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Analysis of the Epithelial Damage Produced by Entamoeba histolytica Infection
Published on: June 12, 2014
Entamoeba histolytica: biochemical characterization of a protein disulfide isomerase
Marco A Ramos1, Rosa E Mares, Paloma D Magaña
1Facultad de Ciencias Químicas e Ingeniería, Universidad Autónoma de Baja California, Calzada Tecnológico, Tijuana, Baja California, Mexico. mramos@uabc.edu.mx
Abstract:
Protein disulfide isomerase (PDI) enzymes are eukaryotic oxidoreductases that catalyze oxidation, reduction and isomerization of disulfide bonds in polypeptide substrates. Here, we report the biochemical characterization of a PDI enzyme from the protozoan parasite Entamoeba histolytica (EhPDI). Our results show that EhPDI behaves mainly as an oxidase/isomerase and can be inhibited by bacitracin, a known PDI inhibitor; moreover, it exhibits chaperone-like activity. Albeit its physiological role in the life style of the parasite (including virulence and survival) remains to be studied, EhPDI could represent a potential drug target for anti-amebic therapy.
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