on mucins like MUC2, serve as a critical physical and chemical barrier that protects the underlying epithelium from mechanical stress and enzymatic degradation (Robbe et al., 2004, Evidence of glycosylation changes in the colonic mucosa of patients with inflammatory bowel diseases). They play a pivotal role in host-microbe interactions by providing attachment sites and metabolic substrates for commensal bacteria while acting as decoy receptors to sequester pathogens and toxins (Newburg et al., 2005, Human milk glycans as innate resistance factors). In diseases such as inflammatory bowel disease (IBD) and colorectal cancer, the glycosylation patterns—such as fucosylation and sialylation—are significantly altered, contributing to barrier dysfunction and dysbiosis (Koropatkin et al., 2012, Glycan metabolism in the human gut microbiota). Therapeutic strategies targeting these glycans include the use of glycan mimetics like 2'-fucosyllactose to block pathogen adhesion and mucosal protectants like sucralfate to reinforce the barrier (Morrow et al., 2004, Human milk oligosaccharides are associated with protection against diarrhea).
Competitive inhibition of pathogen adhesion and restoration of mucosal barrier integrity
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