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Cell surface antigens of Mycoplasma species bovine group 7 bind to and activate plasminogen

Kylie Bower1, Steven P Djordjevic, Nicholas M Andronicos

  • 1Department of Biological Sciences, University of Wollongong, Wollongong, New South Wales 2522, Australia.

Infection and Immunity
|July 23, 2003
PubMed

Insights

Mycoplasma bovis group 7 binds plasminogen to its surface via lysine. This bound plasminogen is activated to plasmin, aiding potential virulence mechanisms in cattle.

Area of Science:

  • Microbiology
  • Bovine Pathogen Research
  • Protease Regulation

Background:

  • Mycoplasma species are significant bovine pathogens.
  • Plasminogen/plasmin system plays a role in pathogen virulence and tissue remodeling.
  • Understanding host-pathogen interactions is crucial for controlling bovine diseases.

Purpose of the Study:

  • To investigate the interaction between Mycoplasma species bovine group 7 and plasminogen.
  • To determine the mechanism and functional consequences of plasminogen binding.
  • To identify potential host cell surface proteins involved in this interaction.

Main Methods:

  • Plasminogen binding assays using Mycoplasma bovis group 7.
  • Lysine-dependency of binding was assessed.
  • Plasminogen activation by urokinase was measured.
  • Cross-linking assays were employed to identify binding proteins.

Main Results:

  • Mycoplasma bovis group 7 demonstrated cell surface binding of plasminogen in a lysine-dependent manner.
  • Cell-bound plasminogen was efficiently activated to plasmin by exogenous urokinase.
  • Plasminogen binding capacity correlated with observed enzymatic activity.
  • Several cell surface proteins were identified as potential plasminogen binding partners.

Conclusions:

  • Mycoplasma bovis group 7 actively binds and activates plasminogen on its surface.
  • This interaction may contribute to the pathogenesis of bovine mycoplasmosis.
  • Identification of binding proteins offers targets for future therapeutic strategies.

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