Vitronectin binding by Helicobacter pylori.
Vitronectin, a serum and extracellular matrix protein involved in immunological reactions, interacts with Helicobacter pylori strains. Of the 20 H. pylori strains tested three strains bound more than 50% of the vitronectin added, five strains bound 25-40%, nine strains bound 10-20% and three strains bound 5-8% vitronectin. Two strains, one with high- and one with low-binding properties, were selected for further characterization of 125I-vitronectin binding. Binding to the urea-activated 125I-labelled vitronectin was fast, saturable and reversible when an excess of unlabelled vitronectin was added to the bacteria with bound 125I-vitronectin. The binding was heat- and protease-sensitive, suggesting that the binding was mediated by bacterial cell-surface proteins. Since components such as fetuin and orosomucoid but not asialofetuin inhibited the binding, sialic-acid specific proteins, related to H. pylori sialic-acid specific haemagglutinins, were probably involved.
Ringnér
M
M
Department of Medical Microbiology, University of Lund, Sweden.
Paulsson
M
M
Wadström
T
T
D001798:Blood Proteins / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism*; D016480:Helicobacter pylori / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D011869:Radioligand Assay; D014508:Urea / Q000378:metabolism; D019096:Vitronectin
D001798:Blood Proteins; D016326:Extracellular Matrix Proteins; D006023:Glycoproteins; D019096:Vitronectin; D014508:Urea