Drug resistance mechanisms and novel drug targets for tuberculosis therapy

Journal of Genetics and Genomics

Volumn 44, Issue 1, 2017, Pages 21-37

  Islam, Md Mahmudul ^a,b   Hameed, H M Adnan ^a,b   Mugweru, Julius ^a,b   Chhotaray, Chiranjibi ^a,b   Wang, Changwei ^a,d   Tan, Yaoju ^c   Liu, Jianxiong ^c   Li, Xinjie ^c   Tan, Shouyong ^c   Ojima, Iwao ^d   Yew, Wing Wai ^e   Nuermberger, Eric ^f   Lamichhane, Gyanu ^f   Zhang, Tianyu ^a,b  

^a GUANGZHOU INSTITUTES OF BIOMEDICINE AND HEALTH   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c GUANGZHOU CHEST HOSPITAL   (China)

^d STONY BROOK UNIVERSITY   (United States)

^e CHINESE UNIVERSITY OF HONG KONG   (Hong Kong)

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

Author keywords

Drug target; Mechanism; Mycobacterium tuberculosis; Resistance; Tuberculosis

Indexed keywords

AMIKACIN; AMINOSALICYLIC ACID; BEDAQUILINE; CAPREOMYCIN; CLOFAZIMINE; CYCLOSERINE; DELAMANID; ETHAMBUTOL; ETHIONAMIDE; ISONIAZID; KANAMYCIN; LINEZOLID; N (2 ADAMANTYL) N' GERANYLETHYLENEDIAMINE; PRETOMANID; PROTIONAMIDE; PYRAZINAMIDE; QUINOLINE DERIVED ANTIINFECTIVE AGENT; RIFAMPICIN; STREPTOMYCIN; TUBERCULOSTATIC AGENT; VIOMYCIN;

BACTERIAL GENOME; DRUG RESISTANT TUBERCULOSIS; GENE MUTATION; GENE SEQUENCE; HUMAN; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; REVIEW; WHOLE GENOME SEQUENCING; ANIMAL; ANTIBIOTIC RESISTANCE; DRUG EFFECTS; GENETICS; GENOMICS; MOLECULARLY TARGETED THERAPY; PHYSIOLOGY; PROCEDURES; TUBERCULOSIS;

ANIMALS; ANTITUBERCULAR AGENTS; DRUG RESISTANCE, BACTERIAL; GENOMICS; HUMANS; MOLECULAR TARGETED THERAPY; MYCOBACTERIUM TUBERCULOSIS; TUBERCULOSIS;

EID: 85009108621     PISSN: 16738527     EISSN: 18735533     Source Type: Journal    
DOI: 10.1016/j.jgg.2016.10.002     Document Type: Review

References (278)

