Redox Biology of Tuberculosis Pathogenesis

Advances in Microbial Physiology

Volumn 60, Issue , 2012, Pages 263-324

  Trivedi, Abhishek ^a   Singh, Nisha ^a   Bhat, Shabir Ahmed ^a   Gupta, Pawan ^a   Kumar, Ashwani ^a  

^a INSTITUTE OF MICROBIAL TECHNOLOGY   (India)

Author keywords

DosR; Metabolic flexibility; Mycothiol; Pathogenesis; Protective enzymes; Redox homeostasis; Thioredoxin; Virulence; WhiB3

Indexed keywords

ALKYL HYDROPEROXIDASE; BACTERIAL PROTEIN; CARBON MONOXIDE; CATALASE; DOSS PROTEIN; DOST PROTEIN; NITRIC OXIDE; OXYGEN; PEROXIDASE; PEROXIREDOXIN; PROTEIN; SIGMA FACTOR RSRA; SUPEROXIDE DISMUTASE; THIOREDOXIN; UNCLASSIFIED DRUG;

ACIDITY; ARTICLE; GRANULOMA; HOMEOSTASIS; HYPOXIA; IMMUNE SYSTEM; MACROPHAGE; MYCOBACTERIUM TUBERCULOSIS; NITROSATIVE STRESS; NONHUMAN; OXIDATION REDUCTION STATE; OXIDATIVE STRESS; PATHOGENESIS; REDOX STRESS; SENSOR; TUBERCULOSIS;

CORYNEBACTERINEAE; MYCOBACTERIUM TUBERCULOSIS;

EID: 84861442848     PISSN: 00652911     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-398264-3.00004-8     Document Type: Chapter

References (252)

1. Adams L.B., Dinauer M.C., Morgenstern D.E., Krahenbuhl J.L. Comparison of the roles of reactive oxygen and nitrogen intermediates in the host response to Mycobacterium tuberculosis using transgenic mice. Tuber. Lung Dis. 1997, 78:237-246.
2. Agarwal N., Raghunand T.R., Bishai W.R. Regulation of the expression of whiB1 in Mycobacterium tuberculosis: role of cAMP receptor protein. Microbiology 2006, 152:2749-2756.
3. Akif M., Suhre K., Verma C., Mande S.C. Conformational flexibility of Mycobacterium tuberculosis thioredoxin reductase: crystal structure and normal-mode analysis. Acta Crystallogr. D Biol. Crystallogr. 2005, 61:1603-1611.
4. Akif M., Khare G., Tyagi A.K., Mande S.C., Sardesai A.A. Functional studies of multiple thioredoxins from Mycobacterium tuberculosis. J. Bacteriol. 2008, 190:7087-7095.
5. Alam M.S., Garg S.K., Agrawal P. Molecular function of WhiB4/Rv3681c of Mycobacterium tuberculosis H37Rv: a [4Fe-4S] cluster co-ordinating protein disulphide reductase. Mol. Microbiol. 2007, 63:1414-1431.
6. Alam M.S., Garg S.K., Agrawal P. Studies on structural and functional divergence among seven WhiB proteins of Mycobacterium tuberculosis H37Rv. FEBS J. 2009, 276:76-93.
7. Allen D.M., Chng H.H. Disseminated Mycobacterium flavescens in a probable case of chronic granulomatous disease. J. Infect. 1993, 26:83-86.
8. Andersen P., Askgaard D., Ljungqvist L., Bennedsen J., Heron I. Proteins released from Mycobacterium tuberculosis during growth. Infect. Immun. 1991, 59:1905-1910.
9. Ando M., Suga M., Sugimoto M., Tokuomi H. Superoxide production in pulmonary alveolar macrophages and killing of BCG by the superoxide-generating system with or without catalase. Infect. Immun. 1979, 24:404-410.
10. Ascenzi P., Bolognesi M., Milani M., Guertin M., Visca P. Mycobacterial truncated hemoglobins: from genes to functions. Gene 2007, 398:42-51.
11. Ascenzi P., De Marinis E., Coletta M., Visca P. H2O2 and NO scavenging by Mycobacterium leprae truncated hemoglobin O. Biochem. Biophys. Res. Commun. 2008, 373:197-201.
12. Ascenzi P., De Marinis E., Visca P., Ciaccio C., Coletta M. Peroxynitrite detoxification by ferryl Mycobacterium leprae truncated hemoglobin O. Biochem. Biophys. Res. Commun. 2009, 380:392-396.
13. Aslund F., Beckwith J. Bridge over troubled waters: sensing stress by disulfide bond formation. Cell 1999, 96:751-753.
14. Aston C., Rom W.N., Talbot A.T., Reibman J. Early inhibition of mycobacterial growth by human alveolar macrophages is not due to nitric oxide. Am. J. Respir. Crit. Care Med. 1998, 157:1943-1950.
15. Babior B.M. NADPH oxidase: an update. Blood 1999, 93:1464-1476.
16. Baek S.H., Li A.H., Sassetti C.M. Metabolic regulation of mycobacterial growth and antibiotic sensitivity. PLoS Biol. 2011, 9:e1001065.
17. Barranco-Medina S., Lazaro J.J., Dietz K.J. The oligomeric conformation of peroxiredoxins links redox state to function. FEBS Lett. 2009, 583:1809-1816.
18. Battistoni A. Role of prokaryotic Cu, Zn superoxide dismutase in pathogenesis. Biochem. Soc. Trans. 2003, 31:1326-1329.
19. Baughn A.D., Garforth S.J., Vilcheze C., Jacobs W.R. An anaerobic-type alpha-ketoglutarate ferredoxin oxidoreductase completes the oxidative tricarboxylic acid cycle of Mycobacterium tuberculosis. PLoS Pathog. 2009, 5:e1000662.
20. Berney M., Cook G.M. Unique flexibility in energy metabolism allows mycobacteria to combat starvation and hypoxia. PLoS One 2010, 5:e8614.
21. Beste D.J., Bonde B., Hawkins N., Ward J.L., Beale M.H., Noack S., Noh K., Kruger N.J., Ratcliffe R.G., Mcfadden J. (1)(3)C metabolic flux analysis identifies an unusual route for pyruvate dissimilation in mycobacteria which requires isocitrate lyase and carbon dioxide fixation. PLoS Pathog. 2011, 7:e1002091.
22. Betts J.C., Lukey P.T., Robb L.C., Mcadam R.A., Duncan K. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol. Microbiol. 2002, 43:717-731.
23. Bloch H., Segal W. Biochemical differentiation of Mycobacterium tuberculosis grown in vivo and in vitro. J. Bacteriol. 1956, 72:132-141.
24. Bogdan C., Rollinghoff M., Diefenbach A. Reactive oxygen and reactive nitrogen intermediates in innate and specific immunity. Curr. Opin. Immunol. 2000, 12:64-76.
25. Boon C., Dick T. Mycobacterium bovis BCG response regulator essential for hypoxic dormancy. J. Bacteriol. 2002, 184:6760-6767.
26. Bornemann C., Jardine M.A., Spies H.S., Steenkamp D.J. Biosynthesis of mycothiol: elucidation of the sequence of steps in Mycobacterium smegmatis. Biochem. J. 1997, 325(Pt 3):623-629.
27. Boshoff H.I., Myers T.G., Copp B.R., Mcneil M.R., Wilson M.A., Barry C.E. The transcriptional responses of Mycobacterium tuberculosis to inhibitors of metabolism: novel insights into drug mechanisms of action. J. Biol. Chem. 2004, 279:40174-40184.
28. Boshoff H.I., Xu X., Tahlan K., Dowd C.S., Pethe K., Camacho L.R., Park T.H., Yun C.S., Schnappinger D., Ehrt S., Williams K.J., Barry C.E. Biosynthesis and recycling of nicotinamide cofactors in Mycobacterium tuberculosis. An essential role for NAD in nonreplicating bacilli. J. Biol. Chem. 2008, 283:19329-19341.
29. Braunstein M., Espinosa B.J., Chan J., Belisle J.T., Jacobs W.R. SecA2 functions in the secretion of superoxide dismutase A and in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 2003, 48:453-464.
30. Brugmann W.B., Firmani M.A. Low concentrations of nitric oxide exert a hormetic effect on Mycobacterium tuberculosis in vitro. J. Clin. Microbiol. 2005, 43:4844-4846.
31. Bryk R., Griffin P., Nathan C. Peroxynitrite reductase activity of bacterial peroxiredoxins. Nature 2000, 407:211-215.
32. Bryk R., Lima C.D., Erdjument-Bromage H., Tempst P., Nathan C. Metabolic enzymes of mycobacteria linked to antioxidant defense by a thioredoxin-like protein. Science 2002, 295:1073-1077.
33. Buchmeier N.A., Newton G.L., Fahey R.C. A mycothiol synthase mutant of Mycobacterium tuberculosis has an altered thiol-disulfide content and limited tolerance to stress. J. Bacteriol. 2006, 188:6245-6252.
34. Cardona P.J., Gordillo S., Amat I., Diaz J., Lonca J., Vilaplana C., Pallares A., Llatjos R., Ariza A., Ausina V. Catalase-peroxidase activity has no influence on virulence in a murine model of tuberculosis. Tuberculosis (Edinb.) 2003, 83:351-359.
35. Chan J., Xing Y., Magliozzo R.S., Bloom B.R. Killing of virulent Mycobacterium tuberculosis by reactive nitrogen intermediates produced by activated murine macrophages. J. Exp. Med. 1992, 175:1111-1122.
36. Chan J., Tanaka K., Carroll D., Flynn J., Bloom B.R. Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis. Infect. Immun. 1995, 63:736-740.
37. Chan E.D., Chan J., Schluger N.W. What is the role of nitric oxide in murine and human host defense against tuberculosis? Current knowledge. Am. J. Respir. Cell Mol. Biol. 2001, 25:606-612.
38. Chao J.D., Papavinasasundaram K.G., Zheng X., Chavez-Steenbock A., Wang X., Lee G.Q., Av-Gay Y. Convergence of Ser/Thr and two-component signaling to coordinate expression of the dormancy regulon in Mycobacterium tuberculosis. J. Biol. Chem. 2010, 285:29239-29246.
39. Chater K.F. A morphological and genetic mapping study of white colony mutants of Streptomyces coelicolor. J. Gen. Microbiol. 1972, 72:9-28.
40. Chen L., Xie Q.W., Nathan C. Alkyl hydroperoxide reductase subunit C (AhpC) protects bacterial and human cells against reactive nitrogen intermediates. Mol. Cell 1998, 1:795-805.
41. Cho H.Y., Cho H.J., Kim Y.M., Oh J.I., Kang B.S. Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis. J. Biol. Chem. 2009, 284:13057-13067.
42. Cho H.Y., Cho H.J., Kim M.H., Kang B.S. Blockage of the channel to heme by the E87 side chain in the GAF domain of Mycobacterium tuberculosis DosS confers the unique sensitivity of DosS to oxygen. FEBS Lett. 2011, 585:1873-1878.
43. Chusid M.J., Parrillo J.E., Fauci A.S. Chronic granulomatous disease. Diagnosis in a 27-year-old man with Mycobacterium fortuitum. JAMA 1975, 233:1295-1296.
44. Claiborne A., Malinowski D.P., Fridovich I. Purification and characterization of hydroperoxidase II of Escherichia coli B. J. Biol. Chem. 1979, 254:11664-11668.
45. Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C., Harris D., Gordon S.V., Eiglmeier K., Gas S., Barry C.E., Tekaia F., Badcock K., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393:537-544.
46. Cooper J.B., Mcintyre K., Badasso M.O., Wood S.P., Zhang Y., Garbe T.R., Young D. X-ray structure analysis of the iron-dependent superoxide dismutase from Mycobacterium tuberculosis at 2.0 Angstroms resolution reveals novel dimer-dimer interactions. J. Mol. Biol. 1995, 246:531-544.
47. Cooper A.M., Pearl J.E., Brooks J.V., Ehlers S., Orme I.M. Expression of the nitric oxide synthase 2 gene is not essential for early control of Mycobacterium tuberculosis in the murine lung. Infect. Immun. 2000, 68:6879-6882.
48. Corper H.J., Cohn M.L. The viability and virulence of old cultures of tubercle bacilli; studies on 30-year-old broth cultures maintained at 37 degrees C. Tubercle 1951, 32:232-237.
49. Cox J.S., Shamu C.E., Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993, 73:1197-1206.
50. Crack J.C., Smith L.J., Stapleton M.R., Peck J., Watmough N.J., Buttner M.J., Buxton R.S., Green J., Oganesyan V.S., Thomson A.J., Le Brun N.E. Mechanistic insight into the nitrosylation of the [4Fe-4S] cluster of WhiB-like proteins. J. Am. Chem. Soc. 2010, 133:1112-1121.
51. Daniel J., Maamar H., Deb C., Sirakova T.D., Kolattukudy P.E. Mycobacterium tuberculosis uses host triacylglycerol to accumulate lipid droplets and acquires a dormancy-like phenotype in lipid-loaded macrophages. PLoS Pathog. 2011, 7:e1002093.
52. Deretic V., Philipp W., Dhandayuthapani S., Mudd M.H., Curcic R., Garbe T., Heym B., Via L.E., Cole S.T. Mycobacterium tuberculosis is a natural mutant with an inactivated oxidative-stress regulatory gene: implications for sensitivity to isoniazid. Mol. Microbiol. 1995, 17:889-900.
53. Diaz G.A., Wayne L.G. Isolation and characterization of catalase produced by Mycobacterium tuberculosis. Am. Rev. Respir. Dis. 1974, 110:312-319.
54. Dinauer M.C., Orkin S.H. Chronic granulomatous disease. Molecular genetics. Hematol. Oncol. Clin. North Am. 1988, 2:225-240.
55. Doi T., Ando M., Akaike T., Suga M., Sato K., Maeda H. Resistance to nitric oxide in Mycobacterium avium complex and its implication in pathogenesis. Infect. Immun. 1993, 61:1980-1989.
56. D'orazio M., Folcarelli S., Mariani F., Colizzi V., Rotilio G., Battistoni A. Lipid modification of the Cu, Zn superoxide dismutase from Mycobacterium tuberculosis. Biochem. J. 2001, 359:17-22.
57. Dosanjh N.S., Rawat M., Chung J.H., Av-Gay Y. Thiol specific oxidative stress response in Mycobacteria. FEMS Microbiol. Lett. 2005, 249:87-94.
58. Dussurget O., Stewart G., Neyrolles O., Pescher P., Young D., Marchal G. Role of Mycobacterium tuberculosis copper-zinc superoxide dismutase. Infect. Immun. 2001, 69:529-533.
59. Edwards K.M., Cynamon M.H., Voladri R.K., Hager C.C., Destefano M.S., Tham K.T., Lakey D.L., Bochan M.R., Kernodle D.S. Iron-cofactored superoxide dismutase inhibits host responses to Mycobacterium tuberculosis. Am. J. Respir. Crit. Care Med. 2001, 164:2213-2219.
