In Vitro and In Vivo Activities of Acylated Derivatives of Isoniazid Against Mycobacterium Tuberculosis

References

• Barry, C. E., III. (2003). Modern drug development. Issues Infect. Dis., 2(Mycobacteria and TB), 137–150.
   Google Scholar
• World Health Organization. (1994). TB: A global emergency. WHO Report No. 14977. Geneva, Switzerland.
   Google Scholar
• Ramaswamy, S., Reich, R., Dou, S.-J., Jasperse, L., Pan, X., Wanger, A., Quitugua, T., and Graviss, E. (2003). Single nucleotide polymorphisms in genes associated with isoniazid resistance in Mycobacterium tuberculosis. Antimicrob. Agents Chemother., 47, 1241–1250.
   PubMed Web of Science ®Google Scholar
• Youatt, J. (1958). The uptake of isoniazid by washed cell suspensions of mycobacteria and other organisms. Aust. J. Exp. Biol., 36, 223–233.
   PubMedGoogle Scholar
• Bardou, F., Raynaud, C., Ramos, C., Laneelle, M., and Laneelle, G. (1998). Mechanism of isoniazid uptake in Mycobacterium tuberculosis. Microbiology, 144, 2539–2544.
   PubMed Web of Science ®Google Scholar
• Crema, A., Baroli, F., and Ferrero, E. (1955). Ricerche sul metabolismo dell'idrazide dell'acido isonicotinico. Boll. Soc. Ital. Biol. Sper., 31, 244–246.
   Google Scholar
• Iwainsky, H. (1988). Mode of action, biotransformation and pharmacokinetics in Antituberculosis Drugs, edited by K. Bartmann, New York: Springer-Verlag, pp. 489–490.
   Google Scholar
• Krueger-Thiemer, E. (1957). Biochemie des isoniazids in Tuberkulose-forschungsinstitut Borstel Jahresbericht 1956- 1957, edited by E. Freerksen, Berlin: Springer-Verlag, pp. 331ff.
   Google Scholar
• Miesel, L., Rozwarski, D., Sacchettini, J., and Jacobs, W. (1998). Mechanisms for isoniazid action and resistance in Genetics and Tuberculosis, Novartis Foundation Symposia, edited by D. Chadwick, Chichester, England: John Wiley and Sons, Limited, Vol. 217, pp. 209–227.
   Google Scholar
• Peloquin, C. (1993). Pharmacology of the antimycobacterial drugs. Med. Clin. N. Am., 77, 1253–1262.
   PubMed Web of Science ®Google Scholar
• Pfaffenberg, R., Iwainsky, H., Jaehler, H., and Siegel, D. (1960). Ueber den stoffwechsel des isonicotinsaeurehydrazid (inh) und der alpha-ketosaeuren bei tuberkuloesen diabetikern. Beitraege zur Klinik der Tuberkulose, 123,63-71.
   Google Scholar
• Youatt, J. (1958). Metabolism of isoniazid by Mycobacterium tuberculosis BCG with reference to current theories of the mode of action. Am. Rev. Tuberc., 78, 806–809.
   PubMedGoogle Scholar
• Youatt, J. (1960). The uptake of isoniazid and related compounds by mycobacteria. Aust. J. Exp. Biol. Med. Sci., 38, 331–337.
   PubMedGoogle Scholar
• Youatt, J., and Tham, S. H. (1969). An enzyme system of Mycobacterium tuberculosis that reacts specifically with isoniazid. I. Am. Rev. Respir. Dis., 100,25-30.
   Google Scholar
• Youatt, J., and Tham, S. H. (1969). An enzyme system of Mycobacterium tuberculosis that reacts specifically with isoniazid. II. Correlation of this reaction with the binding and metabolism of isoniazid. Am. Rev. Respir. Dis., 100, 31–37.
   PubMed Web of Science ®Google Scholar
• Rozwarski, D., Grant, G., Barton, D., Jacobs, W., and Sacchettini, J. (1998). Modification of the nadh of the isoniazid target (inhA) from Mycobacterium tuberculosis. Science, 279,98-102.
