IRONy OF FATE: Role of iron-mediated ROS in Leishmania differentiation

Trends in Parasitology

Volumn 29, Issue 10, 2013, Pages 489-496

  Mittra, Bidyottam ^a   Andrews, Norma W ^a  

^a Bldg 142   (United States)

Author keywords

Differentiation; FeSOD; Iron; Leishmania; ROS; Virulence

Indexed keywords

HYDROGEN PEROXIDE; IRON; REACTIVE OXYGEN METABOLITE; SUPEROXIDE DISMUTASE;

AMASTIGOTE; AUTOPHAGY; CELL DIFFERENTIATION; CELL VACUOLE; IRON TRANSPORT; LEISHMANIA; MACROPHAGE; NONHUMAN; OXIDATION REDUCTION REACTION; PH; PROMASTIGOTE; REVIEW; TEMPERATURE; VIRULENCE;

HEXAPODA; MAMMALIA; PROTOZOA;

EID: 84884414859     PISSN: 14714922     EISSN: 14715007     Source Type: Journal    
DOI: 10.1016/j.pt.2013.07.007     Document Type: Review

References (71)

1. World Health Organization Control of the leishmaniases. World Health Organ. Tech. Rep. Ser. 2010, Xii-xiii:1-186.
2. Debrabant A., et al. Generation of Leishmania donovani axenic amastigotes: their growth and biological characteristics. Int. J. Parasitol. 2004, 34:205-217.
3. Gupta N., et al. In vitro cultivation and characterization of axenic amastigotes of Leishmania. Trends Parasitol. 2001, 17:150-153.
4. Saar Y., et al. Characterization of developmentally-regulated activities in axenic amastigotes of Leishmania donovani. Mol. Biochem. Parasitol. 1998, 95:9-20.
5. Tsigankov P., et al. What has proteomics taught us about Leishmania development?. Parasitology 2012, 139:1146-1157.
6. Holzer T.R., et al. Expression profiling by whole-genome interspecies microarray hybridization reveals differential gene expression in procyclic promastigotes, lesion-derived amastigotes, and axenic amastigotes in Leishmania mexicana. Mol. Biochem. Parasitol. 2006, 146:198-218.
7. Saxena A., et al. Analysis of the Leishmania donovani transcriptome reveals an ordered progression of transient and permanent changes in gene expression during differentiation. Mol. Biochem. Parasitol. 2007, 152:53-65.
8. Rosenzweig D., et al. Post-translational modification of cellular proteins during Leishmania donovani differentiation. Proteomics 2008, 8:1843-1850.
9. Lahav T., et al. Multiple levels of gene regulation mediate differentiation of the intracellular pathogen Leishmania. FASEB J. 2011, 25:515-525.
10. Rosenzweig D., et al. Retooling Leishmania metabolism: from sand fly gut to human macrophage. FASEB J. 2008, 22:590-602.
11. Depledge D.P., et al. Comparative expression profiling of Leishmania: modulation in gene expression between species and in different host genetic backgrounds. PLoS Negl. Trop. Dis. 2009, 3:e476.
12. Bates P.A., et al. Axenic cultivation and characterization of Leishmania mexicana amastigote-like forms. Parasitology 1992, 105:193-202.
13. Bates P.A. Housekeeping by Leishmania. Trends Parasitol. 2006, 22:447-448.
14. Mittra B., et al. Iron uptake controls the generation of Leishmania infective forms through regulation of ROS levels. J. Exp. Med. 2013, 210:401-416.
15. Huynh C., Andrews N.W. Iron acquisition within host cells and the pathogenicity of Leishmania. Cell. Microbiol. 2008, 10:293-300.
16. Taylor M.C., Kelly J.M. Iron metabolism in trypanosomatids, and its crucial role in infection. Parasitology 2010, 137:899-917.
17. Blackwell J.M., et al. SLC11A1 (formerly NRAMP1) and disease resistance. Cell. Microbiol. 2001, 3:773-784.
18. Marquis J.F., Gros P. Intracellular Leishmania: your iron or mine?. Trends Microbiol. 2007, 15:93-95.
19. Das N.K., et al. Leishmania donovani depletes labile iron pool to exploit iron uptake capacity of macrophage for its intracellular growth. Cell. Microbiol. 2009, 11:83-94.
20. Borges V.M., et al. Subverted transferrin trafficking in Leishmania-infected macrophages. Parasitol. Res. 1998, 84:811-822.