60. Ellis H.R., Poole L.B. Roles for the two cysteine residues of AhpC in catalysis of peroxide reduction by alkyl hydroperoxide reductase from Salmonella typhimurium. Biochemistry 1997, 36:13349-13356.
61. Esterly J.R., Sturner W.Q., Esterly N.B., Windhorst D.B. Disseminated BCG in twin boys with presumed chronic granulomatous disease of childhood. Pediatrics 1971, 48:141-144.
62. Fang F.C., Degroote M.A., Foster J.W., Baumler A.J., Ochsner U., Testerman T., Bearson S., Giard J.C., Xu Y., Campbell G., Laessig T. Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:7502-7507.
63. Farhana A., Guidry L., Srivastava A., Singh A., Hondalus M.K., Steyn A.J. Reductive stress in microbes: implications for understanding Mycobacterium tuberculosis disease and persistence. Adv. Microb. Physiol. 2011, 57:43-117.
64. Fenhalls G., Stevens L., Moses L., Bezuidenhout J., Betts J.C., Helden Pv P., Lukey P.T., Duncan K. In situ detection of Mycobacterium tuberculosis transcripts in human lung granulomas reveals differential gene expression in necrotic lesions. Infect. Immun. 2002, 70:6330-6338.
65. Fernandes N.D., Wu Q.L., Kong D., Puyang X., Garg S., Husson R.N. A mycobacterial extracytoplasmic sigma factor involved in survival following heat shock and oxidative stress. J. Bacteriol. 1999, 181:4266-4274.
66. Firmani M.A., Riley L.W. Reactive nitrogen intermediates have a bacteriostatic effect on Mycobacterium tuberculosis in vitro. J. Clin. Microbiol. 2002, 40:3162-3166.
67. Flynn J.L., Scanga C.A., Tanaka K.E., Chan J. Effects of aminoguanidine on latent murine tuberculosis. J. Immunol. 1998, 160:1796-1803.
68. Fritz C., Maass S., Kreft A., Bange F.C. Dependence of Mycobacterium bovis BCG on anaerobic nitrate reductase for persistence is tissue specific. Infect. Immun. 2002, 70:286-291.
69. Gangadharam P.R., Pratt P.E. Susceptibility of Mycobacterium intracellulare to hydrogen peroxide. Am. Rev. Respir. Dis. 1984, 130:309-311.
70. Garg S.K., Suhail Alam M., Soni V., Radha Kishan K.V., Agrawal P. Characterization of Mycobacterium tuberculosis WhiB1/Rv3219 as a protein disulfide reductase. Protein Expr. Purif. 2007, 52:422-432.
71. Garg S., Alam M.S., Bajpai R., Kishan K.R., Agrawal P. Redox biology of Mycobacterium tuberculosis H37Rv: protein-protein interaction between GlgB and WhiB1 involves exchange of thiol-disulfide. BMC Biochem. 2009, 10:1.
72. Geiman D.E., Raghunand T.R., Agarwal N., Bishai W.R. Differential gene expression in response to exposure to antimycobacterial agents and other stress conditions among seven Mycobacterium tuberculosis whiB-like genes. Antimicrob. Agents Chemother. 2006, 50:2836-2841.
73. Gomes M.S., Florido M., Pais T.F., Appelberg R. Improved clearance of Mycobacterium avium upon disruption of the inducible nitric oxide synthase gene. J. Immunol. 1999, 162:6734-6739.
74. Gomez J.E., Bishai W.R. whmD is an essential mycobacterial gene required for proper septation and cell division. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:8554-8559.
75. Goodman M., Pedwaydon J., Czelusniak J., Suzuki T., Gotoh T., Moens L., Shishikura F., Walz D., Vinogradov S. An evolutionary tree for invertebrate globin sequences. J. Mol. Evol. 1988, 27:236-249.
76. Gopinathan K.P., Sirsi M., Ramakrishnan T. Nicotin-amide-adenine nucleotides of Mycobacterium tuberculosis H37Rv. Biochem. J. 1963, 87:444-448.
77. Goulding R., King M.B., Knox R., Robson J.M. Relation between in-vitro and in-vivo resistance to isoniazid. Lancet 1952, 2:69-70.
78. Graham J.E., Clark-Curtiss J.E. Identification of Mycobacterium tuberculosis RNAs synthesized in response to phagocytosis by human macrophages by selective capture of transcribed sequences (SCOTS). Proc. Natl. Acad. Sci. U. S. A. 1999, 96:11554-11559.
79. Green D.E. The reduction potentials of cysteine, glutathione and glycylcysteine. Biochem. J. 1933, 27:678-689.
80. Guimaraes B.G., Souchon H., Honore N., Saint-Joanis B., Brosch R., Shepard W., Cole S.T., Alzari P.M. Structure and mechanism of the alkyl hydroperoxidase AhpC, a key element of the Mycobacterium tuberculosis defense system against oxidative stress. J. Biol. Chem. 2005, 280:25735-25742.
81. Gupta R.K., Thakur T.S., Desiraju G.R., Tyagi J.S. Structure-based design of DevR inhibitor active against nonreplicating Mycobacterium tuberculosis. J. Med. Chem. 2009, 52:6324-6334.
82. Gutierrez-Lugo M.T., Baker H., Shiloach J., Boshoff H., Bewley C.A. Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening. J. Biomol. Screen. 2009, 14:643-652.
83. Hall G., Shah M., Mcewan P.A., Laughton C., Stevens M., Westwell A., Emsley J. Structure of Mycobacterium tuberculosis thioredoxin C. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:1453-1457.
84. Harth G., Horwitz M.A. Export of recombinant Mycobacterium tuberculosis superoxide dismutase is dependent upon both information in the protein and mycobacterial export machinery. A model for studying export of leaderless proteins by pathogenic mycobacteria. J. Biol. Chem. 1999, 274:4281-4292.
85. Heym B., Stavropoulos E., Honore N., Domenech P., Saint-Joanis B., Wilson T.M., Collins D.M., Colston M.J., Cole S.T. Effects of overexpression of the alkyl hydroperoxide reductase AhpC on the virulence and isoniazid resistance of Mycobacterium tuberculosis. Infect. Immun. 1997, 65:1395-1401.
86. Hillas P.J., Del Alba F.S., Oyarzabal J., Wilks A., Ortiz De Montellano P.R. The AhpC and AhpD antioxidant defense system of Mycobacterium tuberculosis. J. Biol. Chem. 2000, 275:18801-18809.
87. Honaker R.W., Leistikow R.L., Bartek I.L., Voskuil M.I. Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy. Infect. Immun. 2009, 77:3258-3263.
88. Honaker R.W., Dhiman R.K., Narayanasamy P., Crick D.C., Voskuil M.I. DosS responds to a reduced electron transport system to induce the Mycobacterium tuberculosis DosR regulon. J. Bacteriol. 2010, 192:6447-6455.
89. Hondalus M.K., Bardarov S., Russell R., Chan J., Jacobs W.R., Bloom B.R. Attenuation of and protection induced by a leucine auxotroph of Mycobacterium tuberculosis. Infect. Immun. 2000, 68:2888-2898.
90. Hugo M., Turell L., Manta B., Botti H., Monteiro G., Netto L.E., Alvarez B., Radi R., Trujillo M. Thiol and sulfenic acid oxidation of AhpE, the one-cysteine peroxiredoxin from Mycobacterium tuberculosis: kinetics, acidity constants, and conformational dynamics. Biochemistry 2009, 48:9416-9426.
91. Ioanoviciu A., Yukl E.T., Moenne-Loccoz P., De Montellano P.R. DevS, a heme-containing two-component oxygen sensor of Mycobacterium tuberculosis. Biochemistry 2007, 46:4250-4260.
