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Intestinal epithelial cell surface mannose-containing glycoconjugates are a heterogeneous group of glycoproteins and glycolipids located on the apical membrane of the intestinal epithelium. These molecules serve as critical attachment sites for various pathogenic microorganisms, particularly Enterobacteriaceae like Escherichia coli, which utilize mannose-specific adhesins such as FimH to colonize the gut (Barnich et al., 2007; Spaulding et al., 2017). In the context of inflammatory bowel diseases, specifically Crohn's disease, the expression of certain mannosylated receptors like CEACAM6 is significantly upregulated, promoting the persistence of Adherent-Invasive E. coli (AIEC) and exacerbating mucosal inflammation (Barnich et al., 2007). Therapeutic interventions targeting these glycoconjugates typically involve small-molecule mannosides or FimH antagonists that competitively block the interaction between the bacterial adhesin and the host cell surface (Sivignon et al., 2015). Additionally, these glycoconjugates are utilized in pharmacological research as targets for mannose-functionalized drug delivery systems designed to improve the oral bioavailability and targeted delivery of therapeutics to the intestinal mucosa (Mydock-McGrane et al., 2016).
Competitive inhibition of bacterial adhesins (such as FimH) from binding to host mannosylated glycoconjugates, thereby preventing pathogen colonization and subsequent inflammatory responses.
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