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The CfaE adhesin is the minor, tip-localized subunit of the CFA/I fimbriae, a filamentous structure on ETEC responsible for mediating the initial attachment to the epithelial surface of the human small intestine, a critical step in pathogen colonization and the pathogenesis of ETEC-induced diarrhea. Structurally, CfaE consists of two domains (an N-terminal adhesin domain and a C-terminal pilin domain), both showing immunoglobulin-like folds. The adhesin domain contains a specific receptor-binding pocket necessary for hemagglutination and host-cell specificity. CfaE is a member of the chaperone-usher pathway pilus assembly proteins and shares functional and structural similarities with other bacterial adhesins like FimH. Its role as the tip adhesin makes it a promising candidate for anti-adhesion therapies and vaccines targeting ETEC infections.
Drug or antibody binding inhibits the adhesion of ETEC to host intestinal epithelial cells, blocking the establishment of infection
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