BINDING INTERACTIONS OF COLLAGEN-I, LAMININ AND FIBRONECTIN WITH IMMOBILIZED ESCHERICHIA-COLI O157-H7 USING A SURFACE-PLASMON RESONANCE BIOSENSOR

Real-time interactions of collagen I, fibronectin, laminin, hyaluronic acid and chondroitin sulfate with immobilized Escherichia coli O157:H 7 cells were studied with a surface plasmon resonance biosensor. Resul ts showed that collagen I and laminin bound to the E. coli surface but fibronectin had very low binding while hyaluronic acid and chondroiti n sulfate had no detectable interaction. Calcium ion inhibited laminin binding but enhanced collagen I binding. This research provides a mod el system to study the interactions of bacterial cells with extracellu lar matrix components.