Binding of vitronectin and plasminogen to Helicobacter pylori

• Published in: FEMS immunology and medical microbiology Vol. 9; no. 1; pp. 29 - 34
• Main Authors: RINGNER, M, VALKONEN, K. H, WADSTRÖM, T
• Format: Journal Article
• Language: English
• Published: Oxford Blackwell 01.06.1994
• Subjects: Bacteriology; Biological and medical sciences; Collagen - metabolism; Fibrinogen - metabolism; Fibronectins - metabolism; Fundamental and applied biological sciences. Psychology; Glycoproteins - metabolism; Helicobacter pylori - metabolism; Humans; Iodine Radioisotopes; Microbiology; Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains; Plasminogen - metabolism; Protein Binding; Radioligand Assay; Vitronectin; Proteins; Spirillales; Helicobacter pylori; Collagen; Cell adhesion molecule; Spirillaceae; Bacteria; Extracellular matrix; Host agent relation; Vitronectin; Glycoproteins; Fibronectin
• ISSN: 0928-8244; 1574-695X
• DOI: 10.1016/0928-8244(94)00012-3

We have studied how some extracellular matrix proteins, fibronectin, fibrinogen, collagen type I and type IV, plasminogen and vitronectin bind to Helicobacter pylori. Radiolabelled vitronectin and plasminogen bound to the haemagglutinating H. pylori strain 17874 at a high level (53% and 32%, respectively), type IV collagen showed an intermediate level of binding (16%), while binding by 125I-labelled fibrinogen, fibronectin and collagen type I remained at a low level (5-7%). Both 125I-vitronectin and plasminogen showed a dose-dependent binding to cells of H. pylori 17874. Plasminogen binding by this strain was specific since the binding was inhibited by nonlabelled plasminogen, but not by highly glycosylated glycoproteins such as fetuin and orosomucoid or by a variety of monosaccharides. We have previously shown that 125I-vitronectin shows a specific and saturable binding to H. pylori 17874, and that sialic acid-rich glycoproteins such as fetuin and orosomucoid drastically reduced binding. We now report that a simultaneous incubation of 125I-vitronectin and 125I-plasminogen with cells of H. pylori 17874 showed a total binding approximately similar to the level of binding when either 125I-plasminogen, or 125I-vitronectin only were incubated with the bacterial cells. Nonlabelled vitronectin inhibited the binding of 125I-plasminogen by H. pylori, but nonlabelled plasminogen had no effect on the binding of 125I-vitronectin. Our findings suggest that there are different but probably closely localized binding sites for vitronectin and plasminogen on H. pylori 17874.