Protective role of the Mycobacterium smegmatis IdeR against reactive oxygen species and isoniazid toxicity

Tubercle and Lung Disease

Volumn 79, Issue 2, 1998, Pages 99-106

  Dussurget, O ^a   Rodriguez, M ^a,b   Smith, I ^a  

^a PUBLIC HEALTH RESEARCH INSTITUTE   (United States)

^b NEW YORK UNIVERSITY MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ISONIAZID; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; RNA; SUPEROXIDE DISMUTASE;

ARTICLE; CELL PROTECTION; CONTROLLED STUDY; ENZYME ACTIVITY; GENE EXPRESSION REGULATION; GENE MUTATION; IMMUNOBLOTTING; MYCOBACTERIUM SMEGMATIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; RNA HYBRIDIZATION; STRESS;

MYCOBACTERIUM SMEGMATIS;

EID: 0032453429     PISSN: 09628479     EISSN: None     Source Type: Journal    
DOI: 10.1054/tuld.1998.0011     Document Type: Article

References (59)

1. 1. Miller J F, Mekalanos J J, Falkow S. Coordinate regulation and sensory transduction in the control of bacterial virulence. Science 1989; 243:916-922.
2. 2. Fridovich I. The biology of oxygen radicals. Science 1978; 201:875-880.
3. 3. Clark R A. The human neutrophil respiratory burst oxidase. J Infect Dis 1990; 161: 1140-1147.
4. 4. Eisenstark A. Bacterial genes involved in response to near-ultraviolet irradiation. Adv Genet 1989; 26: 99-147.
5. 5. Kappus H, Sies H. Toxic drug effects associated with oxygen metabolism: redox cycling and lipid peroxidation. Experientia 1981; 37: 1233-1258.
6. 6. Miller R A, Britigan B E. Role of oxidants in microbial pathophysiology. Clin Microbiol Rev 1997; 10: 1-18.
7. 7. Franzon V L, Arondel J, Sansonetti P J. Contribution of superoxide dismutase and catalase activities to Shigella flexneri pathogenesis. Infect Immun 1990; 58: 529-535.
8. 8. Pesci E C, Cottle D L, Pickett C L. Genetic, enzymatic, and pathogenic studies of the iron superoxide dismutase of Campylobacter jejuni. Infect Immun 1994; 62: 2687-2694.
9. 9. Khelef N, DeShazer D, Friedman R L, Guiso N. In vivo and in vitro analysis of Bordetella pertussis catalase and Fe-superoxide dismutase mutants. FEMS Microbiol Lett 1996; 142: 231-235.
10. 10. Farrant J L, Sansone A, Canvin J R et al. Bacterial copper-and zinc-cofactored superoxide dismutase contributes to the pathogenesis of systemic salmonellosis. Mol Microbiol 1997; 25: 785-796.
11. 11. Roggenkamp A, Bittner T, Leitritz L, Sing A, Heesemann J. Contribution of the Mn-cofactored superoxide dismutase (SodA) to the virulence of Yersinia enterocolitica serotype O8. Infect Immun 1997; 65: 4705-4710.
12. 12. D'Mello R A, Langford P R, Kroll J S. Role of bacterial Mn-cofactored superoxide dismutase in oxidative stress responses, nasopharyngeal colonization, and sustained bacteremia caused by Haemophilus infuenzae type b. Infect Immun 1997; 65: 2700-2706.
13. 13. Wilks K E, Dunn K L, Farrant J L et al. Periplasmic superoxide dismutase in meningococcal pathogenicity. Infect Immun 1998; 66: 213-217.
14. 14. Wilson T M, de Lisle G W, Collins D M. Effect of InhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol Microbiol 1995; 15: 1009-1015.
15. 15. Zhang Y, Lathigra R, Garbe T, Catty D, Young D. Genetic analysis of superoxide dismutase, the 23 kilodalton antigen of Mycobacterium tuberculosis. Mol Microbiol 1991; 5: 381-391.
16. 16. Wieles B, van Soolingen D, Holmgren A, Offringa R, Ottenhoff T, Thole J. Unique gene organization of thioredoxin and thioredoxin reductase in Mycobacterium leprae. Mol Microbiol 1995; 16: 921-929.
