Vitronectin binding byHelicobacter pylori
| Autor: | Martina Ringnér, Marianne Paulsson, Torkel Wadström |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Extracellular Matrix Proteins
Helicobacter pylori biology Binding protein Proteolytic enzymes Orosomucoid Blood Proteins Hydrogen-Ion Concentration biology.organism_classification Microbiology Fetuin Radioligand Assay chemistry.chemical_compound Biochemistry chemistry Cell–cell interaction Genetics biology.protein Urea Vitronectin Molecular Biology N-Acetylneuraminic acid Bacteria Glycoproteins |
| Zdroj: | FEMS Microbiology Letters. 105:219-224 |
| ISSN: | 1574-6968 0378-1097 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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