Host intestinal epithelial glycoconjugates

Host intestinal epithelial glycoconjugates are a heterogeneous group of carbohydrate-containing molecules, including glycoproteins and glycolipids, expressed on the apical surface of human enterocytes (Sjöberg et al., 1988, PubMed: 2831155). These molecules function as essential receptors for the Colonization Factor Antigen II (CFA/II) fimbriae of Enterotoxigenic Escherichia coli (ETEC), a leading cause of traveler's diarrhea and childhood mortality in developing nations (Wennerås et al., 1990, PubMed: 2185310). The CFA/II complex, comprising the CS1, CS2, and CS3 adhesins, specifically recognizes and binds to terminal sugar moieties such as sialic acid (N-acetylneuraminic acid) and potentially sulfated glycans on the host cell membrane (Madhun et al., 2005, PubMed: 15659434). This high-affinity binding facilitates bacterial colonization and the subsequent delivery of heat-labile (LT) and heat-stable (ST) toxins into the host cells (Fleckenstein et al., 2010, PubMed: 20339537). Because this adhesion step is a prerequisite for infection, these glycoconjugates are significant targets for the development of anti-adhesive therapies, including decoy oligosaccharides and glycomimetic drugs (Shoaf-Sweeney & Hutkins, 2009, PubMed: 18703114). Research into these targets aims to provide non-antibiotic alternatives for preventing ETEC-mediated enteric diseases by blocking the initial attachment phase of the pathogen.

Other names

ETEC CFA/II receptorsIntestinal cell surface glycansSialylated glycoconjugatesCS1/CS2/CS3 receptors

Competitive inhibition of bacterial fimbrial adhesion to host cell surfaces