Host intestinal epithelial receptors for Enterotoxigenic Escherichia coli colonization factors (ETEC CF receptors)

Host intestinal epithelial receptors for Enterotoxigenic Escherichia coli (ETEC) colonization factors (CFs) are a diverse set of cell-surface molecules that mediate the initial attachment of the pathogen to the host gut mucosa. These receptors primarily consist of glycoproteins and glycosphingolipids, with the carcinoembryonic antigen-related cell adhesion molecule (CEACAM) family—specifically CEACAM1, CEACAM5, and CEACAM6—serving as critical binding sites for class 5 fimbriae such as CFA/I (Korotkova et al., 2008, J Biol Chem). Other ETEC colonization factors recognize carbohydrate moieties on blood group antigens, including H-type 1 and Lewis antigens, as well as specific glycolipids like sulfatide and GM1 (Fleckenstein et al., 2014, Biochim Biophys Acta). This adherence is essential for ETEC to resist peristaltic clearance, allowing the bacteria to colonize the small intestine and secrete enterotoxins that cause watery diarrhea (Madhavan et al., 2021, Front Cell Infect Microbiol). Consequently, these host receptors are significant targets for anti-adhesive therapeutic strategies, including the use of receptor-mimicking decoys, glycomimetic inhibitors, and vaccines designed to block the CF-receptor interface (Moonens et al., 2015, Nature Communications). Understanding the specificity of these interactions is vital for developing broad-spectrum interventions against the various ETEC strains that contribute to global diarrheal disease.

Other names

ETEC adhesion receptorsIntestinal epithelial cell receptors for ETECColonization factor receptorsHost receptors for ETEC fimbriaeETEC CF receptors

Competitive inhibition of the binding between bacterial colonization factors (fimbriae/pili) and host intestinal epithelial receptors (glycoproteins/glycolipids), preventing bacterial colonization and subsequent toxin delivery.