Future prospects for the chemotherapy of Chagas' disease

Medicina

Volumn 59, Issue SUPPL. 2, 1999, Pages 179-187

  Fairlamb, Alan H ^a  

^a UNIVERSITY OF DUNDEE   (United Kingdom)

Author keywords

Drug discovery; Leishmaniasis; Target validation; Trypanosomiasis; Trypanothione reductase

Indexed keywords

ALLOPURINOL; BENZNIDAZOLE; ERGOSTEROL; ETHER LIPID; FOLIC ACID; MESSENGER RNA; NIFURTIMOX; PROTEINASE; PTERIDINE; PURINE; TRYPANOTHIONE;

CHAGAS DISEASE; CONFERENCE PAPER; DRUG DESIGN; DRUG TARGETING; GENE SEQUENCE; KINETOPLAST; METABOLISM; PARASITE; VALIDATION PROCESS;

ANIMALS; CHAGAS DISEASE; DRUG DESIGN; FORECASTING; HUMANS; NADH, NADPH OXIDOREDUCTASES; TRYPANOSOMA CRUZI;

EID: 0032790777     PISSN: 00257680     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper

References (108)

1. de Castro SL. The challenge of Chagas' disease chemotherapy: an update of drugs assayed against Trypanosoma cruzi. Acta Trop 1993; 53: 83-98.
2. Urbina JA. Chemotherapy of Chagas' disease: the how and the why. J Mol Med 1999; 77: 332-8.
3. Gutteridgs WE. Existing chemotherapy and its limitations. Brlt Med Bull 1985; 41: 162-8.
4. Marr JJ, Docampo R. Chemotherapy for Chagas' disease: a perspective of current therapy and considerations for future research. Rev Inf Dis 1986; 8: 884-903.
5. Hunter WN. A structure-based approach to drug discovery; crystallography and implications for the development of antiparasite drugs. Parasitology 1997; 114: S17-S29.
6. Hunter WN. Rational drug design: a multidisciplinary approach. Mol Med Today 1995; 1: 31-4.
7. Douglas KT. Rational drug design in parasitology. Parasitol Today 1994; 10: 389-92.
8. Kuntz ID. Structure-based strategies for drug design and discovery. Science 1992; 257: 1078-82.
9. Hol WGJ Protein crystallography and computer graphics - towards rational drug design. Angew Chem Int Ed Engl 1986; 25: 767-78.
10. Croft SL. Pharmacological approaches to antitrypanosomal chemotherapy. Mem Inst Oswaldo Cruz 1999; 94: 215-20.
11. Wang CC. Validating targets for antiparasite chemotherapy. Parasitology 1997; 114: S31-S44.
12. Hwang HY, Ullman B. Genetic analysis of purine metabolism in Leishmania donovani. J Biol Chem 1997; 272: 19488-96.
13. Hwang HY, Gilberts T, Jardim A, Shlh S, Ullman B. Creation of homozygous mutants of Leishmania donovani with single targeting constructs. J Biol Chem 1996; 271: 30840-6.
14. Marr JJ, Berens RL, Nelson DJ. Antitrypanosomal effect of allopurinol: conversion in vivo to aminopyrazolopyrimidine nucleotides by Trypanosoma cruzi. Science 1978; 201: 1018-20.
15. Cruz AK, Titus R, Beverley SM. Plasticity in chromosome number and testing of essential genes in Leishmania by targeting Proc Natl Acad Sci USA 1993; 90: 1599-603.
16. Mottram JC, McCready BP, Brown KG, Grant KM. Gene disruptiors indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmania mexicana. Mol Microblol 1996; 22: 573-82.
17. Tovar J, Wilkinson S, Mottram JC, Fairlamb AH. Evidence that trypanothlone reductase is an essential enzyme in Leishmania by targeted replacement of the tryA gene locus. Mol Microblol 1998; 29: 653-60.
18. Wirtz E, Clayton C. Inducible gene expression in trypanosomes mediated by a prokaryotic represser. Science 1995; 268: 1179-82.
19. Gutteridge WE. Designer drugs: pipe-dreams or realities? Parasitology 1997; 114: S145-S151.
