ahpC, a gene involved in isoniazid resistance of the Mycobacterium tuberculosis complex

Molecular Microbiology

Volumn 19, Issue 5, 1996, Pages 1025-1034

  Wilson, Theresa M ^a   Collins, Desmond M ^a  

^a AGRESEARCH   (New Zealand)

Author keywords

[No Author keywords available]

Indexed keywords

ALKYL HYDROPEROXIDE REDUCTASE; ENZYME; ISONIAZID; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANTIBIOTIC RESISTANCE; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; GENE EXPRESSION REGULATION; GENE MUTATION; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION;

EID: 0029915633     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1996.449980.x     Document Type: Article

References (48)

1. Banerjee, A., Dubnau, E., Quemard, A., Balasubramanian, V., Sun Um, K., Wilson, T., Collins, D., de Lisle, G., and Jacobs, Jr, W.R. (1994) inhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 263: 227-230.
2. Bardwell, J.C.A., McGovern, K., and Beckwith, J. (1991) Identification of a protein required for disulphide bond formation in vivo. Cell 67: 581-589.
3. Barletta, R.G., Kim, D.D., Snapper, S.B., Bloom, B.R., and Jacobs, Jr, W.R. (1992) Identification of expression signals of the mycobacteriophages Bxb1, L1 and TM4 using the Escherichia-Mycobacterium shuttle plasmids pYUB75 and pYUB76 designed to create translational fusions to the lacZ gene. J Gen Microbiol 138: 23-30.
4. Beaman, L., and Beaman, B.L. (1984) The role of oxygen and its derivatives in microbial pathogenesis and host defense. Annu Rev Microbiol 38: 27-48.
5. Belisle, J.T., Pascopella, L., Inamine, J.M., Brennan, P.J., and Jacobs, W.R. (1991) Isolation and expression of a gene cluster responsible for biosynthesis of the glycopeptidolipid antigens of Mycobacterium avium. J Bacteriol 173: 6991-6997.
6. Bergh, S., and Cole, S.T. (1994) MycDB: an integrated mycobacterial database. Mol Microbiol 12: 517-534.
7. Bergler, H., Wallner, P., Ebeling, A., Leitinger, B., Fuchsbichler, S., Aschauer, H., Kollenz, G., Hogenauer, G., and Turnowsky, F. (1994) Protein EnvM is the NADH-dependent enoyl-ACP reductase (Fabl) of Escherichia coli. J Biol Chem 269: 5493-5496.
8. Bishai, W.R., Howard, N.S., Winkelstein, J.A., and Smith, H.O. (1994) Characterization and virulence analysis of catalase mutants of Haemophilus influenzae. Infect Immun 62: 4855-4860.
9. Chae, H.Z., Robison, K., Poole, L.B., Church, G., Storz, G., and Rhee, S.G. (1994a) Cloning and sequencing of thiol-specific antioxidant from mammalian brain: Alkyl hydroperoxide reductase and thiol-specific antioxidant define a large family of antioxidant enzymes. Proc Natl Acad Sci USA 91: 7017-7021.
10. Chae, H.Z., Chung, S.J., and Rhee, S.G. (1994b) Thioredoxin-dependent peroxide reductase from yeast. J Biol Chem 269: 27670-27678.
11. Chae, H.Z., Uhm, T.B., and Rhee, S.G. (1994c) Dimerization of thiol-specific antioxidant and the essential role of cysteine 47. Proc Natl Acad Sci USA 91: 7022-7026.
12. Christman, M.F., Storz, G., and Ames, B.N. (1989) OxyR, a positive regulator of hydrogen peroxide-inducible genes in Escherichia coli and Salmonella typhimurium, is homologous to a family of bacterial regulatory proteins. Proc Natl Acad Sci USA 86: 3484-3488.
