Catalase-peroxidase of Mycobacterium bovis BCG converts isoniazid to isonicotinamide, but not to isonicotinic acid: Differentiation parameter between enzymes of Mycobacterium bovis BCG and Mycobacterium tuberculosis

Biochimica et Biophysica Acta - General Subjects

Volumn 1760, Issue 5, 2006, Pages 724-729

  Kang, Sung Koo ^a,b   Lee, Jong Ho ^a,b   Lee, Young Choon ^c   Kim, Cheorl Ho ^a,b  

^a Sungkyunkwan University   (South Korea)

^b National Research Laboratory for Glycobiology   (South Korea)

^c Dong A University   (South Korea)

Author keywords

Catalase Peroxidase; Isoniazid; Isonicotinamide; Isonicotinic acid; Mycobacterium bovis BCG

Indexed keywords

BCG VACCINE; ISONIAZID; ISONICOTINAMIDE; ISONICOTINIC ACID; KATG PROTEIN; PROTEIN SUBUNIT;

ARTICLE; DRUG ACTIVATION; ENZYME ACTIVITY; GAS CHROMATOGRAPHY; GEL FILTRATION; MASS SPECTROMETRY; MOLECULAR WEIGHT; MYCOBACTERIUM BOVIS; MYCOBACTERIUM TUBERCULOSIS; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STRUCTURE;

BACTERIAL PROTEINS; ISONIAZID; ISONICOTINIC ACIDS; MOLECULAR WEIGHT; MYCOBACTERIUM BOVIS; MYCOBACTERIUM TUBERCULOSIS; NIACINAMIDE; PEROXIDASES;

MYCOBACTERIUM BOVIS BCG; MYCOBACTERIUM TUBERCULOSIS;

EID: 33646106106     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2005.12.026     Document Type: Article

References (41)

1. Altamirano M., Marostenmaki J., Wong A., Fitzgerald M., Black W.A., and Smith J.A. Mutations in the catalase-peroxidase gene from isoniazid-resistant Mycobacterium tuberculosis isolates. J. Infect. Dis. 169 (1994) 1162-1165
2. Heym B., Alzari P.M., Jonore N., and Cole S.T. Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol. Microbiol. 15 (1995) 235-245
3. Magliozzo R.S., and Marcinkeviciene J.A. The role of Mn(II)-peroxidase activity of mycobacterial catalase-peroxidase in activation of the antibiotic isoniazid. J. Biol. Chem. 272 (1997) 8867-8870
4. Marcinkeviciene J.A., Magliozzo R.S., and Blanchard J.S. Purification and characterization of the Mycobacterium smegmatis catalase-peroxidase involved in isoniazid activation. J. Biol. Chem. 270 (1995) 22290-22295
5. Bertrand T., Eady N.A., Jones J.N., Jesmin S., Nagy J.M., Jamart-Gregoire B., Raven E.L., and Brown K.A. Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 279 (2004) 38991-38999
6. Rouse D.A., Li Z., Bai G.H., and Morris S.L. Characterization of the katG and inhA genes of isoniazid-resistant clinical isolates of Mycobacterium tuberculosis. Antimicrob. Agents Chemother. 39 (1995) 2472-2477
7. Sherman D.R., Mdluli K., Hichey M.J., Arian T.M., Morris S.L., Barry III C.E., and Stover A.C. Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 272 (1996) 1641-1643
8. Zhang Y., Heym B., Allen B., Young D., and Cole S. The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358 (1992) 591-593
9. O'Brien L., Roberts B., and Andrew P.W. In vitro interaction of Mycobacterium tuberculosis and macrophages: activation of anti-mycobacterial activity of macrophages and mechanisms of anti-mycobacterial activity. Tuberculosis. Curr. Top. Microbiol. Immunol. 215 (1996) 97-130
10. Kim S.Y., Park Y.J., Kim W.I., Lee S.H., Ludgerus Chang C., Kang S.J., and Kang C.S. Molecular analysis of isoniazid resistance in Mycobacterium tuberculosis isolates recovered from South Korea. Diagn. Microbiol. Infect. Dis. 47 (2003) 497-502
11. Johnsson K., Froland W.A., and Schultz P.G. Overexpression, purification, and characterization of the catalase-peroxidase KatG from Mycobacterium tuberculosis. J. Biol. Chem. 272 (1997) 2834-2840
12. Shoeb H.A., Bowman Jr. B.U., ottolenghi A.C., and Merola A.J. Peroxidase-mediated oxidation of isoniazid. Antimicrob. Agents Chemother. 27 (1985) 399-403
13. Shoeb H.A., Bowman Jr. B.U., ottolenghi A.C., and Merola A.J. Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra. Antimicrob. Agents Chemother. 27 (1985) 404-407
14. Baker R.D., Cook C.O., and Goodwin D.C. Properties of catalase-peroxidase lacking its C-terminal domain. Biochem. Biophys. Res. Commun. 320 (2004) 833-839
15. Kang S.K., Jung Y.J., Kim C.H., and Song C.Y. Extracellular and cytosolic iron superoxide dismutase from Mycobacterium bovis BCG. Clin. Diagn. Lab. Immunol. 5 (1998) 784-789
16. Kim J.R., Choe Y.K., Chang J.E., Song E.Y., Ko J.H., Lee Y.C., Choi I.S., and Kim C.H. Genomic heterogeneity in clinical strains of Mycobacterium tuberculosis, M. terrae Complex, M. gordonae, M. avium-intracellulae Complex and M. fortuitum by pulsed-field gel electrophoresis. J. Biochem. Mol. Biol. 29 (1996) 569-573
17. Kim J.R., Lee Y.C., and Kim C.H. Genomic polymorphism in clinical mycobacterial strains analyzed by pulsed-field gel electrophoresis. J. Microbiol. 35 (1997) 172-176
18. Choe Y.K., Kim J.R., Chang J.E., Song E.Y., Ko J.H., Lee Y.C., Choi I.S., and Kim C.H. Improved isolation of mycobacterