Entamoeba histolytica: Biochemical characterization of a protein disulfide isomerase

• Published in: Experimental parasitology Vol. 128; no. 1; pp. 76 - 81
• Main Authors: Ramos, Marco A., Mares, Rosa E., Magaña, Paloma D., Rivas, Israel D., Meléndez-López, Samuel G.
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier Inc 01.05.2011; Elsevier
• Subjects: Anti-Bacterial Agents - pharmacology; bacitracin; Bacitracin - pharmacology; Biochemical characterization; Biological and medical sciences; disulfide bonds; drugs; Entamoeba histolytica; Entamoeba histolytica - drug effects; Entamoeba histolytica - enzymology; Fundamental and applied biological sciences. Psychology; Hydrogen-Ion Concentration; Inhibitory Concentration 50; Insulin - metabolism; isomerization; Life cycle. Host-agent relationship. Pathogenesis; Molecular Chaperones - metabolism; Muramidase - chemistry; Muramidase - metabolism; oxidation; Oxidoreductase; oxidoreductases; Oxidoreductases - metabolism; parasites; parasitology; polypeptides; Protein disulfide isomerase; Protein Disulfide-Isomerases - antagonists & inhibitors; Protein Disulfide-Isomerases - chemistry; Protein Disulfide-Isomerases - metabolism; Protein Folding; Protozoa; Ribonuclease, Pancreatic - chemistry; Ribonuclease, Pancreatic - metabolism; therapeutics; virulence; Protein disulfide isomerase; Biochemical characterization; Eh; PDI; Oxidoreductase; Entamoeba histolytica; ER; LZM; Protozoa; Lobosea; Isomerases; Enzyme; Parasite; Oxidoreductases; Protein
• ISSN: 0014-4894; 1090-2449
• DOI: 10.1016/j.exppara.2011.02.009

[Display omitted] ► EhPDI behaves mainly as disulfide oxidase and isomerase. ► Bacitracin inhibits the oxidoreductase activities of EhPDI. ► The oxidoreductase activities of EhPDI are restricted by pH. ► EhPDI exhibits chaperone-like activity. 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.