Open AccessVitronectin binding by Helicobacter pylori
Author(s) -
Ringnér Martina,
Paulsson Marianne,
Wadström Torkel
Publication year - 1992
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1992.tb05904.x
Subject(s) - vitronectin , fetuin , biochemistry , sialic acid , chemistry , binding protein , binding site , microbiology and biotechnology , biology , glycoprotein , extracellular matrix , fibronectin , gene
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 125 I‐vitronectin binding. Binding to the urea‐activated 125 I‐labelled vitronectin was fast, saturable and reversible when an excess of unlabelled vitronectin was added to the bacteria with bound 125 I‐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.