Novel targets in M. tuberculosis: Search for new drugs

Trends in Molecular Medicine

Volumn 17, Issue 1, 2011, Pages 25-33

  Lamichhane, Gyanu ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1 (6 BROMO 2 METHOXY 3 QUINOLINYL) 4 DIMETHYLAMINO 2 (1 NAPHTHYL) 1 PHENYL 2 BUTANOL; ADENOSINE TRIPHOSPHATE PHOSPHORIBOSYL TRANSFERASE; ANTIMYCOBACTERIAL AGENT; DECAPRENYLPHOSPHORYL BETA DEXTRO RIBOSE 2' EPIMERASE; DOSR; GAMMA GLUTAMYLTRANSFERASE; GLYCOSYLTRANSFERASE; ISOCITRATE LYASE; LEVO DEXTRO TRANSPEPTIDASE; LIGASE; MALTOSYLTRANSFERASE GLGE; METHIONYL AMINOPEPTIDASE; MYCOLIC ACID; MYCOTHIOL LIGASE; PEPTIDE DEFORMYLASE INHIBITOR; PHOSPHORIBOSYLTRANSFERASE; PROTEASOME; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; STREPTOMYCIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; TUBERCULOSTATIC AGENT;

BACTERIAL CELL WALL; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL VIRULENCE; CARD GENE; CELL METABOLISM; CELL RESPIRATION; CYCLOPROPANATION; DORMANCY; DRUG EFFICACY; ENERGY METABOLISM; GENE DELETION; GENETIC IDENTIFICATION; GROWTH INHIBITION; IN VITRO STUDY; LATENT TUBERCULOSIS; MINIMUM INHIBITORY CONCENTRATION; MOLECULARLY TARGETED THERAPY; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PROTEIN PROCESSING; REVIEW; TUBERCULOSIS; ANIMAL; ANTAGONISTS AND INHIBITORS; DRUG DESIGN; DRUG EFFECTS; GENETICS; HUMAN; METABOLISM; MICROBIOLOGY;

MYCOBACTERIUM TUBERCULOSIS;

ANIMALS; ANTITUBERCULAR AGENTS; BACTERIAL PROTEINS; DRUG DESIGN; HUMANS; MYCOBACTERIUM TUBERCULOSIS; TUBERCULOSIS;

EID: 78650994038     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2010.10.004     Document Type: Review

References (99)

