The cellular form of human fibronectin as an adhesion target for the S fimbriae of meningitis-associated Escherichia coli

The adhesion of the S fimbriae of meningitis-associated Escherichia coli O1 8ac:K1:H7 to the cellular and the plasma forms of human fibronectin was stu died. E. coli HB101(pAZZ50) expressing the complete S-fimbria II gene clust er of E, coli O18 adhered to cellular fibronectin (cFn) on glass but not to plasma fibronectin (pFn). Adhesion to cFn was specifically inhibited by ne uraminidase treatment of cFn as well as by incubation of the bacteria with sialyl-alpha 2-3-lactose, a receptor analog of the S fimbriae. No significa nt adhesion to cFn or pFn was detected with E. coli HB101(pAZZ50-67) expres sing S fimbriae lacking the SfaS lectin subunit. Strain HB101(pAZZ50) also adhered to a human fibroblast cell culture known to be rich in cFn, and the adhesion was specifically inhibited in the presence of polyclonal antibodi es to cFn. The results show that the SfaS lectin of the S fimbriae mediates the adherence of meningitis-associated E. coli to sialyl oligosaccharide c hains of cFn.