BIOCHEMICAL CHARACTERIZATION OF THIOREDOXIN REDUCTASE FROM BABESIA BOVIS

ERIKA REGNER; CAROLINA THOMPSON; ALBERTO A. IGLESIAS; SERGIO A. GUERRERO; DIEGO G. ARIAS

BIOCHIMIE

ELSEVIER FRANCE-EDITIONS SCIENTIFIQUES MEDICALES ELSEVIER

Lugar: Paris; Año: 2014 vol. 99 p. 44 - 53

0300-9084

This paper addresses the identification, cloning, expression, purification and functionalcharacterization of thioredoxin reductase from Babesia bovis, the etiological agent of babesiosis. Thework deals with in vitro steady state kinetic studies and other complementary analyses of thethioredoxin reductase found in the pathogenic protist. Thioredoxin reductase from B. bovis wascharacterized as a homodimeric flavoprotein that catalyzes the NADPH-dependent reduction of Trxwith a high catalytic efficiency. Moreover, the enzyme exhibited a disulfide reductase activity usingDTNB as substrate, being this activity highly sensitive to inhibition by Eosin B. The thioredoxinreductase/thioredoxin system can reduce oxidized glutathione and S nitrosoglutathione. Our in vitrodata suggest that antioxidant defense in B. bovis could be supported by this enzyme. We haveperformed an enzymatic characterization, searching for targets for rational design of inhibitors. Thiswork contributes to the better understanding of the redox biochemistry occurring in the parasite.