92. Jackett P.S., Aber V.R., Lowrie D.B. Virulence of Mycobacterium tuberculosis and susceptibility to peroxidative killing systems. J. Gen. Microbiol. 1978, 107:273-278.
93. Jaeger T. Peroxiredoxin systems in mycobacteria. Subcell. Biochem. 2007, 44:207-217.
94. Jaeger T., Budde H., Flohe L., Menge U., Singh M., Trujillo M., Radi R. Multiple thioredoxin-mediated routes to detoxify hydroperoxides in Mycobacterium tuberculosis. Arch. Biochem. Biophys. 2004, 423:182-191.
95. Jakimowicz P., Cheesman M.R., Bishai W.R., Chater K.F., Thomson A.J., Buttner M.J. Evidence that the Streptomyces developmental protein WhiD, a member of the WhiB family, binds a [4Fe-4S] cluster. J. Biol. Chem. 2005, 280:8309-8315.
96. Jeong E.H., Son Y.M., Hah Y.S., Choi Y.J., Lee K.H., Song T., Kim D.R. RshA mimetic peptides inhibiting the transcription driven by a Mycobacterium tuberculosis sigma factor SigH. Biochem. Biophys. Res. Commun. 2006, 339:392-398.
97. Jia W., Cole J.A. Nitrate and nitrite transport in Escherichia coli. Biochem. Soc. Trans. 2005, 33:159-161.
98. Joseph P., Abdo M.R., Boigegrain R.A., Montero J.L., Winum J.Y., Kohler S. Targeting of the Brucella suis virulence factor histidinol dehydrogenase by histidinol analogues results in inhibition of intramacrophagic multiplication of the pathogen. Antimicrob. Agents Chemother. 2007, 51:3752-3755.
99. Jung Y.J., Lacourse R., Ryan L., North R.J. Virulent but not avirulent Mycobacterium tuberculosis can evade the growth inhibitory action of a T helper 1-dependent, nitric oxide Synthase 2-independent defense in mice. J. Exp. Med. 2002, 196:991-998.
100. Kadokura H., Katzen F., Beckwith J. Protein disulfide bond formation in prokaryotes. Annu. Rev. Biochem. 2003, 72:111-135.
101. Kalinina E.V., Chernov N.N., Saprin A.N. Involvement of thio-, peroxi-, and glutaredoxins in cellular redox-dependent processes. Biochemistry (Mosc.) 2008, 73:1493-1510.
102. Kang J.G., Paget M.S., Seok Y.J., Hahn M.Y., Bae J.B., Hahn J.S., Kleanthous C., Buttner M.J., Roe J.H. RsrA, an anti-sigma factor regulated by redox change. EMBO J. 1999, 18:4292-4298.
103. Karavolos M.H., Horsburgh M.J., Ingham E., Foster S.J. Role and regulation of the superoxide dismutases of Staphylococcus aureus. Microbiology 2003, 149:2749-2758.
104. Katoch V.M., Wayne L.G., Diaz G.A. Serological approaches for the characterization of catalase in tissue-derived mycobacteria. Ann. Microbiol. (Paris) 1982, 133:407-414.
105. Kaushal D., Schroeder B.G., Tyagi S., Yoshimatsu T., Scott C., Ko C., Carpenter L., Mehrotra J., Manabe Y.C., Fleischmann R.D., Bishai W.R. Reduced immunopathology and mortality despite tissue persistence in a Mycobacterium tuberculosis mutant lacking alternative sigma factor, SigH. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:8330-8335.
106. Kinger A.K., Tyagi J.S. Identification and cloning of genes differentially expressed in the virulent strain of Mycobacterium tuberculosis. Gene 1993, 131:113-117.
107. Klebanoff S.J. Myeloperoxidase-halide-hydrogen peroxide antibacterial system. J. Bacteriol. 1968, 95:2131-2138.
108. Klebanoff S.J., Shepard C.C. Toxic effect of the peroxidase-hydrogen peroxide-halide antimicrobial system on Mycobacterium leprae. Infect. Immun. 1984, 44:534-536.
109. Kohanski M.A., Dwyer D.J., Hayete B., Lawrence C.A., Collins J.J. A common mechanism of cellular death induced by bactericidal antibiotics. Cell 2007, 130:797-810.
110. Koledin T., Newton G.L., Fahey R.C. Identification of the mycothiol synthase gene (mshD) encoding the acetyltransferase producing mycothiol in actinomycetes. Arch. Microbiol. 2002, 178:331-337.
111. Koul A., Vranckx L., Dendouga N., Balemans W., Van Den Wyngaert I., Vergauwen K., Gohlmann H.W., Willebrords R., Poncelet A., Guillemont J., Bald D., Andries K. Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008, 283:25273-25280.
112. Kumar A., Toledo J.C., Patel R.P., Lancaster J.R., Steyn A.J. Mycobacterium tuberculosis DosS is a redox sensor and DosT is a hypoxia sensor. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:11568-11573.
113. Kumar A., Deshane J.S., Crossman D.K., Bolisetty S., Yan B.S., Kramnik I., Agarwal A., Steyn A.J. Heme oxygenase-1-derived carbon monoxide induces the Mycobacterium tuberculosis dormancy regulon. J. Biol. Chem. 2008, 283:18032-18039.
114. Laurent T.C., Moore E.C., Reichard P. Enzymatic synthesis of deoxyribonucleotides. IV. Isolation and characterization of thioredoxin, the hydrogen donor from Escherichia coli B. J. Biol. Chem. 1964, 239:3436-3444.
115. Leistikow R.L., Morton R.A., Bartek I.L., Frimpong I., Wagner K., Voskuil M.I. The Mycobacterium tuberculosis DosR regulon assists in metabolic homeostasis and enables rapid recovery from nonrespiring dormancy. J. Bacteriol. 2010, 192:1662-1670.
116. Leyten E.M., Lin M.Y., Franken K.L., Friggen A.H., Prins C., Van Meijgaarden K.E., Voskuil M.I., Weldingh K., Andersen P., Schoolnik G.K., Arend S.M., Ottenhoff T.H., et al. Human T-cell responses to 25 novel antigens encoded by genes of the dormancy regulon of Mycobacterium tuberculosis. Microbes Infect. 2006, 8:2052-2060.
117. Li Z., Kelley C., Collins F., Rouse D., Morris S. Expression of katG in Mycobacterium tuberculosis is associated with its growth and persistence in mice and guinea pigs. J. Infect. Dis. 1998, 177:1030-1035.
118. Li S., Peterson N.A., Kim M.Y., Kim C.Y., Hung L.W., Yu M., Lekin T., Segelke B.W., Lott J.S., Baker E.N. Crystal structure of AhpE from Mycobacterium tuberculosis, a 1-Cys peroxiredoxin. J. Mol. Biol. 2005, 346:1035-1046.
119. Li A.H., Lam W.L., Stokes R.W. Characterization of genes differentially expressed within macrophages by virulent and attenuated Mycobacterium tuberculosis identifies candidate genes involved in intracellular growth. Microbiology 2008, 154:2291-2303.
120. Liu K., Yu J., Russell D.G. pckA-deficient Mycobacterium bovis BCG shows attenuated virulence in mice and in macrophages. Microbiology 2003, 149:1829-1835.
121. Long R., Light B., Talbot J.A. Mycobacteriocidal action of exogenous nitric oxide. Antimicrob. Agents Chemother. 1999, 43:403-405.
122. Long R., Jones R., Talbot J., Mayers I., Barrie J., Hoskinson M., Light B. Inhaled nitric oxide treatment of patients with pulmonary tuberculosis evidenced by positive sputum smears. Antimicrob. Agents Chemother. 2005, 49:1209-1212.
