Control of iron metabolism in Mycobacterium tuberculosis

Trends in Microbiology

Volumn 14, Issue 7, 2006, Pages 320-327

  Rodriguez, G Marcela ^a  

^a PUBLIC HEALTH RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL SURVIVAL; BIOAVAILABILITY; CONTROLLED STUDY; GENETIC TRANSCRIPTION; IRON METABOLISM; IRON TRANSPORT; MICROBIAL GROWTH; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; REVIEW; TUBERCULOSIS;

BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; DRUG DESIGN; HOMEOSTASIS; IRON; MODELS, BIOLOGICAL; MODELS, MOLECULAR; MYCOBACTERIUM TUBERCULOSIS; OXAZOLES; REPRESSOR PROTEINS;

BACTERIA (MICROORGANISMS); MYCOBACTERIUM TUBERCULOSIS;

EID: 33745484154     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2006.05.006     Document Type: Review

References (51)

1. Weinberg E.D. Iron loading and disease surveillance. Emerg. Infect. Dis. 5 (1999) 346-352
2. Imlay J.A., et al. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240 (1988) 640-642
3. Litwin C.M., and Calderwood S.B. Role of iron in regulation of virulence genes. Clin. Microbiol. Rev. 6 (1993) 137-149
4. Ratledge C. Iron Metabolism. In: Ratledge C., and Dale J. (Eds). Mycobacteria: Molecular Biology and Virulence (1999), Blackwell Science 260-286
5. Gobin J., and Horwitz M. Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J. Exp. Med. 183 (1996) 1527-1532
6. Ratledge C., and Ewing M. The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis. Microbiology 142 (1996) 2207-2212
7. De Voss J.J., et al. The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 1252-1257
8. Raghu B., et al. Effect of iron on the growth and siderophore production of mycobacteria. Biochem. Mol. Biol. Int. 31 (1993) 341-348
9. Rodriguez G.M., et al. ideR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect. Immun. 70 (2002) 3371-3381
10. Quadri L.E.N., et al. Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem. Biol. 5 (1998) 631-645
11. Krithika R., et al. A genetic locus required for iron acquisition in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2069-2074
12. Braun V., and Killmann H. Bacterial solutions to the iron-supply problem. Trends Biochem. Sci. 24 (1999) 104-109
13. Rodriguez G.M., and Smith I. Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J. Bacteriol. 188 (2006) 424-430
14. Braibant M., et al. The ATP binding cassette (ABC) transport systems of Mycobacterium tuberculosis. FEMS Microbiol Rev 24 (2000) 449-467
15. Luo M., et al. Mycobactin-mediated iron acquisition within macrophages. Nat. Chem. Biol. 1 (2005) 149-153
16. Agranoff D., et al. Mycobacterium tuberculosis expresses a novel pH-dependent divalent cation transporter belonging to the Nramp family. J. Exp. Med. 190 (1999) 717-724
17. Boechat N., et al. Disruption of the gene homologous to mammalian Nramp1 in Mycobacterium tuberculosis does not affect virulence in mice. Infect. Immun. 70 (2002) 4124-4131
18. Wagner D., et al. Changes of the phagosomal elemental concentrations by Mycobacterium tuberculosis Mramp. Microbiology 151 (2005) 323-332
19. Calder K.M., and Horwitz M.A. Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microb. Pathog. 24 (1998) 133-143
20. Wong D., et al. Identification of Fur, aconitase and other proteins expressed by Mycobacterium tuberculosis under conditions of low and high concentrations of iron by combined two-dimensional gel electrophoresis and mass spectrometry. Infect. Immun. 67 (1999) 327-336
21. Zahrt T.C., and Deretic V. An essential two-component signal transduction system in Mycobacterium tuberculosis. J. Bacteriol. 182 (2000) 3832-3838
22. Bagg A., and Neilands J.B. Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol. Rev. 51 (1987) 509-518
23. Delany I., et al. Fur functions as an activator and as a repressor of putative virulence genes in Neisseria meningitidis. Mol. Microbiol. 52 (2004) 1081-1090
24. Masse E., and Arguin M. Ironing out the problem: new mechanisms of iron homeostasis. Trends Biochem. Sci. 30 (2005) 462-468
25. Cole S.T., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393 (1998) 537-544