20. Ridley RG. Plasmodium: drug discovery and development - an industrial perspective. Exp Parasitol 1997; 87: 293-304.
21. Nakayama GR. Microplate assays for high-throughput screening. Curr Opin Drug Disc Devel 1998; 1: 85-91.
22. Fairlamb AH, Cerami A. Metabolism and functions of trypanothione in the Kinetoplastida. Annu Rev Microbiol 1992; 46: 695-729.
23. Ariyanayagam MR, Fairlamb AH. Diamine auxotrophy may be a universal feature of Trypanosoma cruzl epimastigotes. Mol Biochem Parasitol 1997; 84: 111-21.
24. Le Quesne SA, Fairlamb AH. Regulation of a high-affinity diamine transport system in Trypanosoma cruzi epimastigotes. Biochem J 1996; 316: 481-6.
25. 9bis(glutathionyl)aminopropylcadaverine (homotrypanothione) in Trypanosoma cruzi. Eur J Biochem 1994; 226: 1019-27.
26. Docampo R. Antioxidant mechanisms, In: Marr, JJ, Müller, M, editors. Biochemistry and Molecular Biology of Parasites. London: Academic Press, 1995: 147-60.
27. Docampo R. Sensitivity of parasites to free radical damage by antiparasitic drugs. Chem Biol Interact 1990; 73: 1-27.
28. Henderson GB, Ulrich P, Fairlamb AH, Rosenberg I, Pereira M, Sela M, Cerami A, "Subversive" substrates for the enzyme trypanothione disulfide reductase: alternative approach to chemotherapy of Chagas' disease. Proc Natl Acad Sci USA 1988; 85: 5374-78.
29. Shames SL, Fairlamb AH, Cerami A, Walsh CT. Purification and characterization of trypanothione reductase from Crithidia fasciculata, a newly discovered member of the family of disulphide-containlng flavoprotein reductases. Biochemistry 1986; 25: 3519-26.
30. Cunningham ML, Fairlamb AH. Trypanothione reductase from Leist mania donovani-Purification, characterisation and inhibition by trivalent antimonials. Eur J Biochem 1995; 230: 460-8.
31. Krauth-Siegel RL, Enders B, Henderson GB, Fairlamb AH, Schirmer RH. Trypanothione reductase from Trypanosoma cruzi: purification and characterization of the crystalline enzyme. Eur J Biochem 1987; 164: 123-8.
32. Moutiez M, Aumercier M, Schoneck R, Meziane-Cherif D, Lucas V, Aumercier P, Ouaissi A, Sergheraert C, Tartar A. Purification and characterization of a trypanothioneglutathione thioltransferase from Trypanosoma cruzi. Biochem J 1995; 310: 433-7.
33. Moutiez M, Quemeneur E, Sergheraert C, Lucas V, Tartar A, Davioud-Charvet E. Glutathione-dependent activities of Trypanosoma cruzi p52 makes it a new member of the thiol:disulphide oxidoreductase family. Biochem J 1997; 322: 43-8.
34. Gommel DU, Nogoceke E, Morr M, Kiess M, Kalisz HM, Flohé L. Catalytic characteristics of tryparedoxin. Eur J Biochem 1997; 248: 913-8.
35. Nogoceke E, Gommel DU, Kiess M, Kalisz HM, Flohé L. A unique cascade of oxidoreductases catalyses trypanothione-mediated peroxide metabolism in Crithidia fasciculata. Biol Chem 1997; 378: 827-36.
36. Henderson GB, Fairlamb AH, Cerami A. Trypanothione dependent peroxide metabolism in Crithidia fasciculata and Trypanosoma brucei. Mol Biochem Parasitol 1987; 24: 39-45.
37. Guerrero SA, Flohé L, Kalisz HM, Montemartini M, Nogoceke E, Hecht HJ, Steinert P, Singh M. Sequence, heterologous expression and functional characterization of tryparedoxin1 from Crithidia fasciculata. Eur J Biochem 1999; 259: 789-94.
