6533b862fe1ef96bd12c6f16
RESEARCH PRODUCT
Identification of enolase as a plasminogen-binding protein in excretory-secretory products ofFasciola hepatica
Dolores BernalAna M Carrasco-abadJosé Enrique De La RubiaSantiago Mas-comaRafael ToledoAntonio Marcillasubject
ProteomicsAmino Acid MotifsBlotting WesternMolecular Sequence DataEnolaseEnolaseBiophysicsProteomicsBiochemistryMass SpectrometryHost-Parasite InteractionsStructural BiologyHepaticaparasitic diseasesGeneticsAnimalsFasciola hepaticaElectrophoresis Gel Two-DimensionalAmino Acid SequenceIsoelectric PointPlasminogen bindingMolecular BiologyConserved Sequencechemistry.chemical_classificationGel electrophoresisSheepbiologyExcretory–secretoryPlasminogenHelminth ProteinsCell BiologyFasciola hepaticaHydrogen-Ion Concentrationbiology.organism_classificationMolecular biologyMolecular WeightBlotEnzymeLiverchemistryBiochemistryExcretory systemAntigens HelminthPhosphopyruvate HydrataseCarrier Proteinsdescription
AbstractWe 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2004-01-29 | FEBS Letters |