INTERACTION OF HELICOBACTER-PYLORI WITH EXTRACELLULAR-MATRIX PROTEINS

Binding of 11 isolates of the gastroduodenal pathogen Helicobacter pyl ori from three geographical regions to extracellular matrix proteins w as investigated. None of the strains bound soluble proteins, but a pro portion (27%) bound immobilized laminin, fibronectin, and types I and V collagens. Microaerobic conditions were required to demonstrate repr oducible binding. Contrary to previous reports, interstrain variation in the pattern of binding to various proteins was observed, possibly r eflecting pathogenic or virulence differences between strains. Binding was strongest to laminin. Purified lipopolysaccharide completely inhi bited the binding of H. pylori to laminin indicating that this bacteri al surface molecule is involved in the adhesion process.