13. Collins, D.M., and de Lisle, G.W. (1984) DNA restriction endonuclease analysis of Mycobacterium tuberculosis and Mycobacterium bovis BCG. J Gen Microbiol 130: 1019-1021.
14. Dessen, A., Quemard, A., Blanchard, J.S., Jacobs, W.R., and Sacchettini, J.C. (1995) Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science 267: 1638-1641.
15. Edman, J.C. Ellis, L., Blacher, R.W., Roth, R.A., and Rutter, W.J. (1985) Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 317: 267-270.
16. Freedman, R.B. (1984) Native disulphide bond formation in protein biosynthesis: evidence for the role of protein disulphide isomerase. Trends Biochem Sci 9: 438-441.
17. Genetics Computer Group (1991) Program manual for the GCG package, Version 7, Madison, Wisconsin, U.S.A.
18. Heym, B., Alzari, P.M., Honore, N., and Cole, S.T. (1995) Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol Microbiol 15: 235-245.
19. Hochman, A., Figueredo, A., and Wall, J.D. (1992) Physiological functions of hydroperoxidases in Rhodobacter capsulatus. J Bacteriol 174: 3386-3391.
20. Holmgren, A. (1985) Thioredoxin. Annu Rev Biochem 54: 237-271.
21. Jacobson, F.S., Morgan, R.W., Christman, M.F., and Ames, B.N. (1989) An alkyl hydroperoxide reductase from Salmonella typhimurium involved in the defence of DNA against oxidative damage. J Biol Chem 264: 1488-1496.
22. Jacobs, Jr, W.R., Kalpana, G.V., Cirillo, J.D., Pascopella, L., Snapper, S.B., Udani, R.A., Jones, W., Barletta, R.G., and Bloom, B.R. (1991) Genetic systems for mycobacteria. Meth Enzymol 204: 537-555.
23. Johnsson, K., and Schultz, P.G. (1994) Mechanistic studies of isoniazid by the catalase peroxidase from Mycobacterium tuberculosis. J Am Chem Soc 116: 7425-7426.
24. Kapur, V., Li, L., Hamrick, M.R., Plikaytis, B.B., Shinnick, T.M., Telenti, A., Jacobs, W.R., Banerjee, A., Cole, S., Yuen, K.Y., Clarridge, J.E., Kreiswirth, B.N., and Musser, J.M. (1995) Rapid Mycobacterium species assignment and unambiguous identification of mutations associated with antimicrobial resistance in Mycobacterium tuberculosis by automated DNA sequencing. Arch Pathol Lab Med 119: 131-138.
25. Levin, M.E., and Hatfull, G.F. (1993) Mycobacterium smegmatis RNA polymerase: DNA supercoiling, action of rifampicin and mechanism of rifampicin resistance. Mol Microbiol 8: 277-285.
26. Lim, Y.S., Cha, M.K., Kim, H.K., Uhm, T.B., Park, J.W., Kim, K., and Kim, I.H. (1993) Removals of hydrogen peroxide and hydroxy radical by thiol-specific antioxidant protein as a possible role in vivo. Biochem Biophys Res Commun 192: 273-280.
27. Middlebrook, G. (1954) Isoniazid-resistance and catalase activity of tubercle bacilli. Am Rev Tuberc 69:471-472.
28. Middlebrook, G., and Conn, M.L. (1953) Some observations on the pathogenicity of isoniazid-resistant variants of tubercle bacilli. Science 118:297-299.
29. Miller, J.H. (1972) Experiments in Molecular Genetics. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory Press.
30. Morris, R.S., Pfeiffer, D.U., and Jackson, R. (1994) The epidemiology of Mycobacterium bovis infections. Vet Microbiol 40: 153-177.
31. Quemard, A., Lacave, C., and Laneelle, G. (1991) Isoniazid inhibition of mycolic acid synthesis by cell extracts of sensitive and resistant strains of Mycobacterium aurum. Antimicrob Ag Chemother 35:1035-1039.