38. Tetaud E, Fairlamb AH. Cloning, expression and reconstitution of the trypanothione-dependent peroxidase system of Crithidia fasciculata. Mol Biochem Parasitol 1998; 96: 111-23.
39. Montemartini M, Nogoceke E, Singh M, Steinert P, Flohé L, Kalisz HM. Sequence analysis of the tryparedoxin peroxidase gene from Crithidia fasciculata and its functional expression in Escherichia coli. J Biol Chem 1998; 273: 4864-71.
40. Carnieri EGS, Moreno SNJ, Docampo R. Trypanothione-dependent peroxide metabolism in Trypanosoma cruzi different stages. Mol Biochem Parasitol 1993; 61: 79-86.
41. Levick MP, Tetaud E, Fairlamb AH, Blackwell JM. Identification and characterisation of a functional peroxidoxin from Leishmania major. Mol Biochem Parasitol 1998; 96: 125-37.
42. Yawetz A, Agosin M. Purification of the glutathione-S-transferass of Trypanosoma cruzi. Comp Biochem Physiol 1981; 68B: 237-43.
43. Yawetz A, Agosin M. Glutathione-S-transferase and drug metabolism in Trypanosoma cruzi: in vivo and in vitro formation of thioethers. Comp Biochem Physiol 1980; 66C: 265-7.
44. Mukhopadhyay R, Dey S, Xu N, Gage D, Lightbody J, Ouellette M, Rosen BP. Trypanothione overproduction and resistance to antimonials and arsenicals in Leishmania. Proc Natl Acad Sci USA 1996; 93; 10383-7.
45. Dey S, Ouellette M, Lightbody J, Papadopoulou B, Rosen BP. An ATP-dependent As(III)-glutathione transport system in membrane vesicles of Leishmania tarentolae. Proc Natl Acad Sci USA 1996; 93: 2192-7.
46. Légaré D, Papadopoulou B, Roy G, Mukhopadhyay R, Haimeur A, Dey S, Grondin K, Brochu C, Rosen BP, Ouellette M. Efflux systems and increased trypanothione levels in arsenite-reslstant Leishmania. Exp Parasitol 1997; 87: 275-82.
47. Ziegler DM. Role of reversible oxidation-reduction of enzyme thiols-disulfides in metabolic regulation. Annu Rev Biochem 1985; 54: 305-29.
48. Lovkvist E, Stjernborg L, Persson L. Feedback regulation of mammalian ornithine decarboxylase. Studies using a transient expression system. Eur J Biochem 1993; 215: 753-59.
49. 1-acetyltransferase - The turning point in polyamine metabolism. FASEB J 1993; 7: 653-61.
50. Davis RH, Morris DR, Coffino P. Sequestered end products and enzyme regulation: The case of ornithine decarboxylase. Microbiol Rev 1992; 56: 280-90.
51. Davis RH. Management of polyamine pools and the regulation of ornithine decarboxylase. J Cell Biochem 1990; 44: 199-205.
52. Hua SB, Li X, Coffino P, Wang CC. Rat antizyme inhibits the activity but does not promote the degradation of mouse ornithine decarboxylase in Trypanosoma brucei. J Biol Chem 1995; 270: 10264-71.
53. Ghoda L, Phillips MA, Bass KE, Wang CC, Coffino P. Trypanosome ornithine decarboxylase is stable because it lacks sequences found in the carboxyl terminus of the mouse enzyme which target the latter for intracellular degradation. J Biol Chem 1990; 265: 11823-6.
54. Phillips MA, Coffino P, Wang CC. Trypanosoma brucei ornithine decarboxylase: enzyme purification, characterization, and expression in Escherichia coli. J Biol Chem 1988; 263: 17933-41.
55. Phillips MA, Coffino P, Wang CC. Cloning and sequencing of the ornithine decarboxylase gene from Trypanosoma brucei: implications for enzyme turnover and selective difluoromethylornithine inhibition. J Biol Chem 1987; 262: 8721-7.
