Work

Kinetics, subcellular localization, and contribution to parasite virulence of a Trypanosoma cruzi hybrid type A heme peroxidase ( Tc APx-CcP)

Year: 2017

Type: article

Abstract: Significance Trypanosoma cruzi , the causative agent of Chagas disease, affects 8–10 million people in Latin America. Parasite antioxidant systems are essential for parasite survival and infectivity in the vertebrate host. Herein, we characterized the enzymic properties, subcellular localization, and contribution to parasite virulence of a T. cruzi hybrid type A member of class I heme peroxidases. The enzyme reacts fast with hydrogen peroxide and utilizes both ferrocytochrome c and ascorbate as reducing substrates [ T. cruzi ascorbate peroxidase ( Tc APx)-cytochrome c peroxidase (CcP)]. A unique subcellular distribution of Tc APx-CcP in the infective stages suggests a role during parasite–host interactions. Infection of macrophages and cardiomyocytes, as well as in mice, confirmed the involvement of Tc APx-CcP in pathogen virulence as part of the parasite antioxidant armamentarium.

Source: Proceedings of the National Academy of Sciences

DOI: 10.1073/pnas.1618611114