Peroxiredoxins from Trypanosoma cruzi: Virulence factors and drug targets for treatment of Chagas disease?

Gene

Volumn 408, Issue 1-2, 2008, Pages 45-50

  Piñeyro, María Dolores ^a,b   Parodi Talice, Adriana ^b,c   Arcari, Talia ^a,b   Robello, Carlos ^a,b  

^a DEPARTAMENTO DE BIOQUÍMICA   (Uruguay)

^b INSTITUT PASTEUR DE MONTEVIDEO   (Uruguay)

^c UNIVERSIDAD DE LA REPÚBLICA   (Uruguay)

Author keywords

Chagas disease; Peroxiredoxins; Virulence factors

Indexed keywords

OXIDOREDUCTASE; PEROXIDASE; PEROXIREDOXIN; PEROXYNITRITE REDUCTASE; TRYPAREDOXIN PEROXIDASE; UNCLASSIFIED DRUG; VIRULENCE FACTOR;

ANIMAL CELL; ANTIOXIDANT ACTIVITY; ARTICLE; CELL DIFFERENTIATION; CHAGAS DISEASE; DETOXIFICATION; DRUG DESIGN; ENZYME ACTIVITY; LIFE CYCLE; MITOCHONDRION; MOUSE; NONHUMAN; PARASITE DEVELOPMENT; PARASITE SURVIVAL; PARASITE VIRULENCE; PHAGOCYTE; PRIORITY JOURNAL; PROTEIN EXPRESSION; TRYPANOSOMA CRUZI;

TRYPANOSOMA CRUZI; TRYPANOSOMATIDAE;

EID: 37549058462     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.gene.2007.10.014     Document Type: Article

References (35)

