Binding and activation of human plasminogen by Mycobacterium tuberculosis

Infect Immun. 2000 Jul;68(7):4327-30. doi: 10.1128/IAI.68.7.4327-4330.2000.

Abstract

The first evidence of the interaction of Mycobacterium tuberculosis with the plasminogen system is herein reported. By FACScan analysis and affinity blotting, lysine-dependent binding of plasminogen to M. tuberculosis was demonstrated. The binding molecules were 30-, 60-, and 66-kDa proteins present in cell wall and soluble protein extracts. The activation of plasminogen, which occurred only in presence of fibrin and was not inhibited by the host serpin, alpha(2)-antiplasmin, was also demonstrated.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fibrin / metabolism
  • Humans
  • In Vitro Techniques
  • Mycobacterium tuberculosis / metabolism
  • Mycobacterium tuberculosis / pathogenicity*
  • Plasminogen / metabolism*
  • Protein Binding
  • Receptors, Cell Surface / metabolism
  • Receptors, Urokinase Plasminogen Activator
  • Tuberculosis / etiology
  • alpha-2-Antiplasmin / pharmacology

Substances

  • PLAUR protein, human
  • Receptors, Cell Surface
  • Receptors, Urokinase Plasminogen Activator
  • alpha-2-Antiplasmin
  • Fibrin
  • Plasminogen