Identification of enolase as a plasminogen-binding protein in excretory-secretory products of Fasciola hepatica

FEBS Lett. 2004 Apr 9;563(1-3):203-6. doi: 10.1016/S0014-5793(04)00306-0.

Abstract

We have followed a combined proteomic approach to identify proteins of Fasciola hepatica that could be involved in host-parasite interactions. Using two-dimensional gel electrophoresis, far Western immunoblot and mass spectrometry analyses, we have identified the enolase enzyme, present in the excretory/secretory materials of F. hepatica, as a human plasminogen-binding protein. This enzyme has an apparent molecular weight of 47 kDa with pI ranging from 6.2 to 7.2. These results suggest that enolase could act as a plasminogen receptor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Animals
  • Antigens, Helminth / analysis
  • Blotting, Western
  • Carrier Proteins / metabolism*
  • Conserved Sequence
  • Electrophoresis, Gel, Two-Dimensional
  • Fasciola hepatica / enzymology*
  • Helminth Proteins / analysis*
  • Helminth Proteins / chemistry*
  • Host-Parasite Interactions
  • Hydrogen-Ion Concentration
  • Isoelectric Point
  • Liver / parasitology
  • Mass Spectrometry
  • Molecular Sequence Data
  • Molecular Weight
  • Phosphopyruvate Hydratase / chemistry
  • Phosphopyruvate Hydratase / metabolism*
  • Plasminogen / metabolism
  • Proteomics
  • Sheep / parasitology

Substances

  • Antigens, Helminth
  • Carrier Proteins
  • Helminth Proteins
  • Plasminogen
  • Phosphopyruvate Hydratase

Associated data

  • GENBANK/A53665