123. Lynch M., Kuramitsu H. Expression and role of superoxide dismutases (SOD) in pathogenic bacteria. Microbes Infect. 2000, 2:1245-1255.
124. Macmicking J.D., North R.J., Lacourse R., Mudgett J.S., Shah S.K., Nathan C.F. Identification of nitric oxide synthase as a protective locus against tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 1997, 94:5243-5248.
125. Manca C., Paul S., Barry C.E., Freedman V.H., Kaplan G. Mycobacterium tuberculosis catalase and peroxidase activities and resistance to oxidative killing in human monocytes in vitro. Infect. Immun. 1999, 67:74-79.
126. Manganelli R., Voskuil M.I., Schoolnik G.K., Dubnau E., Gomez M., Smith I. Role of the extracytoplasmic-function sigma factor sigma(H) in Mycobacterium tuberculosis global gene expression. Mol. Microbiol. 2002, 45:365-374.
127. Marklund B.I., Mahenthiralingam E., Stokes R.W. Site-directed mutagenesis and virulence assessment of the katG gene of Mycobacterium intracellulare. Mol. Microbiol. 1998, 29:999-1008.
128. Marrero J., Rhee K.Y., Schnappinger D., Pethe K., Ehrt S. Gluconeogenic carbon flow of tricarboxylic acid cycle intermediates is critical for Mycobacterium tuberculosis to establish and maintain infection. Proc. Natl. Acad. Sci. U. S. A. 2010, 107:9819-9824.
129. Martin J.L. Thioredoxin-a fold for all reasons. Structure 1995, 3:245-250.
130. Marttila H.J., Soini H., Huovinen P., Viljanen M.K. katG mutations in isoniazid-resistant Mycobacterium tuberculosis isolates recovered from Finnish patients. Antimicrob. Agents Chemother. 1996, 40:2187-2189.
131. Master S., Zahrt T.C., Song J., Deretic V. Mapping of Mycobacterium tuberculosis katG promoters and their differential expression in infected macrophages. J. Bacteriol. 2001, 183:4033-4039.
132. Master S.S., Springer B., Sander P., Boettger E.C., Deretic V., Timmins G.S. Oxidative stress response genes in Mycobacterium tuberculosis: role of ahpC in resistance to peroxynitrite and stage-specific survival in macrophages. Microbiology 2002, 148:3139-3144.
133. Mckinney J.D., Honer Zu Bentrup K., Munoz-Elias E.J., Miczak A., Chen B., Chan W.T., Swenson D., Sacchettini J.C., Jacobs W.R., Russell D.G. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 2000, 406:735-738.
134. Middlebrook G., Cohn M.L. Some observations on the pathogenicity of isoniazid-resistant variants of tubercle bacilli. Science 1953, 118:297-299.
135. Mitchison D.A., Selkon J.B., Lloyd J. Virulence in the guinea-pig, susceptibility to hydrogen peroxide, and catalase activity of isoniazid-sensitive tubercle bacilli from South Indian and British patients. J. Pathol. Bacteriol. 1963, 86:377-386.
136. Moens L., Vanfleteren J., Van De Peer Y., Peeters K., Kapp O., Czeluzniak J., Goodman M., Blaxter M., Vinogradov S. Globins in nonvertebrate species: dispersal by horizontal gene transfer and evolution of the structure-function relationships. Mol. Biol. Evol. 1996, 13:324-333.
137. Morris R.P., Nguyen L., Gatfield J., Visconti K., Nguyen K., Schnappinger D., Ehrt S., Liu Y., Heifets L., Pieters J., Schoolnik G., Thompson C.J. Ancestral antibiotic resistance in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:12200-12205.
138. Morse W.C., Weiser O.L., Kuhns D.M., Fusillo M., Dail M.C., Evans J.R. Study of the virulence of isoniazid-resistant tubercle bacilli in guinea pigs and mice: a preliminary report. Am. Rev. Tuberc. 1954, 69:464-468.
139. Munoz-Elias E.J., Mckinney J.D. Mycobacterium tuberculosis isocitrate lyases 1 and 2 are jointly required for in vivo growth and virulence. Nat. Med. 2005, 11:638-644.
140. Munoz-Elias E.J., Upton A.M., Cherian J., Mckinney J.D. Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence. Mol. Microbiol. 2006, 60:1109-1122.
141. Nathan C. Mechanisms and modulation of macrophage activation. Behring Inst. Mitt. 1991, 200-207.
142. Nathan C., Shiloh M.U. Reactive oxygen and nitrogen intermediates in the relationship between mammalian hosts and microbial pathogens. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:8841-8848.
143. Newton G.L., Bewley C.A., Dwyer T.J., Horn R., Aharonowitz Y., Cohen G., Davies J., Faulkner D.J., Fahey R.C. The structure of U17 isolated from Streptomyces clavuligerus and its properties as an antioxidant thiol. Eur. J. Biochem. 1995, 230:821-825.
144. Newton G.L., Arnold K., Price M.S., Sherrill C., Delcardayre S.B., Aharonowitz Y., Cohen G., Davies J., Fahey R.C., Davis C. Distribution of thiols in microorganisms: mycothiol is a major thiol in most actinomycetes. J. Bacteriol. 1996, 178:1990-1995.
145. Newton G.L., Ta P., Fahey R.C. A mycothiol synthase mutant of Mycobacterium smegmatis produces novel thiols and has an altered thiol redox status. J. Bacteriol. 2005, 187:7309-7316.
146. Newton G.L., Buchmeier N., La Clair J.J., Fahey R.C. Evaluation of NTF1836 as an inhibitor of the mycothiol biosynthetic enzyme MshC in growing and non-replicating Mycobacterium tuberculosis. Bioorg. Med. Chem. 2011, 19:3956-3964.
147. Neyrolles O., Hernandez-Pando R., Pietri-Rouxel F., Fornes P., Tailleux L., Barrios Payan J.A., Pivert E., Bordat Y., Aguilar D., Prevost M.C., Petit C., Gicquel B. Is adipose tissue a place for Mycobacterium tuberculosis persistence?. PLoS One 2006, 1:e43.
148. Nguyen M., Claparols C., Bernadou J., Meunier B. A fast and efficient metal-mediated oxidation of isoniazid and identification of isoniazid-NAD(H) adducts. Chembiochem 2001, 2:877-883.
149. Nicholson S., Bonecini-Almeida Mda G., Lapa E., Silva J.R., Nathan C., Xie Q.W., Mumford R., Weidner J.R., Calaycay J., Geng J., Boechat N., Linhares C., et al. Inducible nitric oxide synthase in pulmonary alveolar macrophages from patients with tuberculosis. J. Exp. Med. 1996, 183:2293-2302.
150. Ohga S., Ikeuchi K., Kadoya R., Okada K., Miyazaki C., Suita S., Ueda K. Intrapulmonary Mycobacterium avium infection as the first manifestation of chronic granulomatous disease. J. Infect. 1997, 34:147-150.
151. Ordonez E., Van Belle K., Roos G., De Galan S., Letek M., Gil J.A., Wyns L., Mateos L.M., Messens J. Arsenate reductase, mycothiol, and mycoredoxin concert thiol/disulfide exchange. J. Biol. Chem. 2009, 284:15107-15116.
152. Ouellet H., Ranguelova K., Labarre M., Wittenberg J.B., Wittenberg B.A., Magliozzo R.S., Guertin M. Reaction of Mycobacterium tuberculosis truncated hemoglobin O with hydrogen peroxide: evidence for peroxidatic activity and formation of protein-based radicals. J. Biol. Chem. 2007, 282:7491-7503.
