6533b7dafe1ef96bd126f5e7
RESEARCH PRODUCT
Molecular cloning and characterization ofEchinostoma caproniheat shock protein-70 and differential expression in the parasite derived from low- and high-compatible hosts
José-guillermo EstebanCarlos MonteagudoAntonio MarcillaRafael ToledoM. HigónBernard Friedsubject
MaleMolecular Sequence DataBiologyMolecular cloningmedicine.disease_causeHost-Parasite Interactionslaw.inventionFeceslawCricetinaeEchinostomaHeat shock proteinmedicineAnimalsParasite hostingHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularRats WistarParasite Egg CountEscherichia coliMessenger RNAMesocricetusImmunohistochemistryMolecular biologyRatsOpen reading frameInfectious DiseasesGene Expression RegulationPolyclonal antibodiesRecombinant DNAbiology.proteinAnimal Science and ZoologyParasitologydescription
SUMMARYWe cloned and expressedEchinostoma caproniHSP70 inEscherichia coli. This molecule presents an open reading frame (ORF) of 655 amino acids, and a theoretical molecular weight of 71 kDa.E. caproniHSP70 protein showed a high homology to other helminth molecules, major differences being located in the C-terminal region of the molecule, with a hydrophobic portion. Studies of protein and messenger RNA (mRNA) expression revealed a distinct pattern, depending on the host (low- or high-compatible). Specific polyclonal antisera raised against the recombinant protein expressed inEscherichia colidemonstrated its selective presence in excretory/secretory products (ESP) of adult parasites obtained from high-compatible hosts. Immunological studies showed clearly the association of HSP70 with the parasite surface and other structures, including eggs.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2008-08-30 | Parasitology |