56. Fairlamb AH, Le Quesne SA. Polyamine metabolism in trypanosomes. In: Hide, G, Mottram, JC, Coombs, GH, Holmes, PH, editors. Trypanosomiasis and Leishmaniasis: Biology and Control. Wallingford: CAB International, 1997: 149-61.
57. Shim H, Fairlamb AH. Levels of polyamines, glutathione and glutathione-spermidine conjugates during growth of the insect trypanosomatid Crithidia fasciculata. J Gen Microbiol 1988; 134: 807-17.
58. Tabor H, Tabor CW. Isolation, characterization, and turnover of glutathionylspermidine from Escherichia coli. J Biol Chem 1975; 250: 2648-54.
59. Smith K, Borges A, Ariyanayagam MR, Fairlamb AH. Glutathionylspermidine metabolism in Escherichia coli. Biochem J 1995; 312: 465-9.
60. Bollinger JMJ, Kwon DS, Huisman GW, Kolter R, Walsh CT. Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/ amidase. J Biol Chem 1995; 270: 14031-41.
61. Tetaud E, Manai F, Barrett MP, Nadeau K, Walsh CT, Fairlamb AH. Cloning and characterization of the two enzymes responsible for trypanothione biosynthesis in Crithidia fasciculata. J Biol Chem 1998; 273:19383-90.
62. Alphey MS, Leonard GA, Gourley DG, Tetaud E, Fairlamb AH, Hunter WN. The high-resolution crystal structure of recombinant Crithidia fasdculata tryparedoxin-l. J Biol Chem 1999; in press.
63. Ludemann H, Dormeyer M, Sticherling C, Stallmann D, Follmann H, Krauth-Siegel RL. Trypanosoma brucei tryparedoxin, a thioredoxin-like protein in African trypanosomes. FEBS Lett 1998; 431: 381-5.
64. Henderson GB, Fairlamb AH, Ulrich P, Ceraml A. Substrate specificity of the flavoprotein trypanothione disulfide reductase from Crithidia fasciculata. Biochemistry 1987; 26: 3023-7.
65. Marsh IR, Bradley M. Substrate specificity of trypanothione reductase. Eur J Biochem 1997; 243: 690-4.
66. Jockers-Scherubl MC, Schirmer RH, Krauth-Siegel RL. Trypanothione reductase from Trypanosoma cruzi: catalytic properties of the enzyme and inhibition studies with trypanocidal compounds. Eur J Biochem 1989; 180: 267-72.
67. Borges A, Cunningham ML, Tovar J, Fairlamb AH. Site-directed mutagenesis of the redox-active cysteines of Trypanosoma cruzi trypanothione reductase. Eur J Biochem 1995; 228: 745-52.
68. Zhang Y, Bond CS, Bailey S, Cunningham ML, Fairlamb AH, Hunter WN. The crystal structure of trypanothione reductase from the human pathogen Trypanosoma cruzi at 2.3 Å resolution. Protein Science 1996; 5: 52-61.
69. Jacoby EM, Schlichting I, Lantwin CB, Kabsch W, Krauth-Siegel RL. Crystal structure of the Trypanosoma cruzi trypanothlone reductase-mepacrine complex. Proteins: Structure, Function and Genetics 1996; 24: 73-80.
70. Lantwin CB, Schlichting I, Kabsch W, Pai EF, Krauth-Siegel RL. The structure of Trypanosoma cruzi trypanothione reductase in the oxidized and NADPH reduced state. Proteins: Structure, Function and Genetics 1994; 18: 161-73.
71. Bond CS, Zhang YH, Berrlman M, Cunningham ML, Fairlamb AH, Hunter WN. Crystal structure of Trypanosoma cruzi trypanothione reductase in complex with trypanothione, and the structure-based discovery of new natural product inhibitors. Structure 1999; 7: 81-89.
72. Chan C, Yin H, Garforth J, McKie JH, Jaouhari R, Speers P, Douglas KT, Rock PJ, Yardley V, Croft SL, Fairlamb AH. Phenothiazine inhibitors of trypanothione reductase as potential antitrypanosomal and antlleishmanial drugs. J Med Chem 1998; 41: 148-56.