32. Rosner, J.L. (1993) Susceptibilities of oxyR regulon mutants of Escherichia coli and Salmonella typhimurium to isoniazid. Antimicrob Ag Chemother 37: 2251-2253.
33. Rosner, J.L., and Storz, G. (1994) Effects of peroxides on susceptibilities of Escherichia coli and Mycobacterium smegmatis to isoniazid. Antimicrob Ag Chemother 38: 1829-1833.
34. Sherman, D.R., Sabo, P.J., Hickey, M.J., Arain, T.M., Mahairas, G.G., Yuan, Y., Barry, III, C.E., and Stover, C.K. (1995) Disparate responses to oxidative stress in saprophytic and pathogenic mycobacteria. Proc Natl Acad Sci USA 92: 6625-6629.
35. Shoeb, H.A., Bowman, B.U., Ottolenghi, A.C., and Merola, A.J. (1985) Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra. Antimicrob Ag Chemother 27: 404-407.
36. van Soolingen, D., Hermans, P.W.M., de Haas, P.E.W., Soll, D.R., and van Embden, J.D.A. (1991) Occurrence and stability of insertion sequences in Mycobacterium tuberculosis complex strains: Evaluation of an insertion sequence-dependent DNA polymorphism as a tool in the epidemiology of tuberculosis. J Clin Microbiol 29: 2578-2586.
37. Steenken, Jr, W., and Wolinsky, E. (1955) Studies on the pathogenicity of several INH-resistant cultures in mice, guinea pigs, and rabbits. In Transactions of the 14th Veterans Administration Conference on the Chemotherapy of Tuberculosis. Washington, DC: US Veterans Administration, pp. 210-217.
38. Storz, G., Jacobson, F.S., Tartaglia, L.A., Morgan, R.W., Silveira, L.A., and Ames, B.N. (1989) An alkyl hydroperoxide reductase induced by oxidative stress in Salmonella typhimurium and Escherichia coli: Genetic characterization and cloning of ahp. J Bacteriol 171: 2049-2055.
39. Storz, G., Tartaglia, L.A., and Ames, B.N. (1990) Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248: 189-194.
40. Tai, S.S., and Zhu, Y.Y. (1995) Cloning of a Corynebacterium diphtheriae iron-repressible gene that shares homology with the AhpC subunit of alkyl hydroperoxide of Salmonella typhimurium. J Bacteriol 177: 3512-3517.
41. Wayne, L.G., and Diaz, G.A. (1982) Serological, taxonomic and kinetic studies of the T and M classes of mycobacterial catalase. Int J System Bacteriol 32: 296-304.
42. Wilson, T.M., de Lisle, G.W., and Collins, D.M. (1995) Effect of inhA and katG on isoniazid resistance and virulence of Mycobacterium bovis. Mol Microbiol 15: 1009-1015.
43. Winder, F. (1964) The antibacterial action of streptomycin, isoniazid, and PAS. In Chemotherapy of Tuberculosis, Barry, V.C. (ed.). London: Butterworths, pp. 111-149.
44. Yamaguchi, R., Matsuo, K., Yamazaki, A., Takahashi, M., Fukasawa, Y., Wada, M., and Abe, C. (1992) Cloning and expression of the gene for the Avi-3 antigen of Mycobacterium avium and mapping its epitopes. Infect Immun 60: 1210-1216.
45. Zhang, Y., and Young, D., (1994) Strain variation in the katG region of Mycobacterium tuberculosis. Mol Microbiol 14: 301-308.
46. Zhang, Y., Heym, B., Allen, B., Young, D., and Cole, S. (1992) The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358: 591-593.
47. Zhang, Y., Garbe, T., and Young, D. (1993) Transformation with katG restores isoniazid-sensitivity in Mycobacterium tuberculosis isolates resistant to a range of drug concentrations. Mol Microbiol 8: 521-524.
48. Zheng, H., Hassett, D.J., Bean, K., and Cohen, M.S. (1992) Regulation of catalase in Neisseria gonorrhoeae. J Clin Invest 90: 1000-1006.