1. Wirth T., et al. Origin, spread and demography of the Mycobacterium tuberculosis complex. PLoS Pathogens 2008, 4:e1000160.
2. Burman W.J. Rip Van Winkle wakes up: development of tuberculosis treatment in the 21st century. Clin. Infect. Dis. 2010, 50(Suppl. 3):S165-S172.
3. Waksman S.A., et al. Strain specificity and production of antibiotic substances: v. strain resistance of bacteria to antibiotic substances, especially to streptomycin. Proc. Natl. Acad. Sci. U. S. A. 1945, 31:157-164.
4. Camacho L.R., et al. Identification of a virulence gene cluster of Mycobacterium tuberculosis by signature-tagged transposon mutagenesis. Mol. Microbiol. 1999, 34:257-267.
5. Rubin E.J., et al. In vivo transposition of mariner-based elements in enteric bacteria and mycobacteria. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:1645-1650.
6. Sassetti C.M., et al. Genes required for mycobacterial growth defined by high density mutagenesis. Mol. Microbiol. 2003, 48:77-84.
7. Rengarajan J., et al. Genome-wide requirements for Mycobacterium tuberculosis adaptation and survival in macrophages. Proc. Natl. Acad. Sci. U. S. A. 2005, 102:8327-8332.
8. Lamichhane G., et al. Designer arrays for defined mutant analysis to detect genes essential for survival of Mycobacterium tuberculosis in mouse lungs. Infect. Immun. 2005, 73:2533-2540.
9. Jain S.K., et al. Accelerated detection of Mycobacterium tuberculosis genes essential for bacterial survival in guinea pigs, compared with mice. J. Infect. Dis. 2007, 195:1634-1642.
10. Dutta N.K., et al. Genetic requirements for the survival of tubercle bacilli in primates. J. Infect. Dis. 2010, 201:1743-1752.
11. Boshoff H.I., et al. The transcriptional responses of Mycobacterium tuberculosis to inhibitors of metabolism: novel insights into drug mechanisms of action. J. Biol. Chem. 2004, 279:40174-40184.
12. Lamichhane G., Bishai W. Defining the 'survivasome' of Mycobacterium tuberculosis. Nat. Med. 2007, 13:280-282.
13. Ioerger T.R., Sacchettini J.C. Structural genomics approach to drug discovery for Mycobacterium tuberculosis. Curr. Opin. Microbiol. 2009, 12:318-325.
14. Cole S.T., et al. Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 1998, 393:537-544.
15. Dannenberg, A.M. and Tomashefski, J.F. (1998) Pathogenesis of pulmonary tuberculosis. In Fishman's Pulmonary Disease and Disorders (3rd edn) (Fishman, A.P., ed.), pp. 2447-2471, McGraw-Hill.
16. Deretic V., Fratti R.A. Mycobacterium tuberculosis phagosome. Mol. Microbiol. 1999, 31:1603-1609.
17. Hopewell, P.C. and Bloom, B.R. (2000) Tuberculosis and other mycobacterial disease. In Textbook of respiratory medicine (3rd edn) (Murray, J.F. and Nadel, J.A., eds), pp. 1043-1105, WB Saunders.
18. Dye C., et al. Consensus statement. Global burden of tuberculosis: estimated incidence, prevalence, and mortality by country. WHO Global Surveillance and Monitoring Project. Jama 1999, 282:677-686.
19. Stead W.W. Pathogenesis of a first episode of chronic pulmonary tuberculosis in man: recrudescence of residuals of the primary infection or exogenous reinfection?. Am. Rev. Respir. Dis. 1967, 95:729-745.
20. Mukadi Y.D., et al. Tuberculosis case fatality rates in high HIV prevalence populations in sub-Saharan Africa. AIDS (London, England) 2001, 15:143-152.
21. Selwyn P.A., et al. A prospective study of the risk of tuberculosis among intravenous drug users with human immunodeficiency virus infection. N. Engl. J. Med. 1989, 320:545-550.
22. Burzynski, J.N. et al. (2004) Tuberculosis and the human immunodeficiency virus infection. In Tuberculosis (2nd edn) (Rom, W.N. and Garay, S.M., eds), pp. 663-688, Lippincott Williams & Wilkins.
23. Kalscheuer R., et al. Self-poisoning of Mycobacterium tuberculosis by targeting GlgE in an alpha-glucan pathway. Nat. Chem. Biol. 2010, 6:376-384.
24. Marrakchi H., et al. A comprehensive overview of mycolic acid structure and biosynthesis. The Mycobacterial Cell Envelope 2008, 41-62. ASM Press. M. Daffe, J.M. Reyrat (Eds.).