21. Wilson M.E., et al. Acquisition of iron from transferrin and lactoferrin by the protozoan Leishmania chagasi. Infect. Immun. 1994, 62:3262-3269.
22. Wilson M.E., Britigan B.E. Iron acquisition by parasitic protozoa. Parasitol. Today 1998, 14:348-353.
23. Flannery A.R., et al. LFR1 ferric iron reductase of Leishmania amazonensis is essential for the generation of infective parasite forms. J. Biol. Chem. 2011, 286:23266-23279.
24. Huynh C., et al. A Leishmania amazonensis ZIP family iron transporter is essential for parasite replication within macrophage phagolysosomes. J. Exp. Med. 2006, 203:2363-2375.
25. Hindt M.N., Guerinot M.L. Getting a sense for signals: regulation of the plant iron deficiency response. Biochim. Biophys. Acta 2012, 1823:1521-1530.
26. Campos-Salinas J., et al. A new ATP-binding cassette protein is involved in intracellular haem trafficking in Leishmania. Mol. Microbiol. 2011, 79:1430-1444.
27. Carvalho S., et al. Heme as a source of iron to Leishmania infantum amastigotes. Acta Trop. 2009, 109:131-135.
28. Huynh C., et al. Heme uptake by Leishmania amazonensis is mediated by the transmembrane protein LHR1. PLoS Pathog. 2012, 8:e1002795.
29. Williams R.A., et al. Cysteine peptidases CPA and CPB are vital for autophagy and differentiation in Leishmania mexicana. Mol. Microbiol. 2006, 61:655-674.
30. Balaban R.S., et al. Mitochondria, oxidants, and aging. Cell 2005, 120:483-495.
31. Wallace D.C. A mitochondrial paradigm of metabolic and degenerative diseases, aging, and cancer: a dawn for evolutionary medicine. Annu. Rev. Genet. 2005, 39:359-407.
32. Buetler T.M., et al. Role of superoxide as a signaling molecule. News Physiol. Sci. 2004, 19:120-123.
33. 2, a necessary evil for cell signaling. Science 2006, 312:1882-1883.
34. Owusu-Ansah E., Banerjee U. Reactive oxygen species prime Drosophila haematopoietic progenitors for differentiation. Nature 2009, 461:537-541.
35. Hamanaka R.B., Chandel N.S. Mitochondrial reactive oxygen species regulate cellular signaling and dictate biological outcomes. Trends Biochem. Sci. 2010, 35:505-513.
36. Kinnula V.L., Crapo J.D. Superoxide dismutases in malignant cells and human tumors. Free Radic. Biol. Med. 2004, 36:718-744.
37. Gius D., Spitz D.R. Redox signaling in cancer biology. Antioxid. Redox Signal. 2006, 8:1249-1252.
38. Pervaiz S., Clement M.V. Superoxide anion: oncogenic reactive oxygen species?. Int. J. Biochem. Cell Biol. 2007, 39:1297-1304.
39. Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 2002, 82:47-95.
40. Finkel T. Oxidant signals and oxidative stress. Curr. Opin. Cell Biol. 2003, 15:247-254.
41. Theopold U. Developmental biology: a bad boy comes good. Nature 2009, 461:486-487.
42. Dunand C., et al. Distribution of superoxide and hydrogen peroxide in Arabidopsis root and their influence on root development: possible interaction with peroxidases. New Phytol. 2007, 174:332-341.
43. Tsukagoshi H., et al. Transcriptional regulation of ROS controls transition from proliferation to differentiation in the root. Cell 2010, 143:606-616.
44. 2 signaling. Antioxid. Redox Signal. 2011, 14:459-468.
45. Alzate J.F., et al. Mitochondrial superoxide mediates heat-induced apoptotic-like death in Leishmania infantum. Mol. Biochem. Parasitol. 2007, 152:192-202.
46. Miller M.A., et al. Inducible resistance to oxidant stress in the protozoan Leishmania chagasi. J. Biol. Chem. 2000, 275:33883-33889.
47. Wilson M.E., et al. Response of Leishmania chagasi promastigotes to oxidant stress. Infect. Immun. 1994, 62:5133-5141.
48. Plewes K.A., et al. Iron superoxide dismutases targeted to the glycosomes of Leishmania chagasi are important for survival. Infect. Immun. 2003, 71:5910-5920.