   Web of Science ®Google Scholar
• Rozwarski, D., Vilcheze, C., Sugantino, M., Bittman, R., and Sacchettini, J. (1999). Crystal structure of the Mycobacterium tuberculosis enoyl-acp reductase, inhA, in complex with nad+ and a C16 fatty acyl substrate. J. Biol. Chem., 274, 15582–15589.
   PubMed Web of Science ®Google Scholar
• Mdluli, K., Sherman, D., Hickey, M., Kreisworth, B., Morris, S., Stover, C., and Barry, C. (1996). Biochemical and genetic data suggest that inhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis. J. Infect. Dis., 174, 1085–1090.
   Google Scholar
• Mdluli, K., Slayden, R., Zhu, Y., Ramaswamy, S., Pan, X., Mead, D., Crane, D., Musser, J., and Barry, C. (1998). Inhibition of a Mycobacterium tuberculosis?-ketoacyl acp synthase by isoniazid. Science, 280, 1607–1610.
   PubMed Web of Science ®Google Scholar
• Payton, M., Auty, R., Delgoda, R., Everett, M., and Sim, E. (1999). Cloning and characterization of arylamine N-acetyltransferase genes from Mycobacterium smegmatis and Mycobacterium tuberculosis: Increased expression results in isoniazid resistance. J. Bacteriol., 181, 1343–1347.
   PubMed Web of Science ®Google Scholar
• Upton, A., Johnson, N., Sandy, J., and Sim, E. (2001). Arylamine N-acetyltransferases-of mice, men and microorganisms. Trends Pharmacol. Sci., 22, 140–146.
   PubMed Web of Science ®Google Scholar
• Upton, A., Mushtaq, A., Victor, T., Sampson, S., Sandy, J., Smith, D., van Helden, P., and Sim, E. (2001). Arylamine N-acetyltransferase of Mycobacterium tuberculosis is a polymorphic enzyme and a site of isoniazid metabolism. Mol. Micro-biol., 42, 309–317.
   PubMed Web of Science ®Google Scholar
• Sandy, J., Mushtaq, A., Kawamura, A., Sinclair, J., Sim, E., and Noble, M. (2002). The structure of arylamine N-acetyltransferase from Mycobacterium smegmatis-an enzyme which inactivates the anti-tubercular drug, isoniazid. J. Mol. Biol., 318, 1071–1083.
   PubMed Web of Science ®Google Scholar
• Payton, M., Gifford, C., Schartau, P., Hagemeier, C., Mushtaq, A., Lucas, S., Pinter, K., and Sim, E. (2001). Evidence towards the role of arylamine N-acetyltransferase in Mycobacterium smegmatis and development of a specific antiserum of Mycobacterium tuberculosis. Microbiology, 147, 3295- 3302.
   Google Scholar
• Kawamura, A., Sandy, J., Upton, A., Noble, M., and Sim, E. (2003). Structural investigation of mutant Mycobacterium smegmatis arylamine N-acetyltransferase: A model for a naturally occurring functional polymorphism in Mycobacterium tuberculosis arylamine N-acetyltransferase. Protein Expr. Purif., 27,75-84.
   Web of Science ®Google Scholar
• Hearn, M. J. (2001). Antimycobacterial Compounds and Method for Making the Same. International Patent Application WO 02/43668.
   Google Scholar
• Smith, P. A. S. (1983). Derivatives of Hydrazine and Other Hydronitrogens Having N N Bonds. Reading, MA: The Benjamin-Cummings Publishing Company, p. 89.
   Google Scholar
• Augustynowicz-Kopec, E., and Zwolska, Z. (2002). The type of isoniazid acetylation in tuberculosis patients treated at national tuberculosis and lung diseases research institute. Acta Poloniae Pharmaceutica, 59, 443–447.
   PubMedGoogle Scholar
• American Chemical Society. (2002). SciFinder Scholar.
