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Intestinal epithelial cell surface glycans, collectively forming the glycocalyx, are complex carbohydrate structures covalently linked to proteins and lipids on the apical surface of enterocytes (UniProt, 2023). These glycans serve as a critical interface between the host and the intestinal lumen, facilitating nutrient absorption and providing a protective barrier against mechanical and chemical stress (PubMed, PMID: 22531130). They play a pivotal role in host-microbe interactions, acting as attachment sites for commensal bacteria and as receptors for various enteric pathogens, including Norovirus, Rotavirus, and Vibrio cholerae (NCBI, PMC3145120). In diseases such as inflammatory bowel disease (IBD) and colorectal cancer, the glycosylation patterns are significantly altered, often characterized by reduced complexity or aberrant expression of specific antigens like Sialyl-Lewis X (PubMed, PMID: 21464369). Therapeutic interventions target these glycans using glycomimetics or human milk oligosaccharides (HMOs), which function as decoy receptors to prevent pathogen binding and promote a healthy microbiome (PubMed, PMID: 22513079). These strategies aim to restore the natural barrier function and prevent the initiation of infection or chronic inflammation.
Competitive inhibition of pathogen adhesion to host cell surface glycans and modulation of the mucosal immune response (PubMed, PMID: 22513079).
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