Interaction of a group A Streptococcus within human plasma results in assembly of a surface plasminogen activator that contributes to occupancy of surface plasmin-binding structures

Microb Pathog. 1998 Jun;24(6):341-9. doi: 10.1006/mpat.1998.0207.

Abstract

Group A streptococcal isolate 187061 incubated in human plasma or serum reconstituted with fibrinogen but not plasminogen-depleted plasma or serum alone acquired a surface plasminogen activator activity. Assembly of the surface plasminogen activator was inhibited by the presence of neutralizing antibodies to streptokinase. Once assembled, the bacterial-associated plasminogen activator could generate plasmin when incubated in human plasminogen, plasmin or serum which could bind to bacterial surface plasmin-binding structures despite the presence of host physiological inhibitors. These studies provide evidence that the pathways by which group A isolates interact with human plasmin(ogen) are potentially linked and may provide a mechanism for bacteria to acquire host enzymatic activity efficiently in the infected host.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Aminocaproic Acid / analysis
  • Aminocaproic Acid / metabolism
  • Antibodies, Bacterial / administration & dosage
  • Bacterial Proteins / metabolism*
  • Fibrinogen / chemistry
  • Fibrinolysin / metabolism*
  • Humans
  • Plasma
  • Plasminogen Activators / metabolism*
  • Streptococcus pyogenes / enzymology
  • Streptococcus pyogenes / metabolism*
  • Streptococcus pyogenes / pathogenicity
  • Streptokinase / metabolism
  • alpha-Macroglobulins / metabolism

Substances

  • Antibodies, Bacterial
  • Bacterial Proteins
  • alpha-Macroglobulins
  • plasmin-alpha(2)-macroglobulin complex
  • Fibrinogen
  • Streptokinase
  • Plasminogen Activators
  • Fibrinolysin
  • Aminocaproic Acid