Binding of immobilized Fibronectin by Biliary Drain Isolates

Abstract

Occlusion of biliary stents, as the result of bacterial adhesion and colonization onto biliary stents, still remains a major problem. Biliary proteins, such as fibronectin (Fn) and vitronectin (Vn), have been presumed to be involved in the process of bacterial adhesion to biliary biomaterial. In the present study, Fn binding by 5 strains of E. coli isolated from biliary drains or from bile was studied. All strains did not bind detectable amounts of soluble Fn but bound to immobilized plasma Fn. Adhesion of four strains of E. coli to ovalbumin was reduced by periodate treatment of ovalbumin, but adhesion to Fn was unaffected. Adhesion was inhibited by mannose-containing saccharides, trypsin treatment of the protein, and protease treatment of the bacterial cells. Autoradiography showed that components of cell extracts from three E. coli strains bind 125I-Fn but not a 150 kD Fn fragment. The findings indicate that the adhesion of these bacteria to Fn is a protein-protein interaction, inhibited by D-mannose, and possibly mediated by fimbrial components.