Enterotoxigenic Escherichia coli F18 fimbrial adhesin (FedF) (FedF)

Enterotoxigenic Escherichia coli F18 fimbrial adhesin (FedF) is a critical virulence protein found on the surface of specific E. coli strains that infect swine. It serves as the tip-adhesin of F18 fimbriae, functioning as a lectin that mediates the attachment of the bacteria to carbohydrate receptors on the porcine intestinal epithelium [4, 9]. This adherence is a prerequisite for the colonization of the small intestine and the subsequent release of enterotoxins or Shiga toxins, which lead to post-weaning diarrhea and edema disease [8, 10, 12]. The presence of the host receptor for FedF is genetically controlled by the alpha-(1,2)-fucosyltransferase 1 (FUT1) gene, making certain pig populations naturally resistant to infection [1, 5]. Because of its essential role in pathogenesis, FedF is a primary target for the development of veterinary vaccines, neutralizing antibodies, and anti-adhesion therapies aimed at preventing ETEC-related morbidity and mortality in the swine industry [6, 10]. These interventions focus on blocking the initial attachment phase to prevent the cascade of secretory diarrhea and systemic complications [8, 11].

Other names

F18 fimbriaeF18 adhesinFedF proteinF107 fimbriae2134P fimbriae8813 fimbriae

Inhibition of bacterial attachment to intestinal enterocytes and neutralization of fimbrial-mediated colonization.