17. 17. Sherman D R, Sabo P J, Hickey M J et al. Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria. Proc Natl Acad Sci USA 1995; 92: 6625-6629.
18. 18. Rosner J L, Storz G. Regulation of bacterial responses to oxidative stress. Curr Top Cell Regul 1997; 35 163-177.
19. 19. Deretic V, Philipp W, Dhandayuthapani S et al. Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid. Mol Microbiol 1995; 17: 889-900.
20. 20. Dussurget O, Rodriguez M, Smith I. An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response. Mol Microbiol 1996; 22: 535-544.
21. 21. Snapper S B, Melton R E, Mustapha S, Kieser T, Jacobs W R Jr. Isolation and characterization of efficient plasmid transformation mutants of Mycobacterium smegmatis. Mol Microbiol 1990; 4: 1911-1919.
22. 22. Cutting S, Roels R, Losick R. Sporulation operon spoIVF and the characterization of mutations that uncouple mother-cell from forespore gene expression in Bacillus subtilis. J Mol Biol 1991; 221: 1237-1256.
23. 23. Connell N D. Mycobacterium: Isolation, Maintenance, Transformation and Mutant selection, Vol. 45. San Diego, Academic Press, 1994.
24. 24. Beauchamp C, Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal Biochem 1971; 44: 276-287.
25. 25. Harlow E, Lane L. Antibodies. A Laboratory Manual. Cold Spring Harbor, N Y, Cold Spring Harbor Laboratory, 1988.
26. 26. Middlebrook G. Isoniazid-resistance and catalase activity of tubercle bacilli. Am Rev Tubercul 1954; 69: 472-473.
27. 27. Zhang Y, Heym B, Allen B, Young D, Cole S. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 1992; 358: 591-593.
28. 28. Heym B, Alzari P M, Honore N, Cole S T. Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol Microbiol 1995; 15: 235-245.
29. 29. Shoeb H A, Bowman J B U, Ottolenghi A C, Merola. A J. Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra. Antimicrob Agents Chemother 1985; 27: 404-407.
30. 30. Shoeb H A, Bowman B U Jr, Ottolenghi A C, Merola A J. Enzymatic and nonenzymatic superoxide-generating reactions of isoniazid. Antimicrob Agents Chemother 1985; 27: 408-412.
31. 31. Kim E J, Chung H J, Suh B, Hah Y C, Roe J H. Expression and regulation of the sodF gene encoding iron- and zinc-containing superoxide dismutase in Streptomyces coelicolor Muller. J Bacteriol 1998; 180: 2014-2020.
32. 32. Zhang Y, Dhandayuthapani S, Deretic V. Molecular basis for the exquisite sensitivity of Mycobacterium tuberculosis to isoniazid. Proc Natl Acad Sci USA 1996; 93: 13212-13216.
33. 33. Schmitt M P, Predich M, Doukhan L, Smith I, Holmes R K. Characterization of an iron-dependent regulatory protein (IdeR) of Mycobacterium tuberculosis as a functional homolog of the diphtheria toxin represser (DtxR) from Corynebacterium diphtheriae. Infect Immun 1995; 63: 4284-4289.
34. 34. Dussurget O, Gomez M, Timm J et al. Submitted for publication.
35. 35. Rodriguez M, Gold B, Dussurget O, Smith I. Submitted for publication.
36. 36. Christman M F, Morgan R W, Jacobson F S, Ames B N. Positive control of a regulon for defenses against oxidative stress and some heat-shock proteins in Salmonella typhimurium. Cell 1985; 41: 753-762.
37. 37. Tartaglia L A, Storz G, Ames B N. Identification and molecular analysis of oxyR-regulated promoters important for the bacterial adaptation to oxidative stress. J Mol Biol 1989; 210: 709-719.
38. 38. Visick J E, Clarke S. RpoS- and OxyR-independent induction of HPI catalase at stationary phase in Escherichia coli and identification of rpoS mutations in common laboratory strains. J Bacteriol 1997; 179: 4158-4163.
