Dithiol Glutaredoxin from Trypanosoma cruzi: Cloning, Expresión and Characterization

MARQUEZ VE; ARIAS DG; PIATTONI CV; IGLESIAS AA; GUERRERO SA

San Miguel de Tucumán, Argentina

Congreso; 45th Annual Meeting, Argentine Society for Biochemistry and Molecular Biology Research. XLV Reunión Annual, Sociedad Argentina de Investigación en Bioquímica y Biología Molecular.; 2009

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular.

EN-P02.DITHIOL GLUTAREDOXIN FROM Trypanosoma cruzi:CLONING, EXPRESSION AND CHARACTERIZATIONMárquez VE; Arias DG; Piattoni CV; Iglesias AA; Guerrero SALaboratorio de Bioquímica microbiana. IAL (UNL-CONICET)FBCB. Santa Fe. E-mail: vmarquez@fbcb.unl.edu.arTrypanosoma cruzi is the causative agent of Chagas’ disease.Similar to that found for other aerobic parasites, T. cruzi is exposedto several reactive oxygen species, which are highly toxic for theparasite. These chemical species are generated both during the hostdefense reaction and also as byproducts of the aerobic metabolism.The metabolic pathways used by this organism to cope with suchenvironmental changes and redox homeostasis are matter of ourwork. Glutaredoxins are ubiquitous oxidoreductases that play animportant role in the control of cellular function. Despite a putativedithiol glutaredoxin (TcGrx) is encoded in the genome of T. cruzi, itwas not yet characterized. In this work we present the cloning,expression and functional characterization of recombinant TcGrx.The protein was able to catalyze the reduction of oxidizedglutathione and glutathionylated compounds using trypanothioneas electron donor, demonstrating the functional relevance of thisenzyme for the parasite. We present experimental assays (westernblotting and enzymatic activity) that strongly support theoccurrence of a dithiol glutaredoxin in T. cruzi epimastigote, beingnecessary to consider this protein as a new molecular component ofthe redox metabolism in trypanosomatids.