153. Pagan-Ramos E., Master S.S., Pritchett C.L., Reimschuessel R., Trucksis M., Timmins G.S., Deretic V. Molecular and physiological effects of mycobacterial oxyR inactivation. J. Bacteriol. 2006, 188:2674-2680.
154. Paget M.S., Buttner M.J. Thiol-based regulatory switches. Annu. Rev. Genet. 2003, 37:91-121.
155. Paget M.S., Kang J.G., Roe J.H., Buttner M.J. sigmaR, an RNA polymerase sigma factor that modulates expression of the thioredoxin system in response to oxidative stress in Streptomyces coelicolor A3(2). EMBO J. 1998, 17:5776-5782.
156. Paget M.S., Molle V., Cohen G., Aharonowitz Y., Buttner M.J. Defining the disulphide stress response in Streptomyces coelicolor A3(2): identification of the sigmaR regulon. Mol. Microbiol. 2001, 42:1007-1020.
157. Pal P.G., Horwitz M.A. Immunization with extracellular proteins of Mycobacterium tuberculosis induces cell-mediated immune responses and substantial protective immunity in a guinea pig model of pulmonary tuberculosis. Infect. Immun. 1992, 60:4781-4792.
158. Pandey A.K., Sassetti C.M. Mycobacterial persistence requires the utilization of host cholesterol. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:4376-4380.
159. Park J.H., Roe J.H. Mycothiol regulates and is regulated by a thiol-specific antisigma factor RsrA and sigma(R) in Streptomyces coelicolor. Mol. Microbiol. 2008, 68:861-870.
160. Park S.T., Kang C.M., Husson R.N. Regulation of the SigH stress response regulon by an essential protein kinase in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:13105-13110.
161. Patel M.P., Blanchard J.S. Expression, purification, and characterization of Mycobacterium tuberculosis mycothione reductase. Biochemistry 1999, 38:11827-11833.
162. Pathania R., Navani N.K., Gardner A.M., Gardner P.R., Dikshit K.L. Nitric oxide scavenging and detoxification by the Mycobacterium tuberculosis haemoglobin, HbN in Escherichia coli. Mol. Microbiol. 2002, 45:1303-1314.
163. Pathania R., Navani N.K., Rajamohan G., Dikshit K.L. Mycobacterium tuberculosis hemoglobin HbO associates with membranes and stimulates cellular respiration of recombinant Escherichia coli. J. Biol. Chem. 2002, 277:15293-15302.
164. Pawaria S., Lama A., Raje M., Dikshit K.L. Responses of Mycobacterium tuberculosis hemoglobin promoters to in vitro and in vivo growth conditions. Appl. Environ. Microbiol. 2008, 74:3512-3522.
165. Peng H.P., Chan C.S., Shih M.C., Yang S.F. Signaling events in the hypoxic induction of alcohol dehydrogenase gene in Arabidopsis. Plant Physiol. 2001, 126:742-749.
166. Piddington D.L., Fang F.C., Laessig T., Cooper A.M., Orme I.M., Buchmeier N.A. Cu, Zn superoxide dismutase of Mycobacterium tuberculosis contributes to survival in activated macrophages that are generating an oxidative burst. Infect. Immun. 2001, 69:4980-4987.
167. Pym A.S., Domenech P., Honore N., Song J., Deretic V., Cole S.T. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol. Microbiol. 2001, 40:879-889.
168. Pym A.S., Saint-Joanis B., Cole S.T. Effect of katG mutations on the virulence of Mycobacterium tuberculosis and the implication for transmission in humans. Infect. Immun. 2002, 70:4955-4960.
169. Raghunand T.R., Bishai W.R. Mycobacterium smegmatis whmD and its homologue Mycobacterium tuberculosis whiB2 are functionally equivalent. Microbiology 2006, 152:2735-2747.
170. Raman S., Song T., Puyang X., Bardarov S., Jacobs W.R., Husson R.N. The alternative sigma factor SigH regulates major components of oxidative and heat stress responses in Mycobacterium tuberculosis. J. Bacteriol. 2001, 183:6119-6125.
171. Rao S.P., Alonso S., Rand L., Dick T., Pethe K. The protonmotive force is required for maintaining ATP homeostasis and viability of hypoxic, nonreplicating Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:11945-11950.
172. Rawat M., Newton G.L., Ko M., Martinez G.J., Fahey R.C., Av-Gay Y. Mycothiol-deficient Mycobacterium smegmatis mutants are hypersensitive to alkylating agents, free radicals, and antibiotics. Antimicrob. Agents Chemother. 2002, 46:3348-3355.
173. Raynaud C., Guilhot C., Rauzier J., Bordat Y., Pelicic V., Manganelli R., Smith I., Gicquel B., Jackson M. Phospholipases C are involved in the virulence of Mycobacterium tuberculosis. Mol. Microbiol. 2002, 45:203-217.
174. Reed M.B., Gagneux S., Deriemer K., Small P.M., Barry C.E. The W-Beijing lineage of Mycobacterium tuberculosis overproduces triglycerides and has the DosR dormancy regulon constitutively upregulated. J. Bacteriol. 2007, 189:2583-2589.
175. Resch S.C., Salomon J.A., Murray M., Weinstein M.C. Cost-effectiveness of treating multidrug-resistant tuberculosis. PLoS Med. 2006, 3:e241.
176. Rhee S.G., Kang S.W., Chang T.S., Jeong W., Kim K. Peroxiredoxin, a novel family of peroxidases. IUBMB Life 2001, 52:35-41.
177. Rhee S.G., Chae H.Z., Kim K. Peroxiredoxins: a historical overview and speculative preview of novel mechanisms and emerging concepts in cell signaling. Free Radic. Biol. Med. 2005, 38:1543-1552.
178. Rich E.A., Torres M., Sada E., Finegan C.K., Hamilton B.D., Toossi Z. Mycobacterium tuberculosis (MTB)-stimulated production of nitric oxide by human alveolar macrophages and relationship of nitric oxide production to growth inhibition of MTB. Tuber. Lung Dis. 1997, 78:247-255.
179. Richardson A.R., Libby S.J., Fang F.C. A nitric oxide-inducible lactate dehydrogenase enables Staphylococcus aureus to resist innate immunity. Science 2008, 319:1672-1676.
180. Roberts D.M., Liao R.P., Wisedchaisri G., Hol W.G., Sherman D.R. Two sensor kinases contribute to the hypoxic response of Mycobacterium tuberculosis. J. Biol. Chem. 2004, 279:23082-23087.
181. 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.
182. Rohde K.H., Abramovitch R.B., Russell D.G. Mycobacterium tuberculosis invasion of macrophages: linking bacterial gene expression to environmental cues. Cell Host Microbe 2007, 2:352-364.
183. Roy S., Sharma S., Sharma M., Aggarwal R., Bose M. Induction of nitric oxide release from the human alveolar epithelial cell line A549: an in vitro correlate of innate immune response to Mycobacterium tuberculosis. Immunology 2004, 112:471-480.
184. Rustad T.R., Harrell M.I., Liao R., Sherman D.R. The enduring hypoxic response of Mycobacterium tuberculosis. PLoS One 2008, 3:e1502.
185. Saini D.K., Malhotra V., Tyagi J.S. Cross talk between DevS sensor kinase homologue, Rv2027c, and DevR response regulator of Mycobacterium tuberculosis. FEBS Lett. 2004, 565:75-80.
186. Sambandamurthy V.K., Wang X., Chen B., Russell R.G., Derrick S., Collins F.M., Morris S.L., Jacobs W.R. A pantothenate auxotroph of Mycobacterium tuberculosis is highly attenuated and protects mice against tuberculosis. Nat. Med. 2002, 8:1171-1174.