1. Abrahams, K.A., Cox, J.A., Spivey, V.L., Loman, N.J., Pallen, M.J., Constantinidou, C., Fernandez, R., Alemparte, C., Remuinan, M.J., Barros, D., Ballell, L., Identification of novel imidazo [1, 2-a] pyridine inhibitors targeting M. tuberculosis QcrB. PLoS One, 7, 2012, e52951.
2. Ajbani, K., Rodrigues, C., Shenai, S., Mehta, A., Mutation detection and accurate diagnosis of extensively drug-resistant tuberculosis: report from a tertiary care center in India. J. Clin. Microbiol. 49 (2011), 1588–1590.
3. Alahari, A., Trivelli, X., Guérardel, Y., Dover, L.G., Besra, G.S., Sacchettini, J.C., Reynolds, R.C., Coxon, G.D., Kremer, L., Thiacetazone, an antitubercular drug that inhibits cyclopropanation of cell wall mycolic acids in mycobacteria. PLoS One, 2, 2007, e1343.
4. Alangaden, G.J., Kreiswirth, B.N., Aouad, A., Khetarpal, M., Igno, F.R., Moghazeh, S.L., Manavathu, E.K., Lerner, S.A., Mechanism of resistance to amikacin and kanamycin in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 42 (1998), 1295–1297.
5. Alexander, D.C., Ma, J.H., Guthrie, J.L., Blair, J., Chedore, P., Jamieson, F.B., Gene sequencing for routine verification of pyrazinamide resistance in Mycobacterium tuberculosis: a role for pncA but not rpsA. J. Clin. Microbiol. 50 (2012), 3726–3728.
6. Allegui, Z., Ghariani, A., Draoui, H., Ghezal, A., Mehiri, E., Slim-Saidi, L., Detection of isoniazid and rifampin resistance of Mycobacterium tuberculosis by a multiplex allele-specific polymerase chain reaction (PCR) assay. Int. J. Mycobacteriol. 1 (2012), 34–39.
7. Almeida, D., Ioerger, T., Tyagi, S., Li, S.Y., Mdluli, K., Andries, K., Grosset, J., Sacchettini, J., Nuermberger, E., Mutations in pepQ confer low-level resistance to bedaquiline and clofazimine in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 60 (2016), 4590–4599.
8. Alvarez, N., Zapata, E., Mejía, G.I., Realpe, T., Araque, P., Peláez, C., Rouzaud, F., Robledo, J., The structural modeling of the interaction between levofloxacin and the Mycobacterium tuberculosis gyrase catalytic site sheds light on the mechanisms of fluoroquinolones resistant tuberculosis in Colombian clinical isolates. BioMed. Res. Int. 2014 (2014), 367–368.
9. An, D.D., Duyen, N.T.H., Lan, N.T.N., Ha, D.T.M., Kiet, V.S., Chau, N.V.V., Dung, N.H., Sy, D.N., Farrar, J., Caws, M., Beijing genotype of Mycobacterium tuberculosis is significantly associated with high-level fluoroquinolone resistance in Vietnam. Antimicrob. Agents Chemother. 53 (2009), 4835–4839.
10. Andres, S., Hillemann, D., Rüsch-Gerdes, S., Richter, E., Occurrence of rpoB mutations in isoniazid-resistant but rifampin-susceptible Mycobacterium tuberculosis isolates from Germany. Antimicrob. Agents Chemother. 58 (2014), 590–592.
11. Andries, K., Verhasselt, P., Guillemont, J., Göhlmann, H.W., Neefs, J.M., Winkler, H., Van Gestel, J., Timmerman, P., Zhu, M., Lee, E., Williams, P., A diarylquinoline drug active on the ATP synthase of Mycobacterium tuberculosis. Science 307 (2005), 223–227.
12. Andries, K., Villellas, C., Coeck, N., Thys, K., Gevers, T., Vranckx, L., Lounis, N., de Jong, B.C., Koul, A., Acquired resistance of Mycobacterium tuberculosis to bedaquiline. PLoS One, 9, 2014, e102135.
13. Arbex, M.A., Varella, M.D.C.L., Siqueira, H.R.D., Mello, F.A.F.D., Antituberculosis drugs: drug interactions, adverse effects, and use in special situations-part 1: first-line drugs. J. Bras. Pneumol. 36 (2010), 626–640.
14. Awasthi, D., Kumar, K., Knudson, S.E., Slayden, R.A., Ojima, I., SAR studies on trisubstituted benzimidazoles as inhibitors of Mtb FtsZ for the development of novel antitubercular agents. J. Med. Chem., 56, 2013 9756–7970.
15. Aye, K.S., Nakajima, C., Yamaguchi, T., Win, M.M., Shwe, M.M., Win, A.A., Lwin, T., Nyunt, W.W., Ti, T., Suzuki, Y., Genotypic characterization of multi-drug-resistant Mycobacterium tuberculosis isolates in Myanmar. J. Infect. Chemother. 22 (2016), 174–179.
16. Banerjee, A., Dubnau, E., Quemard, A., Balasubramanian, V., Um, K.S., Wilson, T., Collins, D., De Lisle, G., Jacobs, W.R. Jr., inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 263 (1994), 227–229.
17. Bantubani, N., Kabera, G., Connolly, C., Rustomjee, R., Reddy, T., Cohen, T., Pym, A.S., High rates of potentially infectious tuberculosis and multidrug-resistant tuberculosis (MDR-TB) among hospital inpatients in KwaZulu Natal, South Africa indicate risk of nosocomial transmission. PLoS One, 9, 2014, e90868.
18. Baulard, A.R., Betts, J.C., Engohang-Ndong, J., Quan, S., McAdam, R.A., Brennan, P.J., Locht, C., Besra, G.S., Activation of the pro-drug ethionamide is regulated in mycobacteria. J. Biol. Chem. 275 (2000), 28326–28331.
19. Beckert, P., Hillemann, D., Kohl, T.A., Kalinowski, J., Richter, E., Niemann, S., Feuerriegel, S., rplC T460C identified as a dominant mutation in linezolid-resistant Mycobacterium tuberculosis strains. Antimicrob. Agents Chemother. 56 (2012), 2743–2745.
20. Belanger, A.E., Besra, G.S., Ford, M.E., Mikusová, K., Belisle, J.T., Brennan, P.J., Inamine, J.M., 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. 93 (1996), 11919–11924.
21. Bhuju, S., de Souza Fonseca, L., Marsico, A.G., de Oliveira Vieira, G.B., Sobral, L.F., Stehr, M., Singh, M., Saad, M.H.F., Mycobacterium tuberculosis isolates from Rio de Janeiro reveal unusually low correlation between pyrazinamide resistance and mutations in the pncA gene. Infect. Genet. Evol. 19 (2013), 1–6.
22. Blanchard, J.S., Molecular mechanisms of drug resistance in Mycobacterium tuberculosis. Annu. Rev. Biochem. 65 (1996), 215–239.
23. Bloemberg, G.V., Keller, P.M., Stucki, D., Trauner, A., Borrell, S., Latshang, T., Coscolla, M., Rothe, T., Hömke, R., Ritter, C., Feldmann, J., Acquired resistance to bedaquiline and delamanid in therapy for tuberculosis. N. Engl. J. Med. 373 (2015), 1986–1988.
24. Boonaiam, S., Chaiprasert, A., Prammananan, T., Leechawengwongs, M., Genotypic analysis of genes associated with isoniazid and ethionamide resistance in MDR-TB isolates from Thailand. Clin. Microbiol. Infect. 16 (2010), 396–399.
25. Brossier, F., Sougakoff, W., Bernard, C., Petrou, M., Adeyema, K., Pham, A., de La Breteque, D.A., Vallet, M., Jarlier, V., Sola, C., Veziris, N., Molecular analysis of the embCAB locus and embR gene involved in ethambutol resistance in clinical isolates of Mycobacterium tuberculosis in France. Antimicrob. Agents Chemother. 59 (2015), 4800–4808.
26. Bruning, J.B., Murillo, A.C., Chacon, O., Barletta, R.G., Sacchettini, J.C., Structure of the Mycobacterium tuberculosis D-alanine: D-alanine ligase, a target of the antituberculosis drug D-cycloserine. Antimicrob. Agents Chemother. 55 (2011), 291–301.
27. Caceres, N.E., Harris, N.B., Wellehan, J.F., Feng, Z., Kapur, V., Barletta, R.G., Overexpression of the D-alanine racemase gene confers resistance to D-cycloserine in Mycobacterium smegmatis. J. Bacteriol. 179 (1997), 5046–5055.
28. Campbell, P.J., Morlock, G.P., Sikes, R.D., Dalton, T.L., Metchock, B., Starks, A.M., Hooks, D.P., Cowan, L.S., Plikaytis, B.B., Posey, J.E., Molecular detection of mutations associated with first- and second-line drug resistance compared with conventional drug susceptibility testing of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 55 (2011), 2032–2041.
29. Carette, X., Blondiaux, N., Willery, E., Hoos, S., Lecat-Guillet, N., Lens, Z., Wohlkönig, A., Wintjens, R., Soror, S.H., Frénois, F., Dirié, B., Structural activation of the transcriptional repressor EthR from Mycobacterium tuberculosis by single amino acid change mimicking natural and synthetic ligands. Nucleic Acids Res. 40 (2011), 3018–3030.
30. Casali, N., Nikolayevskyy, V., Balabanova, Y., Harris, S.R., Ignatyeva, O., Kontsevaya, I., Corander, J., Bryant, J., Parkhill, J., Nejentsev, S., Horstmann, R.D., Evolution and transmission of drug resistant tuberculosis in a Russian population. Nat. Genet., 46, 2014, 279.
31. CDC, Treatment of tuberculosis, morbidity and mortality weekly report. Recommen. Rep. 52 (2003), 1–77.
32. Chang, K.C., Yew, W.W., Tam, C.M., Leung, C.C., WHO group 5 drugs and difficult multidrug-resistant tuberculosis: a systematic review with cohort analysis and meta-analysis. Antimicrob. Agents Chemother. 57 (2013), 4097–4104.
33. Chen, J.M., Uplekar, S., Gordon, S.V., Cole, S.T., A point mutation in cycA partially contributes to the D-cycloserine resistance trait of Mycobacterium bovis BCG vaccine strains. PLoS One, 7, 2012, e43467.
34. Chen, Q., Pang, Y., Liang, Q., Lin, S., Wang, Y., Lin, J., Zhao, Y., Wei, S., Zheng, J., Zheng, S., Molecular characteristics of MDR Mycobacterium tuberculosis strains isolated in Fujian, China. Tuberculosis 94 (2014), 159–161.
35. China, A., Mishra, S., Tare, P., Nagaraja, V., Inhibition of Mycobacterium tuberculosis RNA polymerase by binding of a Gre factor homolog to the secondary channel. J. Bacteriol. 194 (2012), 1009–1017.
36. Cohen, K.A., Abeel, T., McGuire, A.M., Desjardins, C.A., Munsamy, V., Shea, T.P., Walker, B.J., Bantubani, N., Almeida, D.V., Alvarado, L., Chapman, S.B., Evolution of extensively drug-resistant tuberculosis over four decades: whole genome sequencing and dating analysis of Mycobacterium tuberculosis isolates from KwaZulu-Natal. PLoS Med., 12, 2015, e1001880.
37. Cholo, M.C., Steel, H.C., Fourie, P.B., Germishuizen, W.A., Anderson, R., Clofazimine: current status and future prospects. J. Antimicrob. Chemother. 67 (2012), 290–298.
38. Comas, I., Borrell, S., Roetzer, A., Rose, G., Malla, B., Kato-Maeda, M., Galagan, J., Niemann, S., Gagneux, S., Whole-genome sequencing of rifampicin-resistant Mycobacterium tuberculosis strains identifies compensatory mutations in RNA polymerase genes. Nat. Genet. 44 (2012), 106–110.
