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Colonization factor antigen I fimbrial adhesin (abbreviated as CFA/I adhesin, also known as CfaE) is the minor, tip-localized adhesive subunit of the class 5 fimbrial structure known as CFA/I, found in enterotoxigenic Escherichia coli (ETEC)[2][1][3][6]. CFA/I adhesin is essential for the attachment of ETEC to intestinal epithelial cells, mediating the initial host-pathogen interaction required for colonization and initiation of diarrheal disease[2][3][8]. Structurally, CfaE consists of an N-terminal adhesin domain responsible for receptor (host glycosphingolipid) binding and a C-terminal pilin domain that interfaces with other fimbrial subunits[2][4][3][7]. The adhesin functions as the receptor-binding tip of a long, helical pilus filament formed mainly by the major subunit CfaB; only one or a few CfaE subunits are present per pilus[3][8]. CfaE binds to specific glycosphingolipids on host intestinal cells, and its function is critical for ETEC pathogenicity[5]. As such, CFA/I fimbrial adhesin has become a focus of vaccine and therapeutic development efforts aimed at preventing ETEC-mediated diarrheal infections[6].
Blockade of host cell binding/attachment, Antibody-mediated neutralization, Inhibition of fimbrial assembly
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