187. Sardiwal S., Kendall S.L., Movahedzadeh F., Rison S.C., Stoker N.G., Djordjevic S. A GAF domain in the hypoxia/NO-inducible Mycobacterium tuberculosis DosS protein binds haem. J Mol Biol 2005, 353:929-936.
188. Sassetti C.M., Boyd D.H., Rubin E.J. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003, 48:77-84.
189. Savvi S., Warner D.F., Kana B.D., Mckinney J.D., Mizrahi V., Dawes S.S. Functional characterization of a vitamin B12-dependent methylmalonyl pathway in Mycobacterium tuberculosis: implications for propionate metabolism during growth on fatty acids. J. Bacteriol. 2008, 190:3886-3895.
190. Scanga C.A., Mohan V.P., Tanaka K., Alland D., Flynn J.L., Chan J. The inducible nitric oxide synthase locus confers protection against aerogenic challenge of both clinical and laboratory strains of Mycobacterium tuberculosis in mice. Infect. Immun. 2001, 69:7711-7717.
191. Schafer F.Q., Buettner G.R. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic. Biol. Med. 2001, 30:1191-1212.
192. Schnappinger D., Ehrt S., Voskuil M.I., Liu Y., Mangan J.A., Monahan I.M., Dolganov G., Efron B., Butcher P.D., Nathan C., Schoolnik G.K. Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J. Exp. Med. 2003, 198:693-704.
193. Seebeck F.P. In vitro reconstitution of Mycobacterial ergothioneine biosynthesis. J. Am. Chem. Soc. 2010, 132:6632-6633.
194. Segal A.W. Cytochrome b-245 and its involvement in the molecular pathology of chronic granulomatous disease. Hematol. Oncol. Clin. North Am. 1988, 2:213-223.
195. Sherman D.R., Mdluli K., Hickey M.J., Arain T.M., Morris S.L., Barry C.E., Stover C.K. Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 1996, 272:1641-1643.
196. Sherman D.R., Mdluli K., Hickey M.J., Barry C.E., Stover C.K. AhpC, oxidative stress and drug resistance in Mycobacterium tuberculosis. Biofactors 1999, 10:211-217.
197. Sherman D.R., Voskuil M., Schnappinger D., Liao R., Harrell M.I., Schoolnik G.K. Regulation of the Mycobacterium tuberculosis hypoxic response gene encoding alpha -crystallin. Proc. Natl. Acad. Sci. U. S. A. 2001, 98:7534-7539.
198. Shi S., Ehrt S. Dihydrolipoamide acyltransferase is critical for Mycobacterium tuberculosis pathogenesis. Infect. Immun. 2006, 74:56-63.
199. Shi L., Sohaskey C.D., Kana B.D., Dawes S., North R.J., Mizrahi V., Gennaro M.L. Changes in energy metabolism of Mycobacterium tuberculosis in mouse lung and under in vitro conditions affecting aerobic respiration. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:15629-15634.
200. Shiloh M.U., Nathan C.F. Reactive nitrogen intermediates and the pathogenesis of Salmonella and mycobacteria. Curr. Opin. Microbiol. 2000, 3:35-42.
201. Shiloh M.U., Manzanillo P., Cox J.S. Mycobacterium tuberculosis senses host-derived carbon monoxide during macrophage infection. Cell Host Microbe 2008, 3:323-330.
202. Singh A., Guidry L., Narasimhulu K.V., Mai D., Trombley J., Redding K.E., Giles G.I., Lancaster J.R., Steyn A.J. Mycobacterium tuberculosis WhiB3 responds to O2 and nitric oxide via its [4Fe-4S] cluster and is essential for nutrient starvation survival. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:11562-11567.
203. Singh A., Crossman D.K., Mai D., Guidry L., Voskuil M.I., Renfrow M.B., Steyn A.J. Mycobacterium tuberculosis WhiB3 maintains redox homeostasis by regulating virulence lipid anabolism to modulate macrophage response. PLoS Pathog. 2009, 5:e1000545.
204. Slayden R.A., Barry C.E. The genetics and biochemistry of isoniazid resistance in mycobacterium tuberculosis. Microbes Infect. 2000, 2:659-669.
205. Sohaskey C.D. Nitrate enhances the survival of Mycobacterium tuberculosis during inhibition of respiration. J. Bacteriol. 2008, 190:2981-2986.
206. Sohaskey C.D., Wayne L.G. Role of narK2X and narGHJI in hypoxic upregulation of nitrate reduction by Mycobacterium tuberculosis. J. Bacteriol. 2003, 185:7247-7256.
207. Soliveri J., Vijgenboom E., Granozzi C., Plaskitt K.A., Chater K.F. Functional and evolutionary implications of a survey of various actinomycetes for homologues of two Streptomyces coelicolor sporulation genes. J. Gen. Microbiol. 1993, 139:2569-2578.
208. Soliveri J.A., Gomez J., Bishai W.R., Chater K.F. Multiple paralogous genes related to the Streptomyces coelicolor developmental regulatory gene whiB are present in Streptomyces and other actinomycetes. Microbiology 2000, 146(Pt 2):333-343.
209. Song T., Dove S.L., Lee K.H., Husson R.N. RshA, an anti-sigma factor that regulates the activity of the mycobacterial stress response sigma factor SigH. Mol. Microbiol. 2003, 50:949-959.
210. Sousa E.H., Tuckerman J.R., Gonzalez G., Gilles-Gonzalez M.A. DosT and DevS are oxygen-switched kinases in Mycobacterium tuberculosis. Protein Sci. 2007, 16:1708-1719.
211. Spagnolo L., Toro I., D'orazio M., O'neill P., Pedersen J.Z., Carugo O., Rotilio G., Battistoni A., Djinovic-Carugo K. Unique features of the sodC-encoded superoxide dismutase from Mycobacterium tuberculosis, a fully functional copper-containing enzyme lacking zinc in the active site. J. Biol. Chem. 2004, 279:33447-33455.
212. Spalding M.D., Prigge S.T. Lipoic acid metabolism in microbial pathogens. Microbiol. Mol. Biol. Rev. 2010, 74:200-228.
213. Springer B., Master S., Sander P., Zahrt T., Mcfalone M., Song J., Papavinasasundaram K.G., Colston M.J., Boettger E., Deretic V. Silencing of oxidative stress response in Mycobacterium tuberculosis: expression patterns of ahpC in virulent and avirulent strains and effect of ahpC inactivation. Infect. Immun. 2001, 69:5967-5973.
214. Stehr M., Hecht H.J., Jager T., Flohe L., Singh M. Structure of the inactive variant C60S of Mycobacterium tuberculosis thiol peroxidase. Acta Crystallogr. D Biol. Crystallogr. 2006, 62:563-567.
215. Stewart V. Nitrate regulation of anaerobic respiratory gene expression in Escherichia coli. Mol. Microbiol. 1993, 9:425-434.
216. Steyn A.J., Collins D.M., Hondalus M.K., Jacobs W.R., Kawakami R.P., Bloom B.R. Mycobacterium tuberculosis WhiB3 interacts with RpoV to affect host survival but is dispensable for in vivo growth. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:3147-3152.
217. Storz G., Tartaglia L.A., Ames B.N. The OxyR regulon. Antonie Van Leeuwenhoek 1990, 58:157-161.
218. Ta P., Buchmeier N., Newton G.L., Rawat M., Fahey R.C. Organic hydroperoxide resistance protein and ergothioneine compensate for loss of mycothiol in Mycobacterium smegmatis mutants. J. Bacteriol. 2011, 193:1981-1990.