39. Comroe, J.H. Jr., Pay dirt: the story of streptomycin. Part I: from Waksman to Waksman. Am. Rev. Respir. Dis. 117 (1978), 773–781.
40. Cooksey, R.C., Morlock, G.P., McQueen, A., Glickman, S.E., Crawford, J.T., Characterization of streptomycin resistance mechanisms among Mycobacterium tuberculosis isolates from patients in New York City. Antimicrob. Agents Chemother. 40 (1996), 1186–1188.
41. Cuevas-Córdoba, B., Cuellar-Sánchez, A., Pasissi-Crivelli, A., Santana-Álvarez, C.A., Hernández-Illezcas, J., Zenteno-Cuevas, R., rrs and rpsL mutations in streptomycin-resistant isolates of Mycobacterium tuberculosis from Mexico. J. Microbiol. Immunol. Infect. 46 (2013), 30–34.
42. Cuevas-Córdoba, B., Juárez-Eusebio, D.M., Almaraz-Velasco, R., Muñiz-Salazar, R., Laniado-Laborin, R., Zenteno-Cuevas, R., Mutation at embB codon 306, a potential marker for the identification of multidrug resistance associated with ethambutol in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 59 (2015), 5455–5462.
43. Cui, Z., Wang, J., Lu, J., Huang, X., Hu, Z., Association of mutation patterns in gyrA/B genes and ofloxacin resistance levels in Mycobacterium tuberculosis isolates from East China in 2009. BMC Infect. Dis., 11, 2011, 78.
44. Cynamon, M.H., Sklaney, M., Gatifloxacin and ethionamide asthe foundation for therapy of tuberculosis. Antimicrob. Agents Chemother. 47 (2003), 2442–2444.
45. D'Ambrosio, L., Centis, R., Sotgiu, G., Pontali, E., Spanevello, A., Migliori, G.B., New anti-tuberculosis drugs and regimens: 2015 update. E.R.J. Open Res. 1 (2015), 00010–02015.
46. Datta, G., Nieto, L.M., Davidson, R.M., Mehaffy, C., Pederson, C., Dobos, K.M., Strong, M., Longitudinal whole genome analysis of pre and post drug treatment Mycobacterium tuberculosis isolates reveals progressive steps to drug resistance. Tuberculosis 98 (2016), 50–55.
47. DeBarber, A.E., Mdluli, K., Bosman, M., Bekker, L.G., Barry, C.E., Ethionamide activation and sensitivity in multidrug-resistant Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 9677–9682.
48. Desjardins, C.A., Cohen, K.A., Munsamy, V., Abeel, T., Maharaj, K., Walker, B.J., Shea, T.P., Almeida, D.V., Manson, A.L., Salazar, A., Padayatchi, N., Genomic and functional analyses of Mycobacterium tuberculosis strains implicate ald in D-cycloserine resistance. Nat. Genet. 48 (2016), 544–551.
49. Dessen, A., Quemard, A., Blanchard, J.S., Jacobs, W.R. Jr., Sacchettin, J.C., Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science 267 (1995), 1638–1641.
50. Devasia, R., Blackman, A., Eden, S., Li, H., Maruri, F., Shintani, A., Alexander, C., Kaiga, A., Stratton, C.W., Warkentin, J., Tang, Y.W., High proportion of fluoroquinolone-resistant Mycobacterium tuberculosis isolates with novel gyrase polymorphisms and a gyrA region associated with fluoroquinolone susceptibility. J. Clin. Microbiol. 50 (2011), 1390–1396.
51. Diacon, A.H., Dawson, R., von Groote-Bidlingmaier, F., Symons, G., Venter, A., Donald, P.R., van Niekerk, C., Everitt, D., Hutchings, J., Burger, D.A., Schall, R., Bactericidal activity of pyrazinamide and clofazimine alone and in combinations with pretomanid and bedaquiline. Am. J. Respir. Crit. Care Med. 191 (2015), 943–953.
52. Diacon, A.H., Dawson, R., von Groote-Bidlingmaier, F., Symons, G., Venter, A., Donald, P.R., van Niekerk, C., Everitt, D., Winter, H., Becker, P., Mendel, C.M., 14-day bactericidal activity of Prm, bedaquiline, pyrazinamide, and moxifloxacin combinations: a randomised trial. Lancet 380 (2012), 986–993.
53. Diacon, A.H., Pym, A., Grobusch, M., Patientia, R., Rustomjee, R., Page-Shipp, L., Pistorius, C., Krause, R., Bogoshi, M., Churchyard, G., Venter, A., The diarylquinoline TMC207 for multidrug-resistant tuberculosis. N. Engl. J. Med., 360, 2009 2397–2305.
54. Diacon, A.H., Pym, A., Grobusch, M.P., de los Rios, J.M., Gotuzzo, E., Vasilyeva, I., Leimane, V., Andries, K., Bakare, N., De Marez, T., Haxaire-Theeuwes, M., Multidrug-resistant tuberculosis and culture conversion with bedaquiline. N. Engl. J. Med. 371 (2014), 723–732.
55. Dillon, N.A., Peterson, N.D., Rosen, B.C., Baughn, A.D., Pantothenate and pantetheine antagonize the antitubercular activity of pyrazinamide. Antimicrob. Agents Chemother. 58 (2014), 7258–7263.
56. Du, Q., Dai, G., Long, Q., Yu, X., Dong, L., Huang, H., Xie, J., Mycobacterium tuberculosis rrs A1401G mutation correlates with high-level resistance to kanamycin, amikacin, and capreomycin in clinical isolates from mainland China. Diagn. Microbiol. Infect. Dis. 77 (2013), 138–142.
57. Dye, C., Williams, B.G., Espinal, M.A., Raviglione, M.C., Erasing the world's slow stain: strategies to beat multidrug-resistant tuberculosis. Science 295 (2002), 2042–2046.
58. Eldholm, V., Monteserin, J., Rieux, A., Lopez, B., Sobkowiak, B., Ritacco, V., Balloux, F., Four decades of transmission of a multidrug-resistant Mycobacterium tuberculosis outbreak strain. Nat. Commun., 6, 2015, 7119.
59. Engström, A., Morcillo, N., Imperiale, B., Hoffner, S.E., Juréen, P., Detection of first- and second-line drug resistance in Mycobacterium tuberculosis clinical isolates by pyrosequencing. J. Clin. Microbiol. 50 (2012), 2026–2033.
60. Engström, A., Perskvist, N., Werngren, J., Hoffner, S.E., Juréen, P., Comparison of clinical isolates and in vitro selected mutants reveals that tlyA is not a sensitive genetic marker for capreomycin resistance in Mycobacterium tuberculosis. J. Antimicrob. Chemother. 66 (2011), 1247–1254.
61. Evans, J., Segal, H., Novel multiplex allele-specific PCR assays for the detection of resistance to second-line drugs in Mycobacterium tuberculosis. J. Antimicrob. Chemother., 65, 2010 897–800.
62. Farhat, M.R., Shapiro, B.J., Kieser, K.J., Sultana, R., Jacobson, K.R., Victor, T.C., Warren, R.M., Streicher, E.M., Calver, A., Sloutsky, A., Kaur, D., Genomic analysis identifies targets of convergent positive selection in drug resistant Mycobacterium tuberculosis. Nat. Genet. 45 (2013), 1183–1189.
63. Falzon, D., Jaramillo, E., Schünemann, H.J., Arentz, M., Bauer, M., Bayona, J., Blanc, L., Caminero, J.A., Daley, C.L., Duncombe, C., Fitzpatrick, C., WHO guidelines for the programmatic management of drug-resistant tuberculosis: 2011 update. Eur. Respir. J. 38 (2011), 516–528.
64. Feng, Y., Liu, S., Wang, Q., Wang, L., Tang, S., Wang, J., Lu, W., Rapid diagnosis of drug resistance to fluoroquinolones, amikacin, capreomycin, kanamycin and ethambutol using genotype MTBDRsl assay: a meta-analysis. PLoS One, 8, 2013, e55292.
65. Feng, Z., Barletta, R.G., Roles of Mycobacterium smegmatis D-Alanine: D-alanine ligase and D-alanine racemase in the mechanisms of action of and resistance to the peptidoglycan inhibitor D-cycloserine. Antimicrob. Agents Chemother. 47 (2003), 283–291.
66. Feuerriegel, S., Köser, C.U., Baù, D., Rüsch-Gerdes, S., Summers, D.K., Archer, J.A., Marti-Renom, M.A., Niemann, S., Impact of fgd1 and ddn diversity in Mycobacterium tuberculosis complex on in vitro susceptibility to Prm. Antimicrob. Agents Chemother. 55 (2011), 5718–5722.
67. Ford, C.B., Shah, R.R., Maeda, M.K., Gagneux, S., Murray, M.B., Cohen, T., Johnston, J.C., Gardy, J., Lipsitch, M., Fortune, S.M., Mycobacterium tuberculosis mutation rate estimates from different lineages predict substantial differences in the emergence of drug-resistant tuberculosis. Nat. Genet. 45 (2013), 784–790.
68. Gao, P., Yang, Y., Xiao, C., Liu, Y., Gan, M., Guan, Y., Hao, X., Meng, J., Zhou, S., Chen, X., Cui, J., Identification and validation of a novel lead compound targeting 4-diphosphocytidyl-2-C-methylerythritol synthetase (IspD) of mycobacteria. Eur. J. Pharmacol. 694 (2012), 45–52.
69. Gavalda, S., Léger, M., van der Rest, B., Stella, A., Bardou, F., Montrozier, H., Chalut, C., Burlet-Schiltz, O., Marrakchi, H., Daffé, M., Quémard, A., The Pks13/FadD32 crosstalk for the biosynthesis of mycolic acids in Mycobacterium tuberculosis. J. Biol. Chem. 284 (2009), 19255–19264.
70. Gellert, M., Mizuuchi, K., O'Dea, M.H., Nash, H.A., DNA gyrase: an enzyme that introduces superhelical turns into DNA. Proc. Natl. Acad. Sci. U. S. A. 73 (1976), 3872–3876.
71. Gikalo, M.B., Nosova, E.Y., Krylova, L.Y., Moroz, A.M., The role of eis mutations in the development of kanamycin resistance in Mycobacterium tuberculosis isolates from the Moscow region. J. Antimicrob. Chemother. 67 (2012), 2107–2109.
72. Gillespie, S.H., Evolution of drug resistance in Mycobacterium tuberculosis: clinical and molecular perspective. Antimicrob. Agents Chemother. 46 (2002), 267–274.
73. Ginsberg, A.M., Laurenzi, M.W., Rouse, D.J., Whitney, K.D., Spigelman, M.K., Safety, tolerability, and pharmacokinetics of Prm in healthy subjects. Antimicrob. Agents Chemother., 53, 2009 3720–3625.
74. Ginsburg, A.S., Woolwine, S.C., Hooper, N., Benjamin, W.H. Jr., Bishai, W.R., Dorman, S.E., Sterling, T.R., The rapid development of fluoroquinolone resistance in M. tuberculosis. N. Engl. J. Med. 349 (2003), 1977–1978.
75. Glickman, M.S., Cahill, S.M., Jacobs, W.R., The Mycobacterium tuberculosis cmaA2 gene encodes a mycolic acid trans-cyclopropane synthetase. J. Biol. Chem. 276 (2001), 2228–2233.
76. Glickman, M.S., Cox, J.S., Jacobs, W.R., A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Mol. Cell 5 (2000), 717–727.
77. Gothi, D., Joshi, J.M., Resistant TB newer drugs and community approach. Recent Pat. Anti-infect. Drug Discov. 6 (2011), 27–37.
78. Grosset, J.H., Singer, T.G., Bishai, W.R., New drugs for the treatment of tuberculosis: hope and reality. Int. J. Tuberc. Lung Dis. 16 (2012), 1005–1014.
