Trypanosoma cruzi tryparedoxin II interacts with different peroxiredoxins under physiological and oxidative stress conditions

Author(s)

Dias, L. ^[1] ; Peloso, E. F. ^[1] ; Leme, A. F. P. ^[2] ; Carnielli, C. M. ^[2] ; Pereira, C. N. ^[1] ; Werneck, C. C. ^[1] ; Guerrero, S. ^[3] ; Gadelha, F. R. ^[1]

Affiliation

^[1] Univ Estadual Campinas, Dept Bioquim & Biol Tecidual, Campinas, SP - Brazil

^[2] Assoc Brasileira Tecnol Luz Sincrotron, Campinas, SP - Brazil

^[3] Univ Nacl Litoral, CONICET, Fac Bioquim & Ciencias Biol, Inst Agrobiotecnol Litoral, Santa Fe - Argentina

• Document type: Journal article
• Source: Experimental Parasitology; v. 184, p. 1-10, JAN 2018.
• Web of Science Citations: 1

Abstract

Trypanosoma cruzi, the etiologic agent of Chagas disease, has to cope with reactive oxygen and nitrogen species during its life cycle in order to ensure its survival and infection. The parasite detoxifies these species through a series of pathways centered on trypanothione that depend on glutathione or low molecular mass dithiol proteins such as tryparedoxins. These proteins transfer reducing equivalents to peroxidases, including mitochondrial and cytosolic peroxiredoxins, TcMPx and TcCPx, respectively. In T. cruzi two tryparedoxins have been identified, TXNI and TXNII with different intracellular locations. TXNI is a cytosolic protein while TXNII due to a C-terminal hydrophobic tail is anchored in the outer membrane of the mitochondrion, endoplasmic reticulum and glycosomes. TXNs have been suggested to be involved in a majority of biological processes ranging from redox mechanisms to protein translation. Herein, a comparison of the TXNII interactomes under physiological and oxidative stress conditions was examined. Under physiological conditions, apart from the proteins with unknown biological process annotation, the majority of the identified proteins are related to cell redox homeostasis and biosynthetic processes, while under oxidative stress conditions, are involved in stress response, cell redox homeostasis, arginine biosynthesis and microtubule based process. Interestingly, although TXNII interacts with both peroxiredoxins under physiological conditions, upon oxidative stress, TcMPx interaction prevails. The relevance of the interactions is discussed opening a new perspective of TXNII functions. (C) 2017 Elsevier Inc. All rights reserved. (AU)

• FAPESP's process: 11/20084-9 - Funcional caracterization and intracellular location of Trypanosoma cruzi mitochondrial and nuclear components of the antioxidant system dependent or not on trypanothione
• Grantee: Fernanda Ramos Gadelha
• Support Opportunities: Regular Research Grants
• FAPESP's process: 11/19872-2 - Determination of the interatome, funcional caracterization and other Trypanosoma cruzi mitochondrial tryparedoxin peroxidase intracellular localizations
• Grantee: Eduardo de Figueiredo Peloso
• Support Opportunities: Scholarships in Brazil - Post-Doctoral