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CfaE is the adhesive subunit at the tip of colonization factor antigen I (CFA/I) fimbriae in enterotoxigenic Escherichia coli (ETEC), responsible for the bacterium’s initial attachment to target cell receptors in the human small intestine during early diarrheal pathogenesis[1][6][7]. CfaE is essential for both the assembly of CFA/I pili and for mediating adhesion to host cells; specifically, it directs binding to host cell receptors such as asialo-GM1 and to erythrocyte receptors, playing a critical role in infection[1][4][6][7]. Structurally, CfaE features two domains (adhesin and pilin), both with immunoglobulin-like folds, and mutations in key residues (notably Arg181) abolish its adhesive function while preserving pilus assembly[1][7]. CfaE is the target of experimental vaccines and monoclonal antibody strategies designed to block ETEC colonization and prevent diarrheal disease[6]. There are no approved small-molecule drugs targeting CfaE; currently, the main therapeutic approach is vaccine-mediated immune blockade of its adhesion function[6].
Inhibition of bacterial adhesion to host cells (by antibodies or vaccines targeting CfaE)
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