Kinetics, subcellular localization, and contribution to parasite virulence of a
| Autor: | Martín, Hugo, Alejandra, Martínez, Madia, Trujillo, Damián, Estrada, Mauricio, Mastrogiovanni, Edlaine, Linares, Ohara, Augusto, Federico, Issoglio, Ari, Zeida, Darío A, Estrín, Harry F G, Heijnen, Lucía, Piacenza, Rafael, Radi |
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| Rok vydání: | 2017 |
| Předmět: |
Male
Mice Inbred BALB C Virulence Phenylalanine Trypanosoma cruzi Electron Spin Resonance Spectroscopy Tryptophan Cytochrome c Group Heme Hydrogen Peroxide Electron Transport Mice Inbred C57BL Kinetics Mice PNAS Plus parasitic diseases Mutagenesis Site-Directed Animals Chagas Disease Female Parasites Oxidation-Reduction Peroxidase |
| Zdroj: | Proceedings of the National Academy of Sciences of the United States of America. 114(8) |
| ISSN: | 1091-6490 |
| Popis: | 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 (TcAPx)-cytochrome c peroxidase (CcP)]. A unique subcellular distribution of TcAPx-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 TcAPx-CcP in pathogen virulence as part of the parasite antioxidant armamentarium. |
| Databáze: | OpenAIRE |
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