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Host intestinal glycan receptors are complex carbohydrate structures, including glycoproteins and glycolipids, expressed on the apical surface of intestinal epithelial cells and within the protective mucus layer (Varki et al., Essentials of Glycobiology, 2017). These glycans, such as sialic acids, fucose, and histo-blood group antigens (HBGAs), serve as essential docking sites for a wide array of enteric pathogens, including Norovirus, Rotavirus, Helicobacter pylori, and various Escherichia coli strains (Ruvoen-Clouet et al., Glycoconj J, 2015). By recognizing specific glycan motifs, these pathogens can adhere to the host mucosa, resist mechanical clearance, and initiate infection or toxin delivery. Beyond their role in pathogenesis, these glycans are critical for the stable colonization of beneficial commensal microbiota and contribute to the structural integrity of the mucosal barrier. Therapeutic strategies targeting these receptors often involve the use of glycan mimetics, such as human milk oligosaccharides (HMOs), which act as soluble decoys to intercept pathogens before they can bind to the intestinal wall (Bode, Glycobiology, 2012). Understanding the diversity of these glycan structures is vital for developing precision anti-adhesion therapies and managing susceptibility to gastrointestinal diseases based on an individual's genetic glycan profile, such as their secretor status.
Competitive inhibition of pathogen adhesion by acting as soluble decoy receptors (glycan mimetics) or by blocking host glycan recognition sites on microbial lectins.
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