Schistosoma bovis: plasminogen binding in adults and the identification of plasminogen-binding proteins from the worm tegument

Exp Parasitol. 2007 Jan;115(1):83-91. doi: 10.1016/j.exppara.2006.07.003. Epub 2006 Sep 8.

Abstract

Schistosoma bovis is a ruminant haematic parasite that lives for years in the mesenteric vessels of the host. The aim of this work was to investigate the ability of adult S. bovis worms to interact with plasminogen, a central component in the host fibrinolytic system. Confocal microscopy analysis revealed that plasminogen bound to the tegument surface of the male-but not female-S. bovis worms and that this binding was strongly dependent on lysine residues. It was also observed that a protein extract of the worm tegument (TG) had the capacity to generate plasmin and to enhance the plasmin generation by the tissue-type plasminogen activator. Proteomic analysis of the TG extract identified 10 plasminogen-binding proteins, among which the major ones were enolase, glyceraldehyde-3-phosphate dehydrogenase and actin. This study represents the first report about the binding of plasminogen to Schistosoma sp. proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / analysis
  • Actins / metabolism
  • Actins / physiology
  • Animals
  • Carrier Proteins / analysis
  • Carrier Proteins / metabolism*
  • Carrier Proteins / physiology
  • Electrophoresis, Gel, Two-Dimensional
  • Electrophoresis, Polyacrylamide Gel
  • Enzyme-Linked Immunosorbent Assay
  • Female
  • Fibrinolysin / biosynthesis
  • Fluorescent Antibody Technique
  • Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) / analysis
  • Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) / metabolism
  • Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+) / physiology
  • Helminth Proteins / analysis
  • Helminth Proteins / metabolism*
  • Helminth Proteins / physiology
  • Humans
  • Ligands
  • Male
  • Mass Spectrometry
  • Membrane Proteins / analysis
  • Membrane Proteins / metabolism*
  • Membrane Proteins / physiology
  • Microscopy, Confocal
  • Phosphopyruvate Hydratase / analysis
  • Phosphopyruvate Hydratase / metabolism
  • Phosphopyruvate Hydratase / physiology
  • Plasminogen / metabolism*
  • Schistosoma / metabolism*
  • Sheep
  • Snails

Substances

  • Actins
  • Carrier Proteins
  • Helminth Proteins
  • Ligands
  • Membrane Proteins
  • Plasminogen
  • Glyceraldehyde 3-Phosphate Dehydrogenase (NADP+)
  • Fibrinolysin
  • Phosphopyruvate Hydratase