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Host enterocyte cell-surface glycan refers to the diverse array of complex carbohydrate structures, including glycoproteins and glycolipids, found on the apical surface of intestinal epithelial cells (enterocytes). These glycans are essential for maintaining the intestinal mucosal barrier and facilitating critical cell-cell communication and recognition processes (Bode, 2012, Glycobiology). However, they also serve as primary attachment factors or receptors for a wide range of enteric pathogens, including Norovirus, Rotavirus, and bacterial toxins like the cholera toxin (Tan & Jiang, 2014, Nature Reviews Microbiology). For example, the expression of specific histo-blood group antigens (HBGAs) on the enterocyte surface determines an individual's susceptibility to certain Norovirus strains, a trait linked to the FUT2 secretor status (McGovern et al., 2010, Nature Genetics). Therapeutic interventions targeting these glycans typically employ glycan mimetics or soluble decoy receptors, such as human milk oligosaccharides (HMOs), to competitively inhibit pathogen binding and prevent infection (Hu et al., 2012, Nature). While promising, these strategies must account for the potential disruption of the host's commensal microbiota, which also interacts with these glycan structures. Overall, the study of enterocyte glycans is vital for developing novel anti-infective agents and understanding the genetic basis of host-pathogen interactions in the gut.
Competitive inhibition of pathogen adhesion by acting as decoy receptors or blocking binding sites on the host cell surface.
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