79. Grosset, J.H., Tyagi, S., Almeida, D.V., Converse, P.J., Li, S.Y., Ammerman, N.C., Bishai, W.R., Enarson, D., Trébucq, A., Assessment of clofazimine activity in a second-line regimen for tuberculosis in mice. Am. J. Respir. Crit. Care Med. 188 (2013), 608–612.
80. Grzegorzewicz, A.E., Pham, H., Gundi, V.A., Scherman, M.S., North, E.J., Hess, T., Jones, V., Gruppo, V., Born, S.E., Korduláková, J., Chavadi, S.S., Inhibition of mycolic acid transport across the Mycobacterium tuberculosis plasma membrane. Nat. Chem. Biol. 8 (2012), 334–341.
81. Gu, Y., Yu, X., Jiang, G., Wang, X., Ma, Y., Li, Y., Huang, H., Pyrazinamide resistance among multidrug-resistant tuberculosis clinical isolates in a national referral center of China and its correlations with pncA, rpsA, and panD gene mutations. Diagn. Microbiol. Infect. Dis. 84 (2016), 207–211.
82. Guerrero, E., Lemus, D., Yzquierdo, S., Vílchez, G., Muñoz, M., Montoro, E., Takiff, H., Association between embB mutations and ethambutol resistance in Mycobacterium tuberculosis isolates from Cuba and the Dominican Republic: reproducible patterns and problems. Rev. Argent. Microbiol. 45 (2013), 21–26.
83. Gupta, R., Lavollay, M., Mainardi, J.L., Arthur, M., Bishai, W.R., Lamichhane, G., The Mycobacterium tuberculosis protein LdtMt2 is a nonclassical transpeptidase required for virulence and resistance to amoxicillin. Nat. Med. 16 (2010), 466–469.
84. Hamze, M., Ismail, M.B., Rahmo, A.K., Dabboussi, F., Pyrosequencing for rapid detection of tuberculosis resistance to rifampicin and isoniazid in Syrian and Lebanese clinical isolates. Int. J. Mycobacteriol., 4, 2015 228–132.
85. Hartkoorn, R.C., Uplekar, S., Cole, S.T., Cross-resistance between clofazimine and bedaquiline through upregulation of MmpL5 in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 58 (2014), 2979–2981.
86. Haver, H.L., Chua, A., Ghode, P., Lakshminarayana, S.B., Singhal, A., Mathema, B., Wintjens, R., Bifani, P., Mutations in genes for the F420 biosynthetic pathway and a nitroreductase enzyme are the primary resistance determinants in spontaneous in vitro-selected Prm-resistant mutants of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 59 (2015), 5316–5323.
87. Hazbón, M.H., Brimacombe, M., del Valle, M.B., Cavatore, M., Guerrero, M.I., Varma-Basil, M., Billman-Jacobe, H., Lavender, C., Fyfe, J., García-García, L., León, C.I., Population genetics study of isoniazid resistance mutations and evolution of multidrug-resistant Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 50 (2006), 2640–2649.
88. Hazbón, M.H., del Valle, M.B., Guerrero, M.I., Varma-Basil, M., Filliol, I., Cavatore, M., Colangeli, R., Safi, H., Billman-Jacobe, H., Lavender, C., Fyfe, J., Role of embB codon 306 mutations in Mycobacterium tuberculosis revisited: a novel association with broad drug resistance and IS 6110 clustering rather than ethambutol resistance. Antimicrob. Agents Chemother. 49 (2005), 3794–3802.
89. He, L., Wang, X., Cui, P., Jin, J., Chen, J., Zhang, W., Zhang, Y., ubiA (Rv3806c) encoding DPPR synthase involved in cell wall synthesis is associated with ethambutol resistance in Mycobacterium tuberculosis. Tuberculosis 95 (2015), 149–154.
90. Heinrich, N., Dawson, R., du Bois, J., Narunsky, K., Horwith, G., Phipps, A.J., Nacy, C.A., Aarnoutse, R.E., Boeree, M.J., Gillespie, S.H., Venter, A., Early phase evaluation of SQ109 alone and in combination with rifampicin in pulmonary TB patients. J. Antimicrob. Chemother. 70 (2015), 1558–1566.
91. Herr Jr., E.B., Hamill, R.L., Mcguire, J.M., 1962. Capreomycin and its preparation. Patent No. 3,143,468 August 4, Indianapolis, USA.
92. Hillemann, D., Rüsch-Gerdes, S., Richter, E., In vitro-selected linezolid-resistant Mycobacterium tuberculosis mutants. Antimicrob. Agents Chemother. 52 (2008), 800–801.
93. Hölzel, C.S., Harms, K.S., Schwaiger, K., Bauer, J., Resistance to linezolid in a porcine Clostridium perfringens strain carrying a mutation in the rplD gene encoding the ribosomal protein L4. Antimicrob. Agents Chemother. 54 (2010), 1351–1353.
94. Hopewell, P.C., Kato-Maeda, M., Ernst, J.D., Tuberculosis, Murray and Nadel's Textbook of Respiratory Medicine. sixth ed., 2016, Elsevier, Philadelphia.
95. Huang, Q., Kirikae, F., Kirikae, T., Pepe, A., Amin, A., Respicio, L., Slayden, R.A., Tonge, P.J., Ojima, I., Targeting FtsZ for antituberculosis drug discovery: noncytotoxic taxanes as novel antituberculosis agents. J. Med. Chem. 49 (2006), 463–466.
96. Huang, W.L., Chi, T.L., Wu, M.H., Jou, R., Performance assessment of the GenoType MTBDRsl test and DNA sequencing for detection of second-line and ethambutol drug resistance among patients infected with multidrug-resistant Mycobacterium tuberculosis. J. Clin. Microbiol. 49 (2011), 2502–2508.
97. Huitric, E., Verhasselt, P., Koul, A., Andries, K., Hoffner, S., Andersson, D.I., Rates and mechanisms of resistance development in Mycobacterium tuberculosis to a novel diarylquinoline ATP synthase inhibitor. Antimicrob. Agents Chemother. 54 (2010), 1022–1028.
98. Iwainsky, H., Mode of action, biotransformation and pharmacokinetics of antituberculosis drugs in animals and man. Bartmann, K., (eds.) Antituberculosis Drugs, 1988, Springer-Verlag, Berlin, Germany, 457–465.
99. Jaber, A.A., Ahmad, S., Mokaddas, E., Minor contribution of mutationsat iniA codon501and embC-embA intergenic region in ethambutol resistant clinical Mycobacterium tuberculosis isolates in Kuwait. Ann. Clin. Microbiol. Antimicrob., 8, 2009, 1.
100. Jagielski, T., Ignatowska, H., Bakuła, Z., Dziewit, Ł., Napiórkowska, A., Augustynowicz-Kopeć, E., Zwolska, Z., Bielecki, J., Screening for streptomycin resistance-conferring mutations in Mycobacterium tuberculosis clinical isolates from Poland. PLoS One, 9, 2014, e100078.
101. Jamieson, F.B., Guthrie, J.L., Neemuchwala, A., Lastovetska, O., Melano, R.G., Mehaffy, C., Profiling of rpoB mutations and MICs for rifampin and rifabutin in Mycobacterium tuberculosis. J. Clin. Microbiol. 52 (2014), 2157–2162.
102. Jnawali, H.N., Hwang, S.C., Park, Y.K., Kim, H., Lee, Y.S., Chung, G.T., Choe, K.H., Ryoo, S., Characterization of mutations in multi- and extensive drug resistance among strains of Mycobacterium tuberculosis clinical isolates in Republic of Korea. Diagn. Microbiol. Infect. Dis. 76 (2013), 187–196.
103. Johansen, S.K., Maus, C.E., Plikaytis, B.B., Douthwaite, S., Capreomycin binds across the ribosomal subunit interface using tlyA-encoded 2′-O-methylations in 16S and 23S rRNAs. Mol. Cell 23 (2006), 173–182.
104. Juréen, P., Werngren, J., Toro, J.C., Hoffner, S., Pyrazinamide resistance and pncA gene mutations in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 52 (2008), 1852–1854.
105. Kantardjieff, K.A., Kim, C.Y., Naranjo, C., Waldo, G.S., Lekin, T., Segelke, B.W., Zemla, A., Park, M.S., Terwilliger, T.C., Rupp, B., Mycobacterium tuberculosis RmlC epimerase (Rv3465): a promising drug-target structure in the rhamnose pathway. Acta Crystallogr. D. Biol. 60 (2004), 895–902.
106. Kato, J.I., Nishimura, Y., Imamura, R., Niki, H., Hiraga, S., Suzuki, H., New topoisomerase essential for chromosome segregation in E. coli. Cell 63 (1990), 393–404.
107. Kaushik, A., Makkar, N., Pandey, P., Parrish, N., Singh, U., Lamichhane, G., Carbapenems and rifampin exhibit synergy against Mycobacterium tuberculosis and Mycobacterium abscessus. Antimicrob. Agents Chemother. 59 (2015), 6561–6567.
108. Klitgaard, R.N., Ntokou, E., Nørgaard, K., Biltoft, D., Hansen, L.H., Trædholm, N.M., Kongsted, J., Vester, B., Mutations in the bacterial ribosomal protein l3 and their association with antibiotic resistance. Antimicrob. Agents Chemother. 59 (2015), 3518–3528.
109. Kocagöz, T., Hackbarth, C.J., Unsal, I., Rosenberg, E.Y., Nikaido, H., Chambers, H.F., Gyrase mutations in laboratory-selected, fluoroquinolone-resistant mutants of Mycobacterium tuberculosis H37Ra. Antimicrob. Agents Chemother. 40 (1996), 1768–1774.
110. Konno, K., Feldmann, F.M., McDermott, W., Pyrazinamide susceptibility and amidase activity of tubercle bacilli. Am. Rev. Respir. Dis. 95 (1967), 461–469.
111. Köser, C.U., Bryant, J.M., Becq, J., Török, M.E., Ellington, M.J., Marti-Renom, M.A., Carmichael, A.J., Parkhill, J., Smith, G.P., Peacock, S.J., Whole-genome sequencing for rapid susceptibility testing of M. tuberculosis. N. Engl. J. Med. 369 (2013), 290–292.
112. Köser, C.U., Comas, I., Feuerriegel, S., Niemann, S., Gagneux, S., Peacock, S.J., Genetic diversity within Mycobacterium tuberculosis complex impacts on the accuracy of geno-typic pyrazinamide drug-susceptibility assay. Tuberculosis 94 (2014), 451–453.
113. Koul, A., Arnoult, E., Lounis, N., Guillemont, J., Andries, K., The challenge of new drug discovery for tuberculosis. Nature 469 (2011), 483–490.
114. Krieger, I.V., Freundlich, J.S., Gawandi, V.B., Roberts, J.P., Gawandi, V.B., Sun, Q., Owen, J.L., Fraile, M.T., Huss, S.I., Lavandera, J.L., Ioerger, T.R., Structure-guided discovery of phenyl-diketo acids as potent inhibitors of M. tuberculosis malate synthase. Chem. Biol. 19 (2012), 1556–1567.
115. Kumar, K., Awasthi, D., Lee, S.Y., Zanardi, I., Ruzsicska, B., Knudson, S., Tonge, P.J., Slayden, R.A., Ojima, I., Novel trisubstituted benzimidazoles, targeting Mtb FtsZ, as a new class of antitubercular agents. J. Med. Chem. 54 (2010), 374–381.
116. Larsen, M.H., Vilchèze, C., Kremer, L., Besra, G.S., Parsons, L., Salfinger, M., Heifets, L., Hazbon, M.H., Alland, D., Sacchettini, J.C., Jacobs, W.R., Overexpression of inhA, but not kasA, confers resistance to isoniazid and ethionamide in Mycobacterium smegmatis, M. bovis BCG and M. tuberculosis. Mol. Microbiol. 46 (2002), 453–466.