73. O'Sullivan MC, Zhou QB, Li ZL, Durham TB, Rattendi D, Lane S, Bacchi CJ. Polyamine derivatives as inhibitors of trypanothione reductase and assessment of their trypanocidal activities. Bioorg Med Chem 1997; 5: 2145-55.
74. Girault S, Baillet S, Horvath D, Lucas V, DavioudCharvet E, Tartar A, Sergheraert C. New potent inhibitors of trypanothione reductase from Trypanosoma cruzi in the 2-aminodiphenylsulfide series. Eur J Med Chem 1997; 32: 39-52.
75. Baillet S, Buisine E, Horvath D, Maes L, Bonnet B, Sergheraert C. 2-Amino diphenylsulfides as inhibitors of trypanothione reductase: Modification of the side chain. Bioorg Med Chem 1996; 4: 891-9.
76. Ponasik JA, Strickland C, Faerman C, Savvides S, Karplus PA, Ganem B. Kukoamine A and other hydrophobic acylpolyamines: Potent and selective inhibitors of Crithidia fasciculata trypanothione reduotase. Biochem J 1995; 311 : 371-5.
77. Moreno SNJ, Carnieri EGS, Docampo R, Inhibition of Trypanosoma cruzi trypanolhione reductase by crystal violet. Mol Biochem Parasitol 1994; 67: 313-20.
78. Garforth J, McKie JH, Jaouhari R, Benson TJ, Fairlamb AH, Douglas KT. Rational design of peptide-based inhibitors of trypanothione reductase as potential antitrypanosomeil drugs. Amino Acids 1994; 6: 295-9.
79. Cunningham ML, Zvelebil MJJM, Fairlamb AH. Mechanism of inhibition of trypanothione reductase and glutathione reductase by trivalent organic arsenlcals. Eur J Biochem 1994; 221: 285-95.
80. Cenas N, Bironaite D, Dickancaite E, Anusevicius Z, Sarlauskas J, Blanchard JS. Chinifur, a selective Inhibitor and 'subversive substrate' for Trypanosoma congolense trypanothione reductase. Biochem Biophys Res Commun 1994; 204: 224-9.
81. Tromelin A, Moutiez M, Meziani-Cherif D, Aumercier M, Tartar A, Sergheraert C. Synthesis of non reducible inhibitors for trypanothione reductase from Trypanosoma cruzi. Bioorg Med Chem Lett 1993; 3: 1971-6.
82. Benson TJ, McKie JH, Garforth J, Borges A, Fairlamb AH, Douglas KT. Rationally designed selective inhibitors of trypanothione reductase: Phenothiazines and related tricyclics as lead structures. Biochem J 1992; 286: 9-11.
83. Tovar J, Fairlamb AH. Extrachromosomal, homologous expressicn of trypanothione reductase and its complementary mRNA in Trypanosoma cruzi. Nucleic Acids Res 1996; 24: 2942-9.
84. Kelly JM, Taylor MC, Smith K, Hunter KJ, Fairlamb AH. Phenotype of recombinant Leishmania donovani and Trypanosoma cruzi which overexpress trypanothione reductase: sensitivity towards agents that are thought to induce oxidative stress. Eur J Biochem 1993; 218: 29-37.
85. Tovar J, Cunningham ML, Smith AC, Croft SL, Fairlamb AH. Down-regulation of Leishmania donovani trypanothione reductase by heterologous expression of a transdominant mutant homologue: effect on parasite intracellular survival. Proc Natl Acad Sci USA 1998; 95: 5311-6.
86. Dumas C, Ouellette M, Tovar J, Cunningham ML, Fairlamb AH, Tamar S, Olivier M, Papadopoulou B. Disruption of the trypanothione reductase gene of Leishmania decreases its ability to survive oxidative stress in macrophages. EMBO J 1997; 16: 2590-8.
87. Wang CC. Molecular mechanisms and therapeutic approaches to the treatment of African trypanosomiasis. Annu Rev Pharmacol Toxicol 1995; 35: 93-127.