26. Zahrt T.C., et al. Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG. Mol. Microbiol. 39 (2001) 1174-1185
27. Pym A.S., et al. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol. Microbiol. 40 (2001) 879-889
28. Canneva F., et al. Rv2358 and FurB: two transcriptional regulators from Mycobacterium tuberculosis which respond to zinc. J. Bacteriol. 187 (2005) 5837-5840
29. Guedon E., and Helmann J.D. Origins of metal ion selectivity in the DtxR/MntR family of metalloregulators. Mol. Microbiol. 48 (2003) 495-506
30. Schmitt M.P., et al. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin repressor (DtxR) from Corynebacterium diphtheriae. Infect. Immun. 63 (1995) 4284-4289
31. Pohl E., et al. Crystal structure of the iron-dependent regulator (IdeR) from Mycobacterium tuberculosis shows both metal binding sites fully occupied. J. Mol. Biol. 285 (1999) 1145-1156
32. Feese M.D., et al. Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-Å resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J. Biol. Chem. 276 (2001) 5959-5966
33. Wisedchaisri G., et al. Crystal structure of an IdeR-DNA complex reveals a conformational change in activated IdeR for base-specific interactions. J. Mol. Biol. 342 (2004) 1155-1169
34. Chou C.J., et al. Functional studies of the Mycobacterium tuberculosis iron-dependent regulator. J. Biol. Chem. 279 (2004) 53554-53561
35. Rodriguez G.M., et al. Identification and characterization of two divergently transcribed iron regulated genes in Mycobacterium tuberculosis. Tuber. Lung Dis. 79 (1999) 287-298
36. Gold B., et al. The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol. Microbiol. 42 (2001) 851-865
37. Dussurget O., et al. Protective role of the mycobacterial IdeR against reactive oxygen species and isoniazid toxicity. Tuber. Lung Dis. 79 (1998) 99-106
38. Schaible U.E., and Kaufmann S.H. Iron and microbial infection. Nat. Rev. Microbiol. 2 (2004) 946-953
39. Gangaidzo I.T., et al. Association of pulmonary tuberculosis with increased dietary iron. J. Infect. Dis. 184 (2001) 936-939
40. Schaible U.E., et al. Correction of the iron overload defect in β-2-microglobulin knockout mice by lactoferrin abolishes their increased susceptibility to tuberculosis. J. Exp. Med. 196 (2002) 1507-1513
41. Sturgill-Koszycki S., et al. Mycobacterium-containing phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis. EMBO J. 15 (1996) 6960-6968
42. Clemens D.L., and Horwitz M.A. The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J. Exp. Med. 184 (1996) 1349-1355
43. Olakanmi O., et al. Intraphagosomal Mycobacterium tuberculosis acquires iron from both extracellular transferrin and intracellular iron pools: impact of interferon-γ and hemochromatosis. J. Biol. Chem. 277 (2002) 49727-49734
44. Wagner D., et al. Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system. J. Immunol. 174 (2005) 1491-1500
45. Timm J., et al. Differential expression of iron-, carbon-, and oxygen-responsive mycobacterial genes in the lungs of chronically infected mice and tuberculosis patients. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 14321-14326
46. Goetz D.H., et al. The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol. Cell 10 (2002) 1033-1043
47. Holmes M.A., et al. Siderocalin (Lcn 2) also binds carboxymycobactins, potentially defending against mycobacterial infections through iron sequestration. Structure 13 (2005) 29-41
48. Ferreras J.A., et al. Small-molecule inhibition of siderophore biosynthesis in Mycobacterium tuberculosis and Yersinia pestis. Nat. Chem. Biol. 1 (2005) 29-32
49. Somu R.V., et al. Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis. J. Med. Chem. 49 (2006) 31-34
50. Manabe Y.C., et al. Both Corynebacterium diphtheriae DtxR(E175K) and Mycobacterium tuberculosis IdeR(D177K) are dominant positive repressors of IdeR-regulated genes in M. tuberculosis. Infect. Immun. 73 (2005) 5988-5994
51. Manabe Y., et al. Attenuation of virulence in Mycobacterium tuberculosis expressing a constitutively active iron repressor. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 12844-12848