25. Yuan Y., et al. Identification of a gene involved in the biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:6630-6634.
26. Glickman M.S., et al. The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase. J. Biol. Chem. 2001, 276:2228-2233.
27. Glickman M.S. The mmaA2 gene of Mycobacterium tuberculosis encodes the distal cyclopropane synthase of the alpha-mycolic acid. J. Biol. Chem. 2003, 278:7844-7849.
28. Glickman M.S., et al. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 2000, 5:717-727.
29. Rao V., et al. Trans-cyclopropanation of mycolic acids on trehalose dimycolate suppresses Mycobacterium tuberculosis-induced inflammation and virulence. J. Clin. Invest. 2006, 116:1660-1667.
30. Barkan D., et al. Mycolic acid cyclopropanation is essential for viability, drug resistance, and cell wall integrity of Mycobacterium tuberculosis. Chem. Biol. 2009, 16:499-509.
31. Makarov V., et al. Benzothiazinones kill Mycobacterium tuberculosis by blocking arabinan synthesis. Science (New York, N.Y) 2009, 324:801-804.
32. Mikusova K., et al. Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose. J. Bacteriol. 2005, 187:8020-8025.
33. Wolucka B.A. Biosynthesis of D-arabinose in mycobacteria - a novel bacterial pathway with implications for antimycobacterial therapy. The FEBS Journal 2008, 275:2691-2711.
34. Christophe T., et al. High content screening identifies decaprenyl-phosphoribose 2′ epimerase as a target for intracellular antimycobacterial inhibitors. PLoS pathogens 2009, 5:e1000645.
35. Manina G., et al. Decaprenylphosphoryl-b-D-ribose 2′-epimerase from Mycobacterium tuberculosis is a magic drug target. Curr. Med. Chem. 2010, 17:3099-3108.
36. Sareen D., et al. Mycothiol is essential for growth of Mycobacterium tuberculosis Erdman. J. Bacteriol. 2003, 185:6736-6740.
37. Rawat M., et al. Mycothiol-deficient Mycobacterium smegmatis mutants are hypersensitive to alkylating agents, free radicals, and antibiotics. Antimicrob. Agents Chemother. 2002, 46:3348-3355.
38. Sareen D., et al. ATP-dependent L-cysteine:1D-myo-inosityl 2-amino-2-deoxy-alpha-D-glucopyranoside ligase, mycothiol biosynthesis enzyme MshC, is related to class I cysteinyl-tRNA synthetases. Biochemistry 2002, 41:6885-6890.
39. Gutierrez-Lugo M.T., et al. Dequalinium, a new inhibitor of Mycobacterium tuberculosis mycothiol ligase identified by high-throughput screening. J. Biomol. Screen 2009, 14:643-652.
40. Karp P.D., et al. Expansion of the BioCyc collection of pathway/genome databases to 160 genomes. Nucleic. Acids Res. 2005, 33:6083-6089.
41. Parish T. Starvation survival response of Mycobacterium tuberculosis. J. Bacteriol. 2003, 185:6702-6706.
42. Cho Y., et al. Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis. J. Biol. Chem. 2003, 278:8333-8339.
43. Cho Y., et al. Discovery of novel nitrobenzothiazole inhibitors for Mycobacterium tuberculosis ATP phosphoribosyl transferase (HisG) through virtual screening. J. Med. Chem. 2008, 51:5984-5992.
44. Andries K., et al. A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis. Science (New York, N.Y) 2005, 307:223-227.
45. Koul A., et al. Diarylquinolines target subunit c of mycobacterial ATP synthase. Nat. Chem. Biol. 2007, 3:323-324.
46. Haagsma A.C., et al. Selectivity of TMC207 towards mycobacterial ATP synthase compared with that towards the eukaryotic homologue. Antimicrob. Agents Chemother. 2009, 53:1290-1292.
47. Koul A., et al. Diarylquinolines are bactericidal for dormant mycobacteria as a result of disturbed ATP homeostasis. J. Biol. Chem. 2008, 283:25273-25280.
48. Diacon A.H., et al. The diarylquinoline TMC207 for multidrug-resistant tuberculosis. N. Engl. J. Med. 2009, 360:2397-2405.
49. Solbiati J., et al. Processing of the N termini of nascent polypeptide chains requires deformylation prior to methionine removal. J. Mol. Biol. 1999, 290:607-614.