39. 39. Ivanova A, Miller C, Glinsky G, Eisenstark A. Role of rpoS (katF) in oxyR-independent regulation of hydroperoxidase I in Escherichia coli. Mol Microbiol 1994; 12: 571-578
40. 40. Eisenstark A, Yallaly P, Ivanova A, Miller C. Genetic mechanisms involved in cellular recovery from oxidative stress. Arch Insect Biochem Physiol 1995; 29: 159-173.
41. 41. Hassett D J, Sokol P A, Howell M L et al. Ferric uptake regulator (Fur) mutants of Pseudomonas aeruginosa demonstrate defective siderophore-mediated iron uptake, altered aerobic growth, and decreased superoxide dismutase and catalase activities. J Bacteriol 1996; 178: 3996-4003.
42. 42. Touati D, Jacques M, Tardat B, Bouchard L, Despied S. Lethal oxidative damage and mutagenesis are generated by iron in Δfur mutants of Escherichia Coli protective role of superoxide dismutase. J Bacteriol 1995; 177: 2305-2314.
43. 43. Niederhoffer E C, Naranjo C M, Bradley K L, Fee J A. Control of Escherichia coli superoxide dismutase (sodA and sodB) genes by the ferric iron uptake regulation (fur) locus. J Bacteriol 1990; 172: 1930-1938.
44. 44. Tardat B, Touati D. Two global regulators repress the anaerobic expression of MnSOD in Escherichia coli: Fur (ferric uptake regulation) and Arc (aerobic respiration control). Mol Microbiol 1991; 5: 455-465.
45. 45. Imlay J A, Linn S. DNA damage and oxygen radical toxicity. Science 1988; 240: 1302-1309.
46. 46. Imlay J A, Chin S M, Linn S. Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 1988; 240: 640-642.
47. 47. Tardat B, Touati D. Iron and oxygen regulation of Escherichia coli MnSOD expression: competition between the global regulators Fur and ArcA for binding to DNA. Mol Microbiol 1993; 9: 53-63.
48. 48. Compan I, Touati D. Interaction of six global transcription regulators in expression of manganese superoxide dismutase in Escherichia Coli K-12. J Bacteriol 1993; 175: 1687-1696.
49. 49. Storz G, Tartaglia L A, Farr S B, Ames B N. Bacterial defenses against oxidative stress. Trends Genet 1990; 6: 363-368.
50. 50. Deretic V, Song J, Pagan-Ramos E. Loss of oxyR in Mycobacterium tuberculosis.Trends Microbiol 1997; 5: 367-372.
51. 51. Banerjee A, Dubnau E, Quemard A et al. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 1994; 263: 227-230.
52. 52. Rozwarski D A, Grant G A, Barton D, Jacobs W R Jr, Sacchettini J C. Modification of the NADH of the isoniazid target (InhA) from mycobacterium tuberculosis. Science 1998; 279: 98-102.
53. 53. Mdluli K, Sherman D R, Hickey M J et al. Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis. J Infect Dis 1996; 174: 1085-1090.
54. 54. Rosner J L, Susceptibilities of oxyR regulon mutants of Escherichia coli and Salmonella typhimurium to isoniazid. Antimicrob Agents Chemother 1993; 37: 2251-2253.
55. 55. Rosner J L, Storz G. Effects of peroxides on susceptibilities of Escherichia coli and Mycobacterium smegmatis to isoniazid. Antimicrob Agents Chemother 1994; 38: 1829-1833.
56. 56. Sinha B K. Enzymatic activation of hydrazine derivatives. A spin-trapping study. J Biol Chem 1983; 258: 796-801.
57. 57. Johnson K, Schultz P G. Mechanistic studies of the oxidation of isoniazid by the catalase peroxidase from Mycobacterium tuberculosis. J Am Chem Soc 1994; 116: 7425-7426.
58. 58. Hillar A, Loewen P C. Comparison of isoniazid oxidation catalyzed by bacterial catalase-peroxidases and horseradish peroxidase. Arch Biochem Biophys 1995; 323: 438-446.
59. 59. Wang J Y, Burger R M, Drlica K. A role for superoxide in catalase-peroxidase mediated isoniazid action against mycobacteria. Antimicrob Agents Chemother 1998; 42: 709-711.