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CfaE is the **tip-localized minor adhesive subunit** of colonization factor antigen I (CFA/I) fimbriae found on the surface of enterotoxigenic *Escherichia coli* (ETEC)[7]. These fimbriae are composed of a polymerized stalk of major subunit CfaB and a single copy of CfaE at the tip, which initiates bacterial binding to host enterocytes in the small intestine, playing a critical role in the pathogenesis of ETEC-induced diarrhea[3][6][7]. CfaE comprises two main structural domains: an N-terminal adhesin domain (responsible for host receptor binding and hemagglutination) and a C-terminal pilin domain (required for incorporation into the pilus and stabilized by donor strand complementation with CfaB)[1][2][3][7][9]. CfaE exhibits **shear force-dependent binding** to host cells, enhancing adherence under physiological conditions similar to the “catch bond” mechanism of other bacterial adhesins like FimH[1][3][4][5]. CfaE is a major target for anti-adhesin vaccine development, with evidence that maternal immunization can confer protection to neonatal mice against ETEC colonization[8].\n\nNo established drugs yet interact with CfaE for therapeutic purposes, but it is a promising **candidate for intervention in ETEC infection** and for vaccine-related studies[8]. Its function and role in **fimbrial assembly**, specific host cell attachment, and disease initiation are well characterized structurally and functionally, making it a highly specific and valid target for intervention strategies against ETEC.
Inhibition of CfaE-host receptor interaction (by antibodies/vaccine-induced immunity or small-molecule inhibitors); Disruption of fimbriae assembly; Blockade of bacterial colonization initiation
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