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Host intestinal epithelial cell glycans and gangliosides are complex carbohydrate structures and sialic acid-containing glycosphingolipids located on the apical surface of enterocytes (Varki et al., 2017). They serve as critical attachment sites and receptors for a wide variety of enteric pathogens, including bacteria like Vibrio cholerae and viruses such as Rotavirus (Schengrund, 2015; Ramani et al., 2016). For instance, the ganglioside GM1 is the primary receptor for the cholera toxin, facilitating its entry into the cell and subsequent induction of secretory diarrhea (Schengrund, 2015). Beyond pathogen binding, these molecules play essential roles in maintaining the intestinal barrier, mediating cell-cell interactions, and modulating local immune responses (Varki et al., 2017). Therapeutic strategies targeting these structures often involve the use of glycan decoys, such as human milk oligosaccharides, to competitively inhibit pathogen attachment (Ramani et al., 2016). Understanding the diversity of these glycans is crucial for developing treatments against infectious diseases and inflammatory bowel conditions.
Competitive inhibition of pathogen and toxin binding to host cell surface glycoconjugates, or enzymatic modification of these receptors to prevent attachment.
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