219. Tan M.P., Sequeira P., Lin W.W., Phong W.Y., Cliff P., Ng S.H., Lee B.H., Camacho L., Schnappinger D., Ehrt S., Dick T., Pethe K., et al. Nitrate respiration protects hypoxic Mycobacterium tuberculosis against acid- and reactive nitrogen species stresses. PLoS One 2010, 5:e13356.
220. Tian J., Bryk R., Itoh M., Suematsu M., Nathan C. Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:10670-10675.
221. Tian J., Bryk R., Shi S., Erdjument-Bromage H., Tempst P., Nathan C. Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes. Mol. Microbiol. 2005, 57:859-868.
222. Trujillo M., Mauri P., Benazzi L., Comini M., De Palma A., Flohe L., Radi R., Stehr M., Singh M., Ursini F., Jaeger T. The mycobacterial thioredoxin peroxidase can act as a one-cysteine peroxiredoxin. J. Biol. Chem. 2006, 281:20555-20566.
223. Tsai M.C., Chakravarty S., Zhu G., Xu J., Tanaka K., Koch C., Tufariello J., Flynn J., Chan J. Characterization of the tuberculous granuloma in murine and human lungs: cellular composition and relative tissue oxygen tension. Cell. Microbiol. 2006, 8:218-232.
224. Ung K.S., Av-Gay Y. Mycothiol-dependent mycobacterial response to oxidative stress. FEBS Lett. 2006, 580:2712-2716.
225. Unson M.D., Newton G.L., Arnold K.F., Davis C.E., Fahey R.C. Improved methods for immunoassay of mycothiol. J. Clin. Microbiol. 1999, 37:2153-2157.
226. Venugopal A., Bryk R., Shi S., Rhee K., Rath P., Schnappinger D., Ehrt S., Nathan C. Virulence of Mycobacterium tuberculosis depends on lipoamide dehydrogenase, a member of three multienzyme complexes. Cell Host Microbe 2011, 9:21-31.
227. Via L.E., Lin P.L., Ray S.M., Carrillo J., Allen S.S., Eum S.Y., Taylor K., Klein E., Manjunatha U., Gonzales J., Lee E.G., Park S.K., et al. Tuberculous granulomas are hypoxic in guinea pigs, rabbits, and nonhuman primates. Infect. Immun. 2008, 76:2333-2340.
228. Vilcheze C., Weisbrod T.R., Chen B., Kremer L., Hazbon M.H., Wang F., Alland D., Sacchettini J.C., Jacobs W.R. Altered NADH/NAD+ ratio mediates coresistance to isoniazid and ethionamide in mycobacteria. Antimicrob. Agents Chemother. 2005, 49:708-720.
229. Vilcheze C., Av-Gay Y., Barnes S.W., Larsen M.H., Walker J.R., Glynne R.J., Jacobs W.R. Coresistance to isoniazid and ethionamide maps to mycothiol biosynthetic genes in Mycobacterium bovis. Antimicrob. Agents Chemother. 2011, 55:4422-4423.
230. Visca P., Fabozzi G., Petrucca A., Ciaccio C., Coletta M., De Sanctis G., Bolognesi M., Milani M., Ascenzi P. The truncated hemoglobin from Mycobacterium leprae. Biochem. Biophys. Res. Commun. 2002, 294:1064-1070.
231. Voskuil M.I., Schnappinger D., Visconti K.C., Harrell M.I., Dolganov G.M., Sherman D.R., Schoolnik G.K. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J. Exp. Med. 2003, 198:705-713.
232. Voskuil M.I., Visconti K.C., Schoolnik G.K. Mycobacterium tuberculosis gene expression during adaptation to stationary phase and low-oxygen dormancy. Tuberculosis (Edinb.) 2004, 84:218-227.
233. Walker L., Lowrie D.B. Killing of Mycobacterium microti by immunologically activated macrophages. Nature 1981, 293:69-71.
234. Wang C.H., Liu C.Y., Lin H.C., Yu C.T., Chung K.F., Kuo H.P. Increased exhaled nitric oxide in active pulmonary tuberculosis due to inducible NO synthase upregulation in alveolar macrophages. Eur. Respir. J. 1998, 11:809-815.
235. Watanabe S., Zimmermann M., Goodwin M.B., Sauer U., Barry C.E., Boshoff H.I. Fumarate reductase activity maintains an energized membrane in anaerobic Mycobacterium tuberculosis. PLoS Pathog. 2011, 7:e1002287.
236. Wayne L.G., Hayes L.G. An in vitro model for sequential study of shiftdown of Mycobacterium tuberculosis through two stages of nonreplicating persistence. Infect. Immun. 1996, 64:2062-2069.
237. Wayne L.G., Lin K.Y. Glyoxylate metabolism and adaptation of Mycobacterium tuberculosis to survival under anaerobic conditions. Infect. Immun. 1982, 37:1042-1049.
238. Wengenack N.L., Jensen M.P., Rusnak F., Stern M.K. Mycobacterium tuberculosis KatG is a peroxynitritase. Biochem. Biophys. Res. Commun. 1999, 256:485-487.
239. WHO global burden of disease: 2004 update. World Health Organization Update 2008, WHO.
240. Global tuberculosis control: 2010 report. World Health Organization Update 2010, WHO.
241. Wieles B., Nagai S., Wiker H.G., Harboe M., Ottenhoff T.H. Identification and functional characterization of thioredoxin of Mycobacterium tuberculosis. Infect. Immun. 1995, 63:4946-4948.
242. Wieles B., Ottenhoff T.H., Steenwijk T.M., Franken K.L., De Vries R.R., Langermans J.A. Increased intracellular survival of Mycobacterium smegmatis containing the Mycobacterium leprae thioredoxin-thioredoxin reductase gene. Infect. Immun. 1997, 65:2537-2541.
243. Wilkin J.M., Soetaert K., Stelandre M., Buyssens P., Castillo G., Demoulin V., Bottu G., Laneelle M.A., Daffe M., De Bruyn J. Overexpression, purification and characterization of Mycobacterium bovis BCG alcohol dehydrogenase. Eur. J. Biochem. 1999, 262:299-307.
244. Williams C.H. Mechanism and structure of thioredoxin reductase from Escherichia coli. FASEB J. 1995, 9:1267-1276.
245. Wilson T.M., Collins D.M. ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex. Mol. Microbiol. 1996, 19:1025-1034.
246. Wu C.H., Tsai-Wu J.J., Huang Y.T., Lin C.Y., Lioua G.G., Lee F.J. Identification and subcellular localization of a novel Cu, Zn superoxide dismutase of Mycobacterium tuberculosis. FEBS Lett. 1998, 439:192-196.
247. Xu X., Vilcheze C., Av-Gay Y., Gomez-Velasco A., Jacobs W.R. Precise null deletion mutations of the mycothiol synthesis genes reveal their role in isoniazid and ethionamide resistance in Mycobacterium smegmatis. Antimicrob. Agents Chemother. 2011, 55:3133-3139.
248. Yesilkaya H., Spissu F., Carvalho S.M., Terra V.S., Homer K.A., Benisty R., Porat N., Neves A.R., Andrew P.W. Pyruvate formate lyase is required for pneumococcal fermentative metabolism and virulence. Infect. Immun. 2009, 77:5418-5427.
249. Zahrt T.C., Song J., Siple J., Deretic V. Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG. Mol. Microbiol. 2001, 39:1174-1185.
250. 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.
251. 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.
252. Zhang Z., Hillas P.J., Ortiz De Montellano P.R. Reduction of peroxides and dinitrobenzenes by Mycobacterium tuberculosis thioredoxin and thioredoxin reductase. Arch. Biochem. Biophys. 1999, 363:19-26.