0000000000365555

AUTHOR

M. Higón

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Molecular cloning and characterization ofEchinostoma caproniheat shock protein-70 and differential expression in the parasite derived from low- and h…

2008

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…

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 ZoologyParasitologyParasitology
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