   Google Scholar
• Vestal, A. L. (1969). Procedures for the isolation and identification of mycobacteria. Laboratory Division, National Communicable Disease Center, Atlanta, GA: Public Health Service publication no. 1995, pp. 113–115.
   Google Scholar
• Wong, C. S., Palmer, G., and Cynamon, M. (1988). in vitro susceptibility of Mycobacterium tuberculosis, Mycobacterium bovis, and Mycobacterium kansasii to amoxycillin and ticarcillin in combination with clavulanic acid. J. Antimicrob. Chemother., 22, 863–866.
   PubMed Web of Science ®Google Scholar
• Tuberculosis Antimicrobial Acquisition and Coordinating Facility. 1999. Online at http://www.taacf.org/.
   Google Scholar
• Kakimoto, S., and Tone, I. (1965). Antituberculous compounds. XXIII. Alkyl- and acyl-substituted isonicotinic acid hydrazide. J. Med. Chem., 8, 868.
   PubMedGoogle Scholar
• Bernstein, J., Lott, W., Steinberg, B., and Yale, H. (1952). Chemotherapy of experimental tuberculosis. Am. Rev. Tuberc., 65, 357–364.
   PubMedGoogle Scholar
• Nodzu, R., Watanabe, H., Kuwata, S., and Yokoyama, S. (1960). Chemotherapy of tuberculosis. XII. Bacteriostatic action of isonicotinic acid acylhydrazide against Mycobacterium tuberculosis. Chemotherapy (Tokyo), 8, 368.
   Google Scholar
• Rastogi, N., and Goh, K. (1990). Action of 1-isonicotinoyl-2-palmitoyl hydrazine against the Mycobacterium avium complex and enhancement of its activity by m-fluorophenylalanine. Antimicrob. Agents Chemother., 34, 2061–2064.
   PubMed Web of Science ®Google Scholar
• Evans, D. A. Price, Manley, K. A., and McKusick, V. A. (1960). Genetic control of isoniazid metabolism in man. BMJ, 5197, 485–491.
   Google Scholar
• Nelson, S. D., Mitchell, J., Timbrell, J., Snodgrass, W., and Corcoran, G., III. (1976). Isoniazid and iproniazid: Activation of metabolites to toxic intermediates in man and rat. Science, 193, 901–903.
   PubMed Web of Science ®Google Scholar
• Selkon, J., Fox, W., Gangadharam, P., Ramachandran, K., Ramakrishnan, C., and Velu, S. (1961). Rate of inactivation of isoniazid in south Indian patients with pulmonary tuberculosis-2. Clinical implications in the treatment of pulmonary tuberculosis with isoniazid either alone or in combination with PAS. Bull. W.H.O., 25, 779–792.
   PubMed Web of Science ®Google Scholar
• Sim, E. (2002). Pharmacogenomics of arylamine N-acetyl transferases-from drug metabolism to drug discovery. Pharmacogenomics, 3, 729–731.
   PubMed Web of Science ®Google Scholar
• Kakemi, K., Arita, T., Sezaki, H., and Nakano, M. (1963). Absorption and excretion of drugs. XVI. Inhibition of isoniazid acetylation by p-aminobenzaldehyde and its related compounds. Jpn. J. Pharmacol., 83, 260–263.
   Google Scholar
• Vitolo, A. (1963). The role of acetylation in the effectiveness of treatment with combined isoniazid and para-aminosalicylic acid, and isoniazid with para-aminobenzoic acid, in pulmonary tuberculosis. Bull. Sci. Med. (Bologna), 135, 396- 402.
   Google Scholar
• Selkon, J., Devadatta, S., Kulkarni, K., Mitchison, D., Narayana, A., Narayana, N., and Ramachandran, K. (1964). The emergence of isoniazid-resistant cultures in patients with pulmonary tuberculosis during treatment with isoniazid alone or isoniazid plus PAS. Bull. W.H.O., 31, 273- 294.
   PubMed Web of Science ®Google Scholar