Binding of human plasminogen and lactoferrin by coccoid forms Free

Abstract

The interactions between spiral and coccoid forms, extracellular matrix (ECM) and plasma proteins were studied in an I-labelled protein assay. The range of binding of collagen V, plasminogen, human lactoferrin (HLf) and vitronectin to coccoid forms of NCTC 11637 was 26–48%. In contrast, binding of radiolabelled fibronectin and collagen types I and III was low (3–8%). The coccoid forms of 14 strains of showed significant HLf binding (median 26%). With plasminogen, no significant difference was found between binding to the coccoid (median = 13%) and spiral (median = 12%) forms, of 13 of the 14 strains of tested; the exception was strain NCTC 11637. I-plasminogen showed a dose-dependent binding to both the coccoid and spiral forms. Plasminogen binding to both forms was specific; the binding was inhibited by non-labelled plasminogen, plasmin, lysine, EACA (epsilon-aminocaproic acid) but not by fetuin or various carbohydrates. Similarly, HLf binding was found to be specific and was inhibited by non-labelled HLf and BLf. The coccoid forms showed either similar or enhanced ECM binding capabilities compared with the spiral forms. As the binding of ECM proteins may be an important mechanism of tissue adhesion for various pathogenic bacteria, the coccoid differentiated form of can be considered as an infective form in the pathogenesis of helicobacter infection and type B gastritis.

Loading

Article metrics loading...

/content/journal/jmm/10.1099/00222615-45-6-433
1996-12-01
2024-03-28
Loading full text...

Full text loading...

/deliver/fulltext/jmm/45/6/medmicro-45-6-433.html?itemId=/content/journal/jmm/10.1099/00222615-45-6-433&mimeType=html&fmt=ahah

References

  1. Westerlund B., Korhonen T. K. Bacterial proteins binding to the mammalian extracellular matrix. Mol Microbiol 1993; 9:687–694
    [Google Scholar]
  2. Ljungh A., Wadstrӧm T. Binding of extracellular matrix proteins by microbes. Methods Enzymol 1995; 253:501–514
    [Google Scholar]
  3. Valkonen K. H., Ringner M., Ljungh A., Wadstrӧm T. High-affinity binding of laminin by Helicobacter pylori: evidence for a lectin-like interaction. FEMS Immunol Med Microbiol 1993; 7:29–37
    [Google Scholar]
  4. Ringner M., Paulsson M., Wadstrӧm T. Vitronectin binding by Helicobacter pylori . FEMS Microbiol Immunol 1992; 5:219–224
    [Google Scholar]
  5. Ringner M., Valkonen K. H., Wadstrӧm T. Binding of vitronectin and plasminogen to Helicobacter pylori . FEMS Immunol Med Microbiol 1994; 9:29–34
    [Google Scholar]
  6. Trust T. J., Doig P., Emӧdy L., Kienle Z., Wadstrӧm T., O’Toole P. High-affinity binding of the basement membrane proteins collagen type IV and laminin to the gastric pathogen Helicobacter pylori . Infect Immun 1991; 59:4398–4404
    [Google Scholar]
  7. Ullberg M., Karlsson I., Wiman B., Kronvall G. Two types of receptors for human plasminogen on group G streptococci. APMIS 1992; 100:21–28
    [Google Scholar]
  8. Ullberg M., Kuusela P., Kristiansen, B-E., Kronvall G. Binding of plasminogen to Neisseria meningitidis and Neisseria gonorrhoeae and formation of surface-associated plasmin. J Infect Dis 1992; 166:1329–1334
    [Google Scholar]
  9. Kuusela P., Ullberg M., Saksela O., Kronvall G. Tissue-type plasminogen activator-mediated activation of plasminogen on the surface of Group A, C, and G streptococci. Infect Immun 1992; 60:196–201
    [Google Scholar]
  10. Ponting C. P., Marshall J. M., Cederholm-Williams S. A. Plasmino-gen: a structural review. Blood Coagul Fibrinolysis 1992; 3:605–614
    [Google Scholar]
  11. Kuusela P., Saksela O. Binding and activation of plasminogen at the surface of Staphylococcus aureus. Increase in affinity after conversion to the Lys form of the ligand. Eur J Biochem 1990; 193:759–765
    [Google Scholar]
  12. Ullberg M., Kronvall G., Karlsson I., Wiman B. Receptors for human plasminogen on gram-negative bacteria. Infect Immun 1990; 58:21–25
    [Google Scholar]
  13. Griffiths E. The iron-uptake systems of pathogenic bacteria. In Bullen J. J., Griffiths E. (eds) Iron and infection: molecular, physiological and clinical aspects Chichester: John Wiley and Sons; 198769–137
    [Google Scholar]
  14. Bullen J. J., Rogers H. J., Leigh L. Iron-binding proteins in milk and resistance to Escherichia coli infections in infants. B M J 1972; 1:69–75
    [Google Scholar]
  15. Yamauchi K., Tomita M., Giehl T. J., Ellison R. T. Antibacterial activity of lactoferrin and a pepsin-derived lactoferrin peptide fragment. Infect Immun 1993; 61:719–728
    [Google Scholar]
  16. Husson M.-O., Legrand D., Spik G., Leclerc H. Iron acquisition by Helicobacter pylori: importance of human lactoferrin. Infect Immun 1993; 61:2694–2697
    [Google Scholar]
  17. Wadstrom T., Ascencio F., Ljungh A. Helicobacter pylori adhesins. Eur J Gastroenterol Hepatol 1993; 5: Suppl 2S12–S15
    [Google Scholar]
  18. Bode G., Mauch F., Malfertheiner P. The coccoid forms of Helicobacter pylori. Criteria for their viability. Epidemiol Infect 1993; 111:483–490
    [Google Scholar]
  19. Vijayakumari S. The two differentiated forms of Helicobacter pylori . PhD Thesis National University of Singapore; Singapore: 1995
    [Google Scholar]
  20. Mai U., Geis G., Leying H., Rühl G., Opferkuch W. Dimorphism of Campylobacter pylori . In Mégraud F., Lamouliatte H. (eds) Gastroduodenal pathology and Campylobacter pylori (Excerpta Medical International Congress Series no. 847) Amsterdam: Elsevier Science Publishers B. V (Biomedical Division); 198929–33
    [Google Scholar]
  21. Markwell M. A. K. A new solid state-reagent to iodinate proteins. 1. Conditions for the efficient labeling of antiserum. Anal Biochem 1982; 125:427–432
    [Google Scholar]
  22. Paulsson M., Wadstrom T. Vitronectin and type-I collagen binding by Staphylococcus aureus and coagulase-negative staphylococci. FEMS Microbiol Immunol 1990; 2:55–62
    [Google Scholar]
  23. Schryvers A. B., Lee B. C. Analysis of bacterial receptors for host iron-binding proteins. J Microbiol Methods 1993; 18:255–266
    [Google Scholar]
  24. Yu R.-H., Schryvers A. B. Regions located in both the N-lobe and C-lobe of human lactoferrin participate in the binding interaction with bacterial lactoferrin receptors. Microb Pathog 1993; 14:343–353
    [Google Scholar]
  25. Jones D. M., Curry A. The genesis of coccal forms of Helicobacter pylori . In Malfertheiner P., Ditschuneit H. (eds) Helicobacter pylori, gastritis and peptic ulcer Heidelberg: Springer-Verlag; 199029–37
    [Google Scholar]
  26. Catrenich C. E., Makin K. M. Characterization of the morphologic conversion of Helicobacter pylori from bacillary to coccoid forms. Scand J Gastroenterol 1991; 26: Suppl 18158–64
    [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/jmm/10.1099/00222615-45-6-433
Loading
/content/journal/jmm/10.1099/00222615-45-6-433
Loading

Data & Media loading...

Most cited Most Cited RSS feed