1. Akerman S.E., and Muller S. Peroxiredoxin-linked detoxification of hydroperoxides in Toxoplasma gondii. J. Biol. Chem. 280 (2005) 564-570
2. Andrade L.O., and Andrews N.W. The Trypanosoma cruzi-host-cell interplay: location, invasion, retention. Nat. Rev. Microbiol. 3 (2005) 819-823
3. Boveris A., Sies H., Martino E.E., Docampo R., Turrens J.F., and Stoppani A.O. Deficient metabolic utilization of hydrogen peroxide in Trypanosoma cruzi. Biochem. J. 188 (1980) 643-648
4. Budde H., Flohe L., Hecht H.J., Hofmann B., Stehr M., Wissing J., and Lunsdorf H. Kinetics and redox-sensitive oligomerisation reveal negative subunit cooperativity in tryparedoxin peroxidase of Trypanosoma brucei brucei. Biol. Chem. 384 (2003) 619-633
5. Burleigh B.A., and Andrews N.W. The mechanisms of Trypanosoma cruzi invasion of mammalian cells. Annu. Rev. Microbiol. 49 (1995) 175-200
6. Castro G.D., Lopez A., and Castro J.A. Evidence for hydroxyl free radical formation during paraquat but not for nifurtimox liver microsomal biotransformation. A dimethyl-sulfoxide scavenging study. Arch. Toxicol. 62 (1988) 355-358
7. Chae H.Z., Kim H.J., Kang S.W., and Rhee S.G. Characterization of three isoforms of mammalian peroxiredoxin that reduce peroxides in the presence of thioredoxin. Diabetes Res. Clin. Pract. 45 (1999) 101-112
8. Contreras V.T., Salles J.M., Thomas N., Morel C.M., and Goldenberg S. In vitro differentiation of Trypanosoma cruzi under chemically defined conditions. Mol. Biochem. Parasitol. 16 (1985) 315-327
9. Contreras V.T., Araujo-Jorge T.C., Bonaldo M.C., Thomaz N., Barbosa H., Meirelles M., and Goldenberg S. Biological aspects of the Dm28c clone of Trypanosoma cruzi after metacyclogenesis in chemically defined media. Mem. Inst. Oswaldo Cruz 83 (1988) 123-133
10. Fairlamb A.H., and Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu. Rev. Microbiol. 46 (1992) 695-729
11. Finzi J.K., Chiavegatto C.W., Corat K.F., Lopez J.A., Cabrera O.G., Mielniczki-Pereira A.A., Colli W., Alves M.J., and Gadelha F.R. Trypanosoma cruzi response to the oxidative stress generated by hydrogen peroxide. Mol. Biochem. Parasitol. 133 (2004) 37-43
12. Flohé L., Hecht H.J., and Steinert P. Glutathione and trypanothione in parasitic hydroperoxide metabolism. Free Radic. Biol. Med. 27 (1999) 966-984
13. Hofmann B., Hecht H.J., and Flohé L. Peroxiredoxins. Biol. Chem. 383 (2002) 347-364
14. Kelly J.M., Taylor M.C., Smith K., Hunter K.J., and Fairlamb A.H. Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which over-express trypanothione reductase. Sensitivity towards agents that are thought to induce oxidative stress. Eur. J. Biochem. 218 (1993) 29-37
15. Krauth-Siegel R.L., Meiering S.K., and Schmidt H. The parasite-specific trypanothione metabolism of Trypanosoma and Leishmania. Biol. Chem. 384 (2003) 539-549
16. Nogoceke E., Gommel D.U., Kiess M., Kalisz H.M., and Flohé L. A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol. Chem. 378 (1997) 827-836
17. Parodi-Talice A., Durán R., Arrambide N., Prieto V., Piñeyro M.D., Pritsch O., Cayota A., Cerveñansky C., and Robello C. Proteome analysis of the causative agent of Chagas disease: Trypanosoma cruzi. Int. J. Parasitol. 34 8 (2004) 881-886
18. Parsonage D., Youngblood D.S., Sarma G.N., Wood Z.A., Karplus P.A., and Poole L.B. Analysis of the link between enzymatic activity and oligomeric state in AhpC, a bacterial peroxiredoxin. Biochemistry 44 (2005) 10583-10592
19. Pineyro M.D., Pizarro J.C., Lema F., Pritsch O., Cayota A., Bentley G.A., and Robello C. Crystal structure of the tryparedoxin peroxidase from the human parasite Trypanosoma cruzi. J. Struct. Biol. 150 (2005) 11-22
20. Pinto Dias J.C., Deane M.P., and Brener Z. Trypanosoma cruzi e a doença de Chagas: A doença (1991), Luis Rey, Rio de Janeiro
21. Robello C., Navarro P., Castanys S., and Gamarro F. A pteridine reductase gene ptr1 contiguous to a P-glycoprotein confers resistance to antifolates in Trypanosoma cruzi. Mol. Biochem. Parasitol. 90 (1997) 525-535
22. Rohloff P., Rodrigues C.O., and Docampo R. Regulatory volume decrease in Trypanosoma cruzi involves amino acid efflux and changes in intracellular calcium. Mol. Biochem. Parasitol. 126 (2003) 219-230
23. Sambrook J., Maniatis T., and Fritsch E.F. Molecular Cloning: a Laboratory Manual (1989), Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
24. Sibley L.D., and Andrews N.W. Cell invasion by un-palatable parasites. Traffic (Copenhagen, Denmark) 1 (2000) 100-106
25. 2-generating system. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 2584-2588
26. Tardieux I., Webster P., Ravesloot J., Boron W., Lunn J.A., Heuser J.E., and Andrews N.W. Lysosome recruitment and fusion are early events required for trypanosome invasion of mammalian cells. Cell 71 (1992) 1117-1130
27. Trujillo M., Budde H., Pineyro M.D., Stehr M., Robello C., Flohé L., and Radi R. Trypanosoma brucei and Trypanosoma cruzi tryparedoxin peroxidases catalytically detoxify peroxynitrite via oxidation of fast reacting thiols. J. Biol. Chem. 279 33 (2004) 34175-34182
28. WHO. The World Health Report (2002), Geneva World Health Organization
29. Wilkinson S.R., Meyer D.J., and Kelly J.M. Biochemical characterization of a trypanosome enzyme with glutathione-dependent peroxidase activity. Biochem. J. 352 3 (2000) 755-761
30. Wilkinson S.R., Temperton N.J., Mondragon A., and Kelly J.M. Distinct mitochondrial and cytosolic enzymes mediate trypanothione-dependent peroxide metabolism in Trypanosoma cruzi. J. Biol. Chem. 275 (2000) 8220-8225
31. Wilkinson S.R., Meyer D.J., Taylor M.C., Bromley E.V., Miles M.A., and Kelly J.M. The Trypanosoma cruzi enzyme TcGPXI is a glycosomal peroxidase and can be linked to trypanothione reduction by glutathione or tryparedoxin. J. Biol. Chem. 277 (2002) 17062-17071
32. Wilkinson S.R., Taylor M.C., Touitha S., Mauricio I.L., Meyer D.J., and Kelly J.M. TcGPXII, a glutathione-dependent Trypanosoma cruzi peroxidase with substrate specificity restricted to fatty acid and phospholipid hydroperoxides, is localized to the endoplasmic reticulum. Biochem. J. 364 (2002) 787-794
33. Wilkinson S.R., Obado S.O., Mauricio I.L., and Kelly J.M. Trypanosoma cruzi expresses a plant-like ascorbate-dependent hemoperoxidase localized to the endoplasmic reticulum. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 13453-13458
34. Wilkinson S.R., Horn D., Prathalingam S.R., and Kelly J.M. RNA interference identifies two hydroperoxide metabolizing enzymes that are essential to the bloodstream form of the African trypanosome. J. Biol. Chem. 278 (2003) 31640-31646
35. Yoshida N. Molecular basis of mammalian cell invasion by Trypanosoma cruzi. An. Acad. Bras. Cienc. 78 (2006) 87-111