50. Teo J.W., et al. Peptide deformylase inhibitors as potent antimycobacterial agents. Antimicrob. Agents Chemother. 2006, 50:3665-3673.
51. Hackbarth C.J., et al. N-alkyl urea hydroxamic acids as a new class of peptide deformylase inhibitors with antibacterial activity. Antimicrob. Agents Chemother. 2002, 46:2752-2764.
52. Lamichhane G., et al. A postgenomic method for predicting essential genes at subsaturation levels of mutagenesis: application to Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:7213-7218.
53. Olaleye O., et al. Methionine aminopeptidases from Mycobacterium tuberculosis as novel antimycobacterial targets. Chem. Biol. 2010, 17:86-97.
54. Gomez J.E., McKinney J.D. M. tuberculosis persistence, latency, and drug tolerance. Tuberculosis (Edinburgh, Scotland) 2004, 84:29-44.
55. Lewis K. Persister cells, dormancy and infectious disease. Nat. Rev. 2007, 5:48-56.
56. Jindani A., et al. Bactericidal and sterilizing activities of antituberculosis drugs during the first 14 days. Am. J. Respir. Crit. Care Med. 2003, 167:1348-1354.
57. McKinney J.D., et al. Persistence of Mycobacterium tuberculosis in macrophages and mice requires the glyoxylate shunt enzyme isocitrate lyase. Nature 2000, 406:735-738.
58. 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.
59. Darwin K.H. Prokaryotic ubiquitin-like protein (Pup), proteasomes and pathogenesis. Nat. Rev. 2009, 7:485-491.
60. Darwin K.H., et al. The proteasome of Mycobacterium tuberculosis is required for resistance to nitric oxide. Science (New York, N.Y) 2003, 302:1963-1966.
61. Valway S.E., et al. An outbreak involving extensive transmission of a virulent strain of Mycobacterium tuberculosis. N. Engl. J. Med. 1998, 338:633-639.
62. Lamichhane G., et al. Deletion of a Mycobacterium tuberculosis proteasomal ATPase homologue gene produces a slow-growing strain that persists in host tissues. J. Infect. Dis. 2006, 194:1233-1240.
63. Hu G., et al. Structure of the Mycobacterium tuberculosis proteasome and mechanism of inhibition by a peptidyl boronate. Mol. Microbiol. 2006, 59:1417-1428.
64. Groll M., et al. Investigations on the maturation and regulation of archaebacterial proteasomes. J. Mol. Biol. 2003, 327:75-83.
65. Lin G., et al. Inhibitors selective for mycobacterial versus human proteasomes. Nature 2009, 461:621-626.
66. Gandotra S., et al. In vivo gene silencing identifies the Mycobacterium tuberculosis proteasome as essential for the bacteria to persist in mice. Nat. Med. 2007, 13:1515-1520.
67. Gandotra S., et al. The Mycobacterium tuberculosis proteasome active site threonine is essential for persistence yet dispensable for replication and resistance to nitric oxide. PLoS pathogens 2010, 6.
68. Wietzerbin J., et al. Occurrence of D-alanyl-(D)-meso-diaminopimelic acid and meso-diaminopimelyl-meso-diaminopimelic acid interpeptide linkages in the peptidoglycan of Mycobacteria. Biochemistry 1974, 13:3471-3476.
69. Lavollay M., et al. The peptidoglycan of stationary-phase Mycobacterium tuberculosis predominantly contains cross-links generated by L,D-transpeptidation. J. Bacteriol. 2008, 190:4360-4366.
70. Gupta R., et al. The Mycobacterium tuberculosis gene, ldtMt2, encodes a non-classical transpeptidase required for virulence and resistance to amoxicillin. Nat. Med. 2010, 16:466-469.
71. Park H.D., et al. Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Mol. Microbiol. 2003, 48:833-843.
72. Voskuil M.I., et al. Inhibition of respiration by nitric oxide induces a Mycobacterium tuberculosis dormancy program. J. Exp. Med. 2003, 198:705-713.
73. Wisedchaisri G., et al. Structures of Mycobacterium tuberculosis DosR and DosR-DNA complex involved in gene activation during adaptation to hypoxic latency. J. Mol. Biol. 2005, 354:630-641.
74. Schnappinger D., et al. Transcriptional adaptation of Mycobacterium tuberculosis within macrophages: insights into the phagosomal environment. J. Exp. Med. 2003, 198:693-704.