117. Lee, H., Cho, S.N., Bang, H.E., Lee, J.H., Bai, G.H., Kim, S.J., Kim, J.D., Exclusive mutations related to isoniazid and ethionamide resistance among Mycobacterium tuberculosis isolates from Korea. Int. J. Tuberc. Lung Dis. 4 (2000), 441–447.
118. Lee, M., Lee, J., Carroll, M.W., Choi, H., Min, S., Song, T., Via, L.E., Goldfeder, L.C., Kang, E., Jin, B., Park, H., Linezolid for treatment of chronic extensively drug-resistant tuberculosis. N. Engl. J. Med. 367 (2012), 1508–1518.
119. Lehmann, J., para-Aminosalicylic acid in the treatment of tuberculosis. Lancet 247 (1946), 15–16.
120. Lei, B., Wei, C.J., Tu, S.C., Action mechanism of antitubercular isoniazid. Activation by Mycobacterium tuberculosis KatG, isolation, and characterization of inhA inhibitor. J. Biol. Chem. 275 (2000), 2520–2526.
121. Lenaerts, A.J., Gruppo, V., Marietta, K.S., Johnson, C.M., Driscoll, D.K., Tompkins, N.M., Rose, J.D., Reynolds, R.C., Orme, I.M., Preclinical testing of the nitroimidazopyran Prm for activity against Mycobacterium tuberculosis in a series of in vitro and in vivo models. Antimicrob. Agents Chemother. 49 (2005), 2294–2301.
122. Lety, M.A., Nair, S., Berche, P., Escuyer, V., A single point mutation in the embB gene is responsible for resistance to ethambutol in Mycobacterium smegmatis. Antimicrob. Agents Chemother. 41 (1997), 2629–2633.
123. Leung, K.L., Yip, C.W., Yeung, Y.L., Wong, K.L., Chan, W.Y., Chan, M.Y., Kam, K.M., Usefulness of resistant gene markers for predicting treatment outcome on second-line anti-tuberculosis drugs. J. Appl. Microbiol. 109 (2010), 2087–2094.
124. Li, W., Upadhyay, A., Fontes, F.L., North, E.J., Wang, Y., Crans, D.C., Grzegorzewicz, A.E., Jones, V., Franzblau, S.G., Lee, R.E., Crick, D.C., Novel insights into the mechanism of inhibition of MmpL3, a target of multiple pharmacophores in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 58 (2014), 6413–6423.
125. Li, W., Xin, Y., McNeil, M.R., Ma, Y., rmlB and rmlC genes are essential for growth of mycobacteria. Biochem. Biophys. Res. Commun. 342 (2006), 170–178.
126. Long, Q., Li, W., Du, Q., Fu, Y., Liang, Q., Huang, H., Xie, J., gyrA/B fluoroquinolone resistance allele profiles amongst Mycobacterium tuberculosis isolates from mainland China. Int. J. Antimicrob. Agents 39 (2012), 486–489.
127. Lougheed, K.E., Osborne, S.A., Saxty, B., Whalley, D., Chapman, T., Bouloc, N., Chugh, J., Nott, T.J., Patel, D., Spivey, V.L., Kettleborough, C.A., Effective inhibitors of the essential kinase PknB and their potential as anti-mycobacterial agents. Tuberculosis 91 (2011), 277–286.
128. Ma, Y., Stern, R.J., Scherman, M.S., Vissa, V.D., Yan, W., Jones, V.C., Zhang, F., Franzblau, S.G., Lewis, W.H., McNeil, M.R., Drug targeting Mycobacterium tuberculosis cell wall synthesis: genetics of dTDP-rhamnose synthetic enzymes and development of a microtiter plate-based screen for inhibitors of conversion of dTDP-glucose to dTDP-rhamnose. Antimicrob. Agents Chemother. 45 (2001), 1407–1416.
129. Machado, D., Perdigão, J., Ramos, J., Couto, I., Portugal, I., Ritter, C., Boettger, E.C., Viveiros, M., High-level resistance to isoniazid and ethionamide in multidrug-resistant Mycobacterium tuberculosis of the Lisboa family is associated with inhA double mutations. J. Antimicrob. Chemother. 68 (2013), 1728–1732.
130. Makafe, G.G., Cao, Y., Tan, Y., Julius, M., Liu, Z., Wang, C., Njire, M.M., Cai, X., Liu, T., Wang, B., Pang, W., Oxazolidinone resistance in Mycobacterium tuberculosis: what is the role of cys154Arg mutation in the ribosomal protein L3?. Antimicrob. Agents Chemother. 60 (2016), 3202–3206.
131. Malik, S., Willby, M., Sikes, D., Tsodikov, O.V., Posey, J.E., New insights into fluoroquinolone resistance in Mycobacterium tuberculosis: functional genetic analysis of gyrA and gyrB mutations. PLoS One, 7, 2012, e39754.
132. Manjunatha, U., Boshoff, H.I., Barry, C.E., The mechanism of action of Prm: novel insights from transcriptional profiling. Comm. Integr. Bio. 2 (2009), 215–218.
133. Manjunatha, U.H., Boshoff, H., Dowd, C.S., Zhang, L., Albert, T.J., Norton, J.E., Daniels, L., Dick, T., Pang, S.S., Barry, C.E., Identification of a nitroimidazo-oxazine-specific protein involved in Prm resistance in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 103 (2006), 431–436.
134. Manten, A., Van Klingeren, B., Voogd, C.E., Meertens, M.G.P., D-cycloserine as a bactericidal drug; antagonism between D-cycloserine and the bacteriostatic antibiotics chloramphenicol and tetracycline. Chemotherapy 13 (1968), 242–248.
135. Maruri, F., Sterling, T.R., Kaiga, A.W., Blackman, A., van der Heijden, Y.F., Mayer, C., Cambau, E., Aubry, A., A systematic review of gyrase mutations associated with fluoroquinolone-resistant Mycobacterium tuberculosis and a proposed gyrase numbering system. J. Antimicrob. Chemother. 67 (2012), 819–831.
136. Maslov, D.A., Zaĭchikova, M.V., Chernousova, L.N., Shur, K.V., Bekker, O.B., Smirnova, T.G., Larionova, E.E., Andreevskaya, S.N., Zhang, Y., Danilenko, V.N., Resistance to pyrazinamide in Russian Mycobacterium tuberculosis isolates: pncA sequencing versus Bactec MGIT 960. Tuberculosis 95 (2015), 608–612.
137. Mathew, B., Ross, L., Reynolds, R.C., A novel quinoline derivative that inhibits mycobacterial FtsZ. Tuberculosis 93 (2013), 398–400.
138. Mathys, V., Wintjens, R., Lefevre, P., Bertout, J., Singhal, A., Kiass, M., Kurepina, N., Wang, X.M., Mathema, B., Baulard, A., Kreiswirth, B.N., Molecular genetics of para-aminosalicylic acid resistance in clinical isolates and spontaneous mutants of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 53 (2009), 2100–2109.
139. Matsumoto, M., Hashizume, H., Tomishige, T., Kawasaki, M., Tsubouchi, H., Sasaki, H., Shimokawa, Y., Komatsu, M., OPC-67683, a nitro-dihydro-imidazooxazole derivative with promising action against tuberculosis in vitro and in mice. PLoS Med., 3, 2006, e466.
140. Maus, C.E., Plikaytis, B.B., Shinnick, T.M., Molecular analysis of cross-resistance to capreomycin, kanamycin, amikacin, and viomycin in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 49 (2005), 3192–3197.
141. ® MTB/RIF in Kampala, Uganda: a retrospective study. BMC Infect. Dis., 14, 2014, 481.
142. Mdluli, K., Slayden, R.A., Zhu, Y., Ramaswamy, S., Pan, X., Mead, D., Crane, D.D., Musser, J.M., Barry, C.E., Inhibition of a Mycobacterium tuberculosis β-ketoacyl ACP synthase by isoniazid. Science 280 (1998), 1607–1610.
143. Merker, M., Kohl, T.A., Roetzer, A., Truebe, L., Richter, E., Rüsch-Gerdes, S., Fattorini, L., Oggioni, M.R., Cox, H., Varaine, F., Niemann, S., Whole genome sequencing reveals complex evolution patterns of multidrug-resistant Mycobacterium tuberculosis Beijing strains in patients. PLoS One, 8, 2013, e82551.
144. Meumann, E.M., Globan, M., Fyfe, J.A., Leslie, D., Porter, J.L., Seemann, T., Denholm, J., Stinear, T.P., Genome sequence comparisons of serial multi-drug-resistant Mycobacterium tuberculosis isolates over 21 years of infection in a single patient. Microb. Genom. 1 (2015), 1–9.
145. Middlebrook, G., Sterilization of tubercle bacilli by isonicotinic acid hydrazide and the incidence of variants resistant to the drug in vitro. Am. Rev. Tuberc. 65 (1952), 765–767.
146. Middlebrook, G., Isoniazid resistance and catalase activity of tubercle bacilli. Am. Rev. Tuberc. 69 (1954), 471–472.
147. Migliori, G.B., Dara, M., de Colombani, P., Kluge, H., Raviglione, M.C., Multidrug-resistant tuberculosis in Eastern Europe: still on the increase?. Eur. Respir. J. 39 (2012), 1290–1291.
148. Milano, A., Pasca, M.R., Provvedi, R., Lucarelli, A.P., Manina, G., Ribeiro, A.L.D.J.L., Manganelli, R., Riccardi, G., Azole resistance in Mycobacterium tuberculosis is mediated by the MmpS5-MmpL5 efflux system. Tuberculosis 89 (2009), 84–90.
149. Mitchison, D.A., The action of antituberculosis drugs in short-course chemotherapy. Tubercle 66 (1985), 219–225.
150. Moazed, D., Noller, H.F., Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327 (1987), 389–394.
151. Mokrousov, I., Otten, T., Manicheva, O., Potapova, Y., Vishnevsky, B., Narvskaya, O., Rastogi, N., Molecular characterization of ofloxacinresistant Mycobacterium tuberculosis strains from Russia. Antimicrob. Agents Chemother. 52 (2008), 2937–2939.
152. Mokrousov, I., Otten, T., Vyshnevskiy, B., Narvskaya, O., Detection of embB306 mutations in ethambutol-susceptible clinical isolates of Mycobacterium tuberculosis from Northwestern Russia: implications for genotypic resistance testing. J. Clin. Microbiol. 40 (2002), 3810–3813.
153. Mori, G., Chiarelli, L.R., Esposito, M., Makarov, V., Bellinzoni, M., Hartkoorn, R.C., Degiacomi, G., Boldrin, F., Ekins, S., Ribeiro, A.L.D.J.L., Marino, L.B., Thiophenecarboxamide derivatives activated by ethA kill Mycobacterium tuberculosis by inhibiting the CTP synthetase PyrG. Chem. Biol. 22 (2015), 917–927.
154. Mothiba, M.T., Anderson, R., Fourie, B., Germishuizen, W.A., Cholo, M.C., Effects of clofazimine on planktonic and biofilm growth of Mycobacterium tuberculosis and Mycobacterium smegmatis. J. Glob. Antimicrob. Res. 3 (2015), 13–18.
155. Moure, R., Español, M., Tudó, G., Vicente, E., Coll, P., Gonzalez-Martin, J., Mick, V., Salvadó, M., Alcaide, F., Characterization of the embB gene in Mycobacterium tuberculosis isolates from Barcelona and rapid detection of main mutations related to ethambutol resistance using a low-density DNA array. J. Antimicrob. Chemother. 69 (2014), 947–954.
156. Mukherjee, T., Boshoff, H., Nitroimidazoles for the treatment of TB: past, present and future. Future Med. Chem. 3 (2011), 1427–1454.
157. Müller, B., Streicher, E.M., Hoek, K.G.P., Tait, M., Trollip, A., Bosman, M.E., Coetzee, G.J., Chabula-Nxiweni, E.M., Hoosain, E., Gey van Pittius, N.C., Victor, T.C., inhA promoter mutations: a gateway to extensively drug-resistant tuberculosis in South Africa?. Int. J. Tuberc. Lung Dis. 15 (2011), 344–351.
