BINDING OF IMMOBILIZED FIBRONECTIN BY BILIARY DRAIN ISOLATES

Occlusion of biliary stents, as the result of bacterial adhesion and c olonization onto biliary stents, still remains a major problem. Biliar y proteins, such as fibronectin (Fn) and vitronectin (Vn), have been p resumed 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 di d not bind detectable amounts of soluble Fn but bound to immobilized p lasma Fn. Adhesion of four strains of E. coli to ovalbumin was reduced by periodate treatment of ovalbumin, but adhesion to Fn was unaffecte d. Adhesion was inhibited by mannose-containing saccharides, trypsin t reatment of the protein, and protease treatment of the bacterial cells . Autoradiography showed that components of cell extracts from three E . coli strains bind I-125-Fn but not a 150kD Fn fragment. The findings indicate that the adhesion of these bacteria to Fn is a protein-prote in interaction, inhibited by D-mannose, and possibly mediated by fimbr ial components.