49. Van Assche T., et al. Leishmania-macrophage interactions: insights into the redox biology. Free Radic. Biol. Med. 2011, 51:337-351.
50. Adak S., Pal S. Ascorbate peroxidase acts as a novel determiner of redox homeostasis in Leishmania. Antioxid. Redox Signal. 2012, 10.1089/ars.2012.4745.
51. Iyer J.P., et al. Crucial role of cytosolic tryparedoxin peroxidase in Leishmania donovani survival, drug response and virulence. Mol. Microbiol. 2008, 68:372-391.
52. Swenerton R.K., et al. Leishmania subtilisin is a maturase for the trypanothione reductase system and contributes to disease pathology. J. Biol. Chem. 2010, 285:31120-31129.
53. Scherz-Shouval R., Elazar Z. Regulation of autophagy by ROS: physiology and pathology. Trends Biochem. Sci. 2011, 36:30-38.
54. Williams R.A., et al. Distinct roles in autophagy and importance in infectivity of the two ATG4 cysteine peptidases of Leishmania major. J. Biol. Chem. 2013, 288:3678-3690.
55. Sardar A.H., et al. Proteome changes associated with Leishmania donovani promastigote adaptation to oxidative and nitrosative stresses. J. Proteomics 2013, 81:185-199.
56. Fleischhacker A.S., Kiley P.J. Iron-containing transcription factors and their roles as sensors. Curr. Opin. Chem. Biol. 2011, 15:335-341.
57. Anderson C.P., et al. Mammalian iron metabolism and its control by iron regulatory proteins. Biochim. Biophys. Acta 2012, 1823:1468-1483.
58. van Weelden S.W., et al. Procyclic Trypanosoma brucei do not use Krebs cycle activity for energy generation. J. Biol. Chem. 2003, 278:12854-12863.
59. Long S., et al. Ancestral roles of eukaryotic frataxin: mitochondrial frataxin function and heterologous expression of hydrogenosomal Trichomonas homologues in trypanosomes. Mol. Microbiol. 2008, 69:94-109.
60. Long S., et al. Mitochondrial localization of human frataxin is necessary but processing is not for rescuing frataxin deficiency in Trypanosoma brucei. Proc. Natl. Acad. Sci. U.S.A. 2008, 105:13468-13473.
61. Groeger G., et al. Hydrogen peroxide as a cell-survival signaling molecule. Antioxid. Redox Signal. 2009, 11:2655-2671.
62. Szoor B., et al. A novel phosphatase cascade regulates differentiation in Trypanosoma brucei via a glycosomal signaling pathway. Genes Dev. 2010, 24:1306-1316.
63. Nascimento M., et al. Identification and characterization of a protein-tyrosine phosphatase in Leishmania: involvement in virulence. J. Biol. Chem. 2006, 281:36257-36268.
64. Naderer T., et al. Calcineurin is required for Leishmania major stress response pathways and for virulence in the mammalian host. Mol. Microbiol. 2011, 80:471-480.
65. Tracy K., Baehrecke E.H. The role of autophagy in Drosophila metamorphosis. Curr. Top. Dev. Biol. 2013, 103:101-125.
66. Klionsky D. An overview of autophagy: morphology, mechanism and regulation. Antioxid. Redox Signal. 2013, 10.1089/ars.2013.5371.
67. Williams R.A., et al. ATG5 is essential for ATG8-dependent autophagy and mitochondrial homeostasis in Leishmania major. PLoS Pathog. 2012, 8:e1002695.
68. Herman M., et al. Turnover of glycosomes during life-cycle differentiation of Trypanosoma brucei. Autophagy 2008, 4:294-308.
69. Getachew F., Gedamu L. Leishmania donovani mitochondrial iron superoxide dismutase A is released into the cytosol during miltefosine induced programmed cell death. Mol. Biochem. Parasitol. 2012, 183:42-51.
70. Atwood J.A., et al. The Trypanosoma cruzi proteome. Science 2005, 309:473-476.
71. Piacenza L., et al. Mitochondrial superoxide radicals mediate programmed cell death in Trypanosoma cruzi: cytoprotective action of mitochondrial iron superoxide dismutase overexpression. Biochem. J. 2007, 403:323-334.