88. Krauth-S egel RL, Schoneck R. Trypanothione reductase and lipoamide dehydrogenase as targets for a structure-based drug design. FASEB J 1995; 9: 1138-46.
89. Fairlamb AH. Trypanothione metabolism in Trypanosoma cruzi. Mem Inst Oswaldo Cruz 1994; 89 (Suppl. I): 37-9.
90. Marr JJ. Purine analogs as chemotherapeutic agents in leishmaniasis and American trypanosomiasis. J Lab Clin Med 1991; 118: 111-9.
91. Nare B, Luba J, Hardy LW, Beverley SM, New approaches to Leishmania chemotherapy: Pteridine reductase 1 (PTR1) as a target and modulator of antifolate sensitivity. Parasitology1997; 114: S101-S110.
92. Lee MGS, VanderPloeg LHT. Transcription of proteincoding genos in trypanosomes by RNA polymerase l. Annu Rev Microbiol 1997; 51: 463-89.
93. Ullu E, Tsohudi C, Gunzl A. Trans -splicing in trypanosomatid proiozoa. In: Smith, D, Parsons, M, editors. Molecular Biology of Parasitic Protozoa. Oxford: Oxford University Press, 1996:115-133.
94. Stuart K. RNA editing in trypanosomatid mitochondria. Annu Rev Microbiol 1991; 45: 327-44.
95. Shapiro TA, Englund PT. The structure and replication of kinetoplast DNA. Annu Rev Microbiol 1995; 49: 117-43.
96. Urbina JA, Payares G, Molina J, Sanoja C, Liendo A, Lazardi K, Piras MM, Piras R, Perez N, Wincker P, Ryley JF. Cure of short-and long-term experimental Chagas' disease using D0870. Science 1996; 273: 969-71.
97. Urbina JA. Lipid biosynthesis pathways as chemotherapeutic targets in kinetoplastid parasites. Parasitology 1997; 114: S91-S99.
98. Chance M-, Goad LJ. Sterol metabolism of Leishmania and trypanosomes: potential for ohemotherapeutio exploitation. In: Hide, G, Mottram, JC, Coombs, GH, Holmes, PH, editors. Trypanosomiasis and Leishmaniasis: CAB International, 1997: 163-76.
99. Cross GAM, Takle GB. The surface trans-sialidase family of Trypanosoma cruzi. Annu Rev Microbiol 1993; 47: 385-411.
100. Ferguson MAJ. The surface glycoconjugates of trypanosomatid parasites. Philosophical Transactions Of The Royal Society Of London Series B-Biological Sciences 1997; 352: 1295-302.
101. Englund FT. The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors. Annu Rev Biochem 1993; 62: 121-38.
102. Coombs GH, Mottram JC. Parasite proteinases and amino acid metabolism: possibilities for chemotherapeutic exploitation. Parasitology 1997; 114: S61-S80.
103. McKerrow JH, Sun E, Rosenthal PJ, Bouvier J. The proteases and pathogenicity of parasitic protozoa. Annu Rev Microbiol 1993; 47: 821-53.
104. McKerrow JH, McGrath ME, Engel JC. The cysteine protease of Trypanosoma cruzi as a model for antiparasite drug design. Parasitol Today 1995; 11: 279-82.
105. Sommer JM, Wang CC. Targeting proteins to the glycosomes of African trypanosomes. Annu Rev Microbiol 1994; 48: 105-38.
106. Opperdoes FR. Compartmentation of carbohydrate metabolism in trypanosomes. Annu Rev Microbiol 1987; 41: 127-51.
107. Fairlamb AH, Opperdoes FR. Carbohydrate metabolism in African trypanosomes, with special reference to the glycosome. In: Morgan, MJ, editors. Carbohydrate Metabolism in Cultured Cells. New York: Plenum Publishing Corporation, 1986: 183-224.
108. Michels PAM, Hannaert V, Bakker BM. Glycolysis of Kinetoplastida. In: Hide, G, Mottram, JC, Coombs, GH, Holmes, PH, editors. Trypanosomiasis and Leishmaniasis: Biology and Control. Wallingford: CAB International, 1997: 133-48.