75. Stallings C.L., et al. CarD is an essential regulator of rRNA transcription required for Mycobacterium tuberculosis persistence. Cell 2009, 138:146-159.
76. Avarbock D., et al. Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 1999, 233:261-269.
77. Dahl J.L., et al. The role of RelMtb-mediated adaptation to stationary phase in long-term persistence of Mycobacterium tuberculosis in mice. Proc. Natl. Acad. Sci. U. S. A. 2003, 100:10026-10031.
78. Primm T.P., et al. The stringent response of Mycobacterium tuberculosis is required for long-term survival. J. Bacteriol. 2000, 182:4889-4898.
79. Campbell E.A., et al. Structural mechanism for rifampicin inhibition of bacterial rna polymerase. Cell 2001, 104:901-912.
80. Feklistov A., et al. Rifamycins do not function by allosteric modulation of binding of Mg2+ to the RNA polymerase active center. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:14820-14825.
81. Telenti A., et al. Detection of rifampicin-resistance mutations in Mycobacterium tuberculosis. Lancet 1993, 341:647-650.
82. Donnabella V., et al. Isolation of the gene for the beta subunit of RNA polymerase from rifampicin-resistant Mycobacterium tuberculosis and identification of new mutations. Am. J. Respir. Cell Mol. Biol. 1994, 11:639-643.
83. Zhang Y., et al. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 1992, 358:591-593.
84. Banerjee A., et al. inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science (New York, N.Y) 1994, 263:227-230.
85. Mdluli K., et al. Inhibition of a Mycobacterium tuberculosis beta-ketoacyl ACP synthase by isoniazid. Science (New York, N.Y) 1998, 280:1607-1610.
86. Kremer L., et al. Inhibition of InhA activity, but not KasA activity, induces formation of a KasA-containing complex in mycobacteria. J. Biol. Chem. 2003, 278:20547-20554.
87. Basso L.A., et al. Mechanisms of isoniazid resistance in Mycobacterium tuberculosis: enzymatic characterization of enoyl reductase mutants identified in isoniazid-resistant clinical isolates. J. Infect. Dis. 1998, 178:769-775.
88. Slayden R.A., et al. Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 2000, 38:514-525.
89. Zimhony O., et al. Pyrazinamide inhibits the eukaryotic-like fatty acid synthetase I (FASI) of Mycobacterium tuberculosis. Nat. Med. 2000, 6:1043-1047.
90. Boshoff H.I., et al. Effects of pyrazinamide on fatty acid synthesis by whole mycobacterial cells and purified fatty acid synthase I. J. Bacteriol. 2002, 184:2167-2172.
91. Belanger A.E., et al. The embAB genes of Mycobacterium avium encode an arabinosyl transferase involved in cell wall arabinan biosynthesis that is the target for the antimycobacterial drug ethambutol. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:11919-11924.
92. Onodera Y., et al. Inhibitory activity of quinolones against DNA gyrase of Mycobacterium tuberculosis. J. Antimicrob. Chemother. 2001, 47:447-450.
93. Purohit P., Stern S. Interactions of a small RNA with antibiotic and RNA ligands of the 30S subunit. Nature 1994, 370:659-662.
94. Halouska S., et al. Use of NMR metabolomics to analyze the targets of D-cycloserine in mycobacteria: role of D-alanine racemase. J. Proteome Res. 2007, 6:4608-4614.
95. WHO Global tuberculosis control. WHO TB Control 2009, 4-5.
96. Wright A., et al. Epidemiology of antituberculosis drug resistance 2002-07: an updated analysis of the Global Project on Anti-Tuberculosis Drug Resistance Surveillance. Lancet 2009, 373:1861-1873.
97. Wei J.R., Rubin E.J. The many roads to essential genes. Tuberculosis (Edinburgh, Scotland) 2008, 88(Suppl. 1):S19-24.
98. Betts J.C., et al. Evaluation of a nutrient starvation model of Mycobacterium tuberculosis persistence by gene and protein expression profiling. Mol. Microbiol. 2002, 43:717-731.
99. Payne D.J., et al. Drugs for bad bugs: confronting the challenges of antibacterial discovery. Nat. Rev. Drug Discov. 2007, 6:29-40.