158. Nair, J., Rouse, D.A., Bai, G.H., Morris, S.L., The rpsL gene and streptomycin resistance in single and multiple drug-resistant strains of Mycobacterium tuberculosis. Mol. Microbiol. 10 (1993), 521–527.
159. Njire, M., Tan, Y., Mugweru, J., Wang, C., Guo, J., Yew, W., Tan, S., Zhang, T., Pyrazinamide resistance in Mycobacterium tuberculosis: review and update. Adv. Med. Sci. 61 (2016), 63–71.
160. Nodieva, A., Jansone, I., Broka, L., Pole, I., Skenders, G., Baumanis, V., Recent nosocomial transmission and genotypes of multidrug-resistant Mycobacterium tuberculosis. Int. J. Tuberc. Lung Dis. 14 (2010), 427–433.
161. Nosova, E.Y., Bukatina, A.A., Isaeva, Y.D., Makarova, M.V., Galkina, K.Y., Moroz, A.M., Analysis of mutations in the gyrA and gyrB genes and their association with the resistance of Mycobacterium tuberculosis to levofloxacin, moxifloxacin and gatifloxacin. J. Med. Microbiol. 62 (2013), 108–113.
162. Ocheretina, O., Escuyer, V.E., Mabou, M.M., Royal-Mardi, G., Collins, S., Vilbrun, S.C., Pape, J.W., Fitzgerald, D.W., Correlation between genotypic and phenotypic testing for resistance to rifampin in Mycobacterium tuberculosis clinical isolates in Haiti: investigation of cases with discrepant susceptibility results. PLoS One, 9, 2014, e9056.
163. Okamoto, S., Tamaru, A., Nakajima, C., Nishimura, K., Tanaka, Y., Tokuyama, S., Suzuki, Y., Ochi, K., Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria. Mol. Microbiol. 63 (2007), 1096–1106.
164. Palomino, J.C., Martin, A., Tuberculosis clinical trial update and the current anti-tuberculosis drug portfolio. Curr. Med. Chem. 20 (2013), 3785–3796.
165. Pandey, B., Grover, S., Tyagi, C., Goyal, S., Jamal, S., Singh, A., Kaur, J., Grover, A., Molecular principles behind pyrazinamide resistance due to mutations in panD gene in Mycobacterium tuberculosis. Gene 581 (2016), 3–42.
166. Pantel, A., Petrella, S., Veziris, N., Brossier, F., Bastian, S., Jarlier, V., Mayer, C., Aubry, A., Extending the definition of the gyrB quinolone resistance determining region in Mycobacterium tuberculosis DNA gyrase for assessing fluoroquinolone resistance in M. tuberculosis. Antimicrob. Agents Chemother. 56 (2012), 1990–1996.
167. Parish, T., Roberts, G., Laval, F., Schaeffer, M., Daffé, M., Duncan, K., Functional complementation of the essential gene fabG1 of Mycobacterium tuberculosis by Mycobacterium smegmatis fabG but not Escherichia coli fabG. J. Bact. 189 (2007), 3721–3728.
168. Park, B., Awasthi, D., Chowdhury, S.R., Melief, E.H., Kumar, K., Knudson, S.E., Slayden, R.A., Ojima, I., Design, synthesis and evaluation of novel 2, 5, 6-trisubstituted benzimidazoles targeting FtsZ as antitubercular agents. Bioorg. Med. Chem. 22 (2014), 2602–2612.
169. Park, H.D., Guinn, K.M., Harrell, M.I., Liao, R., Voskuil, M.I., Tompa, M., Schoolnik, G.K., Sherman, D.R., Rv3133c/dosR is a transcription factor that mediates the hypoxic response of Mycobacterium tuberculosis. Mol. Microbiol. 48 (2003), 833–843.
170. Park, Y.K., Ryoo, S.W., Lee, S.H., Jnawali, H.N., Kim, C.K., Kim, H.J., Kim, S.J., Correlation of the phenotypic ethambutol susceptibility of Mycobacterium tuberculosis with embB gene mutations in Korea. J. Med. Microbiol. 61 (2012), 529–534.
171. Pawelczyk, J., Brzostek, A., Kremer, L., Dziadek, B., Rumijowska-Galewicz, A., Fiolka, M., Dziadek, J., AccD6, a key carboxyltransferase essential for mycolic acid synthesis in Mycobacterium tuberculosis, is dispensable in a nonpathogenic strain. J. Bacteriol. 193 (2011), 6960–6972.
172. Perdigão, J., Macedo, R., Malaquias, A., Ferreira, A., Brum, L., Portugal, I., Genetic analysis of extensively drug resistant Mycobacterium tuberculosis strains in Lisbon, Portugal. J. Antimicrob. Chemother. 65 (2010), 224–227.
173. Perdigão, J., Macedo, R., Ribeiro, A., Brum, L., Portugal, I., Genetic characterisation of the ethambutol resistance-determining region in Mycobacterium tuberculosis: prevalence and significance of embB306 mutations. Int. J. Antimicrob. Agents 33 (2009), 334–338.
174. Pethe, K., Bifani, P., Jang, J., Kang, S., Park, S., Ahn, S., Jiricek, J., Jung, J., Jeon, H.K., Cechetto, J., Christophe, T., Discovery of Q203, a potent clinical candidate for the treatment of tuberculosis. Nat. Med. 19 (2013), 1157–1160.
175. Petrella, S., Cambau, E., Chauffour, A., Andries, K., Jarlier, V., Sougakoff, W., Genetic basis for natural and acquired resistance to the diarylquinoline R207910 in mycobacteria. Antimicrob. Agents Chemother. 50 (2006), 2853–2856.
176. Piccaro, G., Pietraforte, D., Giannoni, F., Mustazzolu, A., Fattorini, L., Rifampin induces hydroxyl radical formation in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 58 (2014), 7527–7533.
177. Plinke, C., Cox, H.S., Zarkua, N., Karimovich, H.A., Braker, K., Diel, R., Rüsch-Gerdes, S., Feuerriegel, S., Niemann, S., embCAB sequence variation among ethambutol-resistant Mycobacterium tuberculosis isolates without embB306 mutation. J. Antimicrob. Chemother. 65 (2010), 1359–1367.
178. Prosser, G.A., de Carvalho, L.P., Metabolomics reveal d-alanine: d-alanine ligase as the target of d-cycloserine in Mycobacterium tuberculosis. ACS Med. Chem. Lett. 4 (2013), 1233–1237.
179. Protopopova, M., Hanrahan, C., Nikonenko, B., Samala, R., Chen, P., Gearhart, J., Einck, L., Nacy, C.A., Identification of a new antitubercular drug candidate, SQ109, from a combinatorial library of 1, 2-ethylenediamines. J. Antimicrob. Chemother. 56 (2005), 968–974.
180. Quemard, A., Sacchettini, J.C., Dessen, A., Vilcheze, C., Bittman, R., Jacobs, W.R. Jr., Blanchard, J.S., Enzymatic characterization of the target for isoniazid in Mycobacterium tuberculosis. Biochemistry 34 (1995), 8235–8241.
181. Rahim, Z., Nakajima, C., Raqib, R., Zaman, K., Endtz, H.P., van der Zanden, A.G., Suzuki, Y., Molecular mechanism of rifampicin and isoniazid resistance in Mycobacterium tuberculosis from Bangladesh. Tuberculosis 92 (2012), 529–534.
182. Ramaswamy, S., Musser, J.M., Molecular genetic basis of antimicrobial agent resistance in Mycobacterium tuberculosis: 1998 update. Tuber. Lung Dis. 79 (1998), 3–29.
183. Ramaswamy, S.V., Amin, A.G., Göksel, S., Stager, C.E., Dou, S.J., El Sahly, H., Moghazeh, S.L., Kreiswirth, B.N., Musser, J.M., Molecular genetic analysis of nucleotide polymorphisms associated with ethambutol resistance in human isolates of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 44 (2000), 326–336.
184. Reddy, V.M., Nadadhur, G., Daneluzzi, D., O'Sullivan, J.F., Gangadharam, P.R., Antituberculosis activities of clofazimine and its new analogs B4154 and B4157. Antimicrob. Agents Chemother. 40 (1996), 633–636.
185. Reeves, A.Z., Campbell, P.J., Sultana, R., Malik, S., Murray, M., Plikaytis, B.B., Shinnick, T.M., Posey, J.E., Aminoglycoside cross-resistance in Mycobacterium tuberculosis due to mutations in the 5′ untranslated region of whiB7. Antimicrob. Agents Chemother. 57 (2013), 1857–1865.
186. Ren, J.X., Qian, H.L., Huang, Y.X., Zhu, N.Y., Si, S.Y., Xie, Y., Virtual screening for the identification of novel inhibitors of Mycobacterium tuberculosis cell wall synthesis: inhibitors targeting RmlB and RmlC. Comput. Biol. Med. 58 (2015), 110–117.
187. Rengarajan, J., Sassetti, C.M., Naroditskaya, V., Sloutsky, A., Bloom, B.R., Rubin, E.J., The folate pathway is a target for resistance to the drug para-aminosalicylic acid (PAS) in mycobacteria. Mol. Microbiol. 53 (2004), 275–282.
188. Rozwarski, D.A., Grant, G.A., Barton, D.H., Jacobs, W.R., Sacchettini, J.C., Modification of the NADH of the isoniazid target (InhA) from Mycobacterium tuberculosis. Science 279 (1998), 98–102.
189. Safi, H., Lingaraju, S., Amin, A., Kim, S., Jones, M., Holmes, M., McNeil, M., Peterson, S.N., Chatterjee, D., Fleischmann, R., Alland, D., Evolution of high-level ethambutol-resistant tuberculosis through interacting mutations in decaprenylphosphoryl-[beta]-D-arabinose biosynthetic and utilization pathway genes. Nat. Genet. 45 (2013), 1190–1197.
190. Saier, M.H., Yen, M.R., Noto, K., Tamang, D.G., Elkan, C., The transporter classification database: recent advances. Nucleic Acids Res. 37 (2009), D274–D278.
191. Saint-Joanis, B., Souchon, H., Wilming, M., Johnsson, K., Alzari, P.M., Use of site-directed mutagenesis to probe the structure, function and isoniazid activation of the catalase/peroxidase, KatG, from Mycobacterium tuberculosis. Biochem. J. 338 (1999), 753–760.
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. 198 (2003), 693–704.
193. Scorpio, A., Zhang, Y., Mutations in pncA, a gene encoding pyrazinamidase/nicotinamidase, cause resistance to the antituberculous drug pyrazinamide in tubercle bacillus. Nat. Med. 2 (1996), 662–667.
194. Seifert, M., Catanzaro, D., Catanzaro, A., Rodwell, T.C., Genetic mutations associated with isoniazid resistance in Mycobacterium tuberculosis: a systematic review. PLoS One, 10, 2015, e0119628.
195. Sensi, P., History of the development of rifampin. Rev. Infect. Dis. 5 (1983), S402–S406.
196. Sharma, D., Cukras, A.R., Rogers, E.J., Southworth, D.R., Green, R., Mutational analysis of S12 protein and implications for the accuracy of decoding by the ribosome. J. Mol. Biol. 374 (2007), 1065–1076.
197. Shekar, S., Yeo, Z.X., Wong, J.C., Chan, M.K., Ong, D.C., Tongyoo, P., Wong, S.Y., Lee, A.S., Detecting novel genetic variants associated with isoniazid-resistant Mycobacterium tuberculosis. PLoS One, 9, 2014, e102383.
198. Shen, X., Shen, G.M., Wu, J., Gui, X.H., Li, X., Mei, J., DeRiemer, K., Gao, Q., Association between embB codon 306 mutations and drug resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 51 (2007), 2618–2620.
199. Shi, D., Li, L., Zhao, Y., Jia, Q., Li, H., Coulter, C., Jin, Q., Zhu, G., Characteristics of embB mutations in multidrug-resistant Mycobacterium tuberculosis isolates in Henan, China. J. Antimicrob. Chemother. 66 (2011), 2240–2247.
200. Shi, W., Chen, J., Feng, J., Cui, P., Zhang, S., Weng, X., Zhang, W., Zhang, Y., Aspartate decarboxylase (PanD) as a new target of pyrazinamide in Mycobacterium tuberculosis. Emerg. Microbes Infect., 3, 2014, e58.
201. Shimokawa, Y., Sasahara, K., Yoda, N., Mizuno, K., Umehara, K., Delamanid does not inhibit or induce cytochrome p450 enzymes in vitro. Biol. Pharm. Bull. 37 (2014), 1727–1735.
202. Singh, N., Tiwari, S., Srivastava, K.K., Siddiqi, M.I., Identification of novel inhibitors of Mycobacterium tuberculosis PknG using pharmacophore based virtual screening, docking, molecular dynamics simulation, and their biological evaluation. J. Chem. Inf. Model 55 (2015), 1120–1129.
203. Sirgel, F.A., Warren, R.M., Streicher, E.M., Victor, T.C., van Helden, P.D., Böttger, E.C., gyrA mutations and phenotypic susceptibility levels to ofloxacin and moxifloxacin in clinical isolates of Mycobacterium tuberculosis. J. Antimicrob. Chemother. 67 (2012), 1088–1093.
204. Siu, G.K.H., Yam, W.C., Zhang, Y., Kao, R.Y., An upstream truncation of the furA-katG operon confers high-level isoniazid resistance in a Mycobacterium tuberculosis clinical isolate with no known resistance-associated mutations. Antimicrob. Agents Chemother. 58 (2014), 6093–6100.
205. Siu, G.K.H., Zhang, Y., Lau, T.C., Lau, R.W., Ho, P.L., Yew, W.W., Tsui, S.K., Cheng, V.C., Yuen, K.Y., Yam, W.C., Mutations outside the rifampicin resistance-determining region associated with rifampicin resistance in Mycobacterium tuberculosis. J. Antimicrob. Chemother. 66 (2011), 730–733.
206. Smittipat, N., Juthayothin, T., Billamas, P., Jaitrong, S., Rukseree, K., Dokladda, K., Chaiyasirinroje, B., Disratthakit, A., Chaiprasert, A., Mahasirimongkol, S., Yanai, H., Mutations in rrs, rpsL and gidB in streptomycin-resistant Mycobacterium tuberculosis isolates from Thailand. J. Glob. Antimicrob. Resist. 4 (2016), 5–10.
207. Somoskovi, A., Dormandy, J., Mitsani, D., Rivenburg, J., Salfinger, M., Use of smear-positive samples to assess the PCR-based genotype MTBDR assay for rapid, direct detection of the Mycobacterium tuberculosis complex as well as its resistance to isoniazid and rifampin. J. Clin. Microbiol. 44 (2006), 4459–4463.
208. Sowajassatakul, A., Prammananan, T., Chaiprasert, A., Phunpruch, S., Molecular characterization of amikacin, kanamycin and capreomycin resistance in M/XDR-TB strains isolated in Thailand. BMC Microb., 14, 2014, 1.
209. Spies, F.S., Ribeiro, A.W., Ramos, D.F., Ribeiro, M.O., Martin, A., Palomino, J.C., Rossetti, M.L.R., da Silva, P.E.A., Zaha, A., Streptomycin resistance and lineage-specific polymorphisms in Mycobacterium tuberculosis gidB gene. J. Clin. Microbiol. 49 (2011), 2625–2630.
210. Sreevatsan, S., Stockbauer, K.E., Pan, X.I., Kreiswirth, B.N., Moghazeh, S.L., Jacobs, W.R., Telenti, A., Musser, J.M., Ethambutol resistance in Mycobacterium tuberculosis: critical role of embB mutations. Antimicrob. Agents Chemother. 41 (1997), 1677–1681.
211. Srivastava, S., Ayyagari, A., Dhole, T.N., Nyati, K.K., Dwivedi, S.K., Emb nucleotide polymorphisms and the role of embB306 mutations in Mycobacterium tuberculosis resistance to ethambutol. Int. J. Med. Microbiol. 299 (2009), 269–280.
212. Stanley, S.A., Kawate, T., Iwase, N., Shimizu, M., Clatworthy, A.E., Kazyanskaya, E., Sacchettini, J.C., Ioerger, T.R., Siddiqi, N.A., Minami, S., Aquadro, J.A., Diarylcoumarins inhibit mycolic acid biosynthesis and kill Mycobacterium tuberculosis by targeting FadD32. Proc. Natl. Acad. Sci. U. S. A. 110 (2013), 11565–11570.
213. Stover, C.K., Warrener, P., VanDevanter, D.R., Sherman, D.R., Arain, T.M., Langhorne, M.H., Anderson, S.W., Towell, J.A., Yuan, Y., McMurray, D.N., Kreiswirth, B.N., A small-molecule nitroimidazopyran drug candidate for the treatment of tuberculosis. Nature 405 (2000), 962–966.
214. Sun, H., Zhang, C., Xiang, L., Pi, R., Guo, Z., Zheng, C., Li, S., Zhao, Y., Tang, K., Luo, M., Rastogi, N., Characterization of mutations in streptomycin-resistant Mycobacterium tuberculosis isolates in Sichuan, China and the association between Beijing-lineage and dual-mutation in gidB. Tuberculosis 96 (2016), 102–106.
215. Suzuki, Y., Katsukawa, C., Tamaru, A., Abe, C., Makino, M., Mizuguchi, Y., Taniguchi, H., Detection of kanamycin-resistant Mycobacterium tuberculosis by identifying mutations in the 16S rRNA gene. J. Clin. Microbiol. 36 (1998), 1220–1225.
216. Swindells, S., New drugs to treat tuberculosis. F1000. Med. Rep., 4, 2012, 12.
217. Tahlan, K., Wilson, R., Kastrinsky, D.B., Arora, K., Nair, V., Fischer, E., Barnes, S.W., Walker, J.R., Alland, D., Barry, C.E., Boshoff, H.I., SQ109 targets MmpL3, a membrane transporter of trehalose monomycolate involved in mycolic acid donation to the cell wall core of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 56 (2012), 1797–1809.
218. Takayama, K., Kilburn, J.O., Inhibition of synthesis of arabinogalactan by ethambutol in Mycobacterium smegmatis. Antimicrob. Agents Chemother. 33 (1989), 1493–1499.
219. Takayama, K., Wang, L., David, H.L., Effect of isoniazid on the in vivo mycolic acid synthesis, cell growth, and viability of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 2 (1972), 29–35.
220. Takiff, H.E., Feo, O., Clinical value of whole-genome sequencing of Mycobacterium tuberculosis. Lancet Infect. Dis. 15 (2015), 1077–1090.
221. Takiff, H.E., Salazar, L., Guerrero, C., Philipp, W., Huang, W.M., Kreiswirth, B., Cole, S.T., Jacobs, W.R., Telenti, A., Cloning and nucleotide sequence of Mycobacterium tuberculosis gyrA and gyrB genes and detection of quinolone resistance mutations. Antimicrob. Agents Chemother. 38 (1994), 773–780.
222. Tan, Y., Hu, Z., Zhang, T., Cai, X., Kuang, H., Liu, Y., Chen, J., Yang, F., Zhang, K., Tan, S., Zhao, Y., Role of pncA and rpsA gene sequencing in detection of pyrazinamide resistance in Mycobacterium tuberculosis isolates from Southern China. J. Clin. Microbiol. 52 (2014), 291–297.
223. Tan, Y., Hu, Z., Zhao, Y., Cai, X., Luo, C., Zou, C., Liu, X., The beginning of the rpoB gene in addition to the rifampin resistance determination region might be needed for identifying rifampin/rifabutin cross-resistance in multidrug-resistant Mycobacterium tuberculosis isolates from Southern China. J. Clin. Microbiol. 50 (2012), 81–85.
224. Tasneen, R., Williams, K., Amoabeng, O., Minkowski, A., Mdluli, K.E., Upton, A.M., Nuermberger, E.L., Contribution of the nitroimidazoles Prm and TBA-354 to the activity of novel regimens in murine models of tuberculosis. Antimicrob. Agents Chemother. 59 (2015), 129–135.
225. Telenti, A., Imboden, P., Marchesi, F., Schmidheini, T., Bodmer, T., Direct, automated detection of rifampin-resistant Mycobacterium tuberculosis by polymerase chain reaction and single-strand conformation polymorphism analysis. Antimicrob. Agents Chemother. 37 (1993), 2054–2058.
226. Telenti, A., Philipp, W.J., Sreevatsan, S., Bernasconi, C., Stockbauer, K.E., Wieles, B., Musser, J.M., Jacobs, W.R., The emb operon, a unique gene cluster of Mycobacterium tuberculosis involved in resistance to ethambutol. Nat. Med. 3 (1997), 567–570.
227. Thee, S., Garcia-Prats, A.J., Donald, P.R., Hesseling, A.C., Schaaf, H.S., A review of the use of ethionamide and prothionamide in childhood tuberculosis. Tuberculosis 97 (2016), 126–136.
228. Thirumurugan, R., Kathirvel, M., Vallayyachari, K., Surendar, K., Samrot, A.V., Muthaiah, M., Molecular analysis of rpoB gene mutations in rifampicin resistant Mycobacterium tuberculosis isolates by multiple allele specific polymerase chain reaction in Puducherry, South India. J. Infect. Pub. Health 8 (2015), 619–625.
229. Tomioka, H., Namba, K., Development of antituberculous drugs: current status and future prospects. Kekkaku Tuberc. 81 (2006), 753–774.
230. Tyagi, S., Ammerman, N.C., Li, S.Y., Adamson, J., Converse, P.J., Swanson, R.V., Almeida, D.V., Grosset, J.H., Clofazimine shortens the duration of the first-line treatment regimen for experimental chemotherapy of tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), 869–874.
231. Udwadia, Z.F., Sen, T., Moharil, G., Assessment of linezolid efficacy and safety in MDR- and XDR-TB: an Indian perspective. Eur. Respir. J. 35 (2010), 936–938.
232. Umezawa, H., Ueda, M., Maeda, K., Yagishita, K., Kondo, S., Okami, Y., Utahara, R., Osato, Y., Nitta, K., Takeuchi, T., Production and isolation of a new antibiotic: kanamycin. J. Antibiot., 10, 1957, 181.
233. Unissa, A.N., Sudha, S., Selvakumar, N., Hassan, S., Binding of activated isoniazid with acetyl-CoA carboxylase from Mycobacterium tuberculosis. Bioinformation, 7, 2011, 107.
234. Valafar, F., Ramirez-Busby, S.M., Torres, J., Paul, L.V., Rodwell, T.C., Victor, T.C., Rodrigues, C., Gler, M.T., Crudu, V., Catanzaro, T., Prognostic significance of novel katG mutations in Mycobacterium tuberculosis. Int. J. Mycobacteriol. 4 (2015), 51–52.
235. Van Deun, A., Maug, A.K.J., Salim, M.A.H., Das, P.K., Sarker, M.R., Daru, P., Rieder, H.L., Short, highly effective, and inexpensive standardized treatment of multidrug-resistant tuberculosis. Am. J. Respir. Crit. Care Med. 182 (2010), 684–692.
236. Van Deun, A., Aung, K.J.M., Hossain, A., De Rijk, P., Gumusboga, M., Rigouts, L., de Jong, B.C., Disputed rpoB mutations can frequently cause important rifampicin resistance among new tuberculosis patients. Int. J. Tuberc. Lung Dis. 19 (2015), 185–190.
237. Vannelli, T.A., Dykman, A., de Montellano, P.R.O., The antituberculosis drug ethionamide is activated by a flavoprotein monooxygenase. J. Biol. Chem. 277 (2002), 12824–12829.
238. Vaubourgeix, J., Bardou, F., Boissier, F., Julien, S., Constant, P., Ploux, O., Daffé, M., Quémard, A., Mourey, L., S-Adenosyl-N-decyl-aminoethyl, a potent bisubstrate inhibitor of Mycobacterium tuberculosis mycolic acid methyltransferases. J. Biol. Chem. 284 (2009), 19321–19330.
239. Via, L.E., Cho, S.N., Hwang, S., Bang, H., Park, S.K., Kang, H.S., Jeon, D., Min, S.Y., Oh, T., Kim, Y., Kim, Y.M., Polymorphisms associated with resistance and cross-resistance to aminoglycosides and capreomycin in Mycobacterium tuberculosis isolates from South Korean patients with drug-resistant tuberculosis. J. Clin. Microbiol. 48 (2010), 402–411.
240. Vilchèze, C., Jacobs, W.R. Jr., Resistance to isoniazid and ethionamide in Mycobacterium tuberculosis: genes, mutations, and causalities. Microbiol. Spectr. 2 (2014), 1–21.
241. Vilchèze, C., Jacobs, W.R. Jr., The mechanism of isoniazid killing: clarity through the scope of genetics. Annu. Rev. Microbiol. 61 (2007), 35–50.
242. Vilchèze, C., Wang, F., Arai, M., Hazbón, M.H., Colangeli, R., Kremer, L., Weisbrod, T.R., Alland, D., Sacchettini, J.C., Jacobs, W.R., Transfer of a point mutation in Mycobacterium tuberculosis inhA resolves the target of isoniazid. Nat. Med. 12 (2006), 1027–1029.
243. Villemagne, B., Crauste, C., Flipo, M., Baulard, A.R., Déprez, B., Willand, N., Tuberculosis: the drug development pipeline at a glance. Eur. J. Med. Chem. 51 (2012), 1–16.
244. Wade, M.M., Zhang, Y., Mechanisms of drug resistance in Mycobacterium tuberculosis. Front. Biosci. 9 (2004), 975–994.
245. Wagenlehner, F.M.E., Naber, K.G., Fluoroquinolone antimicrobial agents in the treatment of prostatitis and recurrent urinary tract infections in men. Curr. Infect. Dis. Rep. 7 (2005), 9–16.
246. Walker, T.M., Kohl, T.A., Omar, S.V., Hedge, J., Elias, C.D.O., Bradley, P., Iqbal, Z., Feuerriegel, S., Niehaus, K.E., Wilson, D.J., Clifton, D.A., Whole-genome sequencing for prediction of Mycobacterium tuberculosis drug susceptibility and resistance: a retrospective cohort study. Lancet Infect. Dis. 15 (2015), 1193–1202.
247. Wengenack, N.L., Uhl, J.R., Amand, A.L.S., Tomlinson, A.J., Benson, L.M., Naylor, S., Kline, B.C., Cockerill, F.R., Rusnak, F., Recombinant Mycobacterium tuberculosis KatG (S315T) is a competent catalase-peroxidase with reduced activity toward isoniazid. J. Infect. Dis. 176 (1997), 722–727.
248. Wilming, M., Johnsson, K., Spontaneous formation of the bioactive form of the tuberculosis drug isoniazid. Angew. Chem. Int. Ed. Engl. 38 (1999), 2588–2590.
249. Wilson, R., Kumar, P., Parashar, V., Vilchèze, C., Veyron-Churlet, R., Freundlich, J.S., Barnes, S.W., Walker, J.R., Szymonifka, M.J., Marchiano, E., Shenai, S., Antituberculosis thiophenes define a requirement for Pks13 in mycolic acid biosynthesis. Nat. Chem. Biol. 9 (2013), 499–506.
250. Wilson, T.M., Collins, D.M., ahpC, a gene involved inisoniazid resistance of the Mycobacterium tuberculosis complex. Mol. Microbiol. 19 (1996), 1025–1034.
251. Winder, F.G., Collins, P.B., Inhibition by isoniazid of synthesis of mycolic acids in Mycobacterium tuberculosis. J. Gen. Microbiol. 63 (1970), 41–48.
252. Witney, A.A., Gould, K.A., Arnold, A., Coleman, D., Delgado, R., Dhillon, J., Pond, M.J., Pope, C.F., Planche, T.D., Stoker, N.G., Cosgrove, C.A., Clinical application of whole-genome sequencing to inform treatment for multidrug-resistant tuberculosis cases. J. Clin. Microbiol. 53 (2015), 1473–1483.
253. Wolucka, B.A., McNeil, M.R., de Hoffmann, E., Chojnacki, T., Brennan, P.J., Recognition of the lipid intermediate for arabinogalactan/arabinomannan biosynthesis and its relation to the mode of action of ethambutol on mycobacteria. J. Biol. Chem. 269 (1994), 23328–23335.
254. Wong, S.Y., Lee, J.S., Kwak, H.K., Via, L.E., Boshoff, H.I., Barry, C.E., Mutations in gidB confer low level streptomycin resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 55 (2011), 2515–2522.
255. WHO, Global Tuberculosis Report 2015., 2015, Switzerland, Geneva.
256. Xia, Q., Zhao, L.L., Li, F., Fan, Y.M., Chen, Y.Y., Wu, B.B., Liu, Z.W., Pan, A.Z., Zhu, M., Phenotypic and genotypic characterization of pyrazinamide resistance among multidrug-resistant Mycobacterium tuberculosis isolates in Zhejiang, China. Antimicrob. Agents Chemother. 59 (2015), 1690–1695.
257. Xu, P., Wu, J., Yang, C., Luo, T., Shen, X., Zhang, Y., Nsofor, C.A., Zhu, G., Gicquel, B., Gao, Q., Prevalence and transmission of pyrazinamide resistant Mycobacterium tuberculosis in China. Tuberculosis 98 (2016), 56–61.
258. Yadav, R., Sethi, S., Dhatwalia, S.K., Gupta, D., Mewara, A., Sharma, M., Molecular characterization of drug resistance in Mycobacterium tuberculosis isolates from North India. Int. J. Tuberc. Lung Dis. 17 (2013), 251–257.
259. Yeager, R.L., Munroe, W.G.C., Dessau, F.I., Pyrazinamide (aldinamide) in the treatment of pulmonary tuberculosis. Am. Rev. Tuberc. Pulmon. Dis. 65 (1952), 523–546.
260. Yoon, J.H., Nam, J.S., Kim, K.J., Ro, Y.T., Simple and rapid discrimination of embB codon 306 mutations in Mycobacterium tuberculosis clinical isolates by a real-time PCR assay using an LNA-TaqMan probe. J. Microbiol. Methods 92 (2013), 301–306.
261. Yuan, X., Zhang, T., Kawakami, K., Zhu, J., Li, H., Lei, J., Tu, S., Molecular characterization of multidrug- and extensively drug-resistant Mycobacterium tuberculosis strains in Jiangxi, China. J. Clin. Microbiol. 50 (2012), 2404–2413.
262. Zaunbrecher, M.A., Sikes, R.D., Metchock, B., Shinnick, T.M., Posey, J.E., Overexpression of the chromosomally encoded aminoglycoside acetyltransferase eis confers kanamycin resistance in Mycobacterium tuberculosis. Proc. Natl. Acad. Sci. U. S. A. 106 (2009), 20004–20009.
263. Zhang, N., Torrelles, J.B., McNeil, M.R., Escuyer, V.E., Khoo, K.H., Brennan, P.J., Chatterjee, D., The Emb proteins of mycobacteria direct arabinosylation of lipoarabinomannan and arabinogalactan via an N-terminal recognition region and a C-terminal synthetic region. Mol. Microbiol. 50 (2003), 69–76.
264. Zhang, Q., Wan, B., Zhou, A., Ni, J., Xu, Z., Li, S., Tao, J., Yao, Y., Whole genome analysis of an MDR Beijing/W strain of Mycobacterium tuberculosis with large genomic deletions associated with resistance to isoniazid. Gene 582 (2016), 128–136.
265. Zhang, S., Chen, J., Shi, W., Liu, W., Zhang, W., Zhang, Y., Mutations in panD encoding aspartate decarboxylase are associated with pyrazinamide resistance in Mycobacterium tuberculosis. Emerg. Microbes Infect., 2, 2013, e34.
266. Zhang, S., Chen, J., Cui, P., Shi, W., Shi, X., Niu, H., Chan, D., Yew, W.W., Zhang, W., Zhang, Y., Mycobacterium tuberculosis mutations associated with reduced susceptibility to linezolid. Antimicrob. Agents Chemother. 60 (2016), 2542–2544.
267. Zhang, S., Chen, J., Cui, P., Shi, W., Zhang, W., Zhang, Y., Identification of novel mutations associated with clofazimine resistance in Mycobacterium tuberculosis. J. Antimicrob. Chemother. 70 (2015), 2507–2510.
268. Zhang, Y., Heym, B., Allen, B., Young, D., Cole, S., The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358 (1992), 591–593.
269. Zhang, Y., Vilcheze, C., Jacobs, W.R., Mechanism of drug resistance in Micobacterium tuberculosis. Cole, S.T., Eisenach, K.D., McMurray, D.N., Jacobs, W.R. Jr., (eds.) Tuberculosis and the Tubercle Bacillus, 2005, ASM press, Washington DC, 115–140.
270. Zhang, Y., Yew, W.W., Mechanisms of drug resistance in Mycobacterium tuberculosis. Int. J. Tuberc. Lung Dis. 13 (2009), 1320–1330.
271. Zhang, Y., Yew, W.W., Mechanisms of drug resistance in Mycobacterium tuberculosis: update 2015. Int. J. Tuberc. Lung Dis. 19 (2015), 1276–1289.
272. Zhang, Z., Pang, Y., Wang, Y., Liu, C., Zhao, Y., Beijing genotype of Mycobacterium tuberculosis is significantly associated with linezolid resistance in multidrug-resistant and extensively drug-resistant tuberculosis in China. Int. J. Antimicrob. Agents 43 (2014), 231–235.
273. Zhang, Z., Wang, Y., Pang, Y., Kam, K.M., Ethambutol resistance as determined by broth dilution method correlates better than sequencing results with embB mutations in multidrug-resistant Mycobacterium tuberculosis isolates. J. Clin. Microbiol. 52 (2014), 638–641.
274. Zhao, F., Wang, X.D., Erber, L.N., Luo, M., Guo, A.Z., Yang, S.S., Gu, J., Turman, B.J., Gao, Y.R., Li, D.F., Cui, Z.Q., Binding pocket alterations in dihydrofolate synthase confer resistance to para-aminosalicylic acid in clinical isolates of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 58 (2014), 1479–1487.
275. Zhao, L.L., Sun, Q., Liu, H.C., Wu, X.C., Xiao, T.Y., Zhao, X.Q., Li, G.L., Jiang, Y., Zeng, C.Y., Wan, K.L., Analysis of embCAB mutations associated with ethambutol resistance in multidrug-resistant Mycobacterium tuberculosis isolates from China. Antimicrob. Agents Chemother. 59 (2015), 2045–2050.
276. Zhao, Y., Xu, S., Wang, L., Chin, D.P., Wang, S., Jiang, G., Xia, H., Zhou, Y., Li, Q., Ou, X., Pang, Y., National survey of drug-resistant tuberculosis in China. N. Engl. J. Med. 366 (2012), 2161–2170.
277. Zheng, J., Rubin, E.J., Bifani, P., Mathys, V., Lim, V., Au, M., Jang, J., Nam, J., Dick, T., Walker, J.R., Pethe, K., para-Aminosalicylic acid is a prodrug targeting dihydrofolate reductase in Mycobacterium tuberculosis. J. Biol. Chem. 288 (2013), 23447–23456.
278. Zhu, M., Namdar, R., Stambaugh, J.J., Starke, J.R., Bulpitt, A.E., Berning, S.E., Peloquin, C.A., Population pharmacokinetics of ethionamide in patients with tuberculosis. Tuberculosis 82 (2002), 91–96.