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Helicobacter pylori interactions with plasminogen.

A Ljungh1

  • 1Department of Infectious Diseases and Medical Microbiology, Lund University, Sölvegatan 23, Lund, S-223 62, Sweden. asa.ljungh@mmb.lu.se

Methods (San Diego, Calif.)
|May 19, 2000
PubMed
Summary

Helicobacter pylori binds plasminogen via surface proteins, converting it to plasmin. This proteolytic activity may aid H. pylori

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Pathogenesis

Background:

  • Helicobacter pylori causes gastritis, ulcers, and gastric cancer.
  • Virulence factors include adhesins, cytotoxins, and extracellular matrix binding.
  • H. pylori binds soluble plasminogen, a key virulence mechanism.

Purpose of the Study:

  • To investigate the mechanism and significance of H. pylori plasminogen binding.
  • To identify the bacterial proteins involved in plasminogen interaction.
  • To understand the role of plasminogen conversion in H. pylori pathogenesis.

Main Methods:

  • Plasminogen binding assays at varying pH.
  • Identification of bacterial binding proteins using SDS-PAGE.
  • Scatchard plot analysis for binding kinetics.
  • Inhibition studies with lysine and E-aminocaproic acid.
  • Assessing plasminogen activator activity in infected patients.

Main Results:

  • Plasminogen binding optimal at pH 7.0, mediated by 42 and 57 kDa proteins.
  • Binding affinity (K(d)) of 7 x 10(-7) M.
  • Lysine and E-aminocaproic acid inhibited binding.
  • The fifth kringle of plasminogen is the binding site.
  • H. pylori infection alters plasminogen activator balance, favoring urokinase.

Conclusions:

  • H. pylori utilizes surface proteins to bind plasminogen.
  • Plasminogen binding and conversion to plasmin represent a unique proteolytic activity.
  • This mechanism may facilitate bacterial tissue invasion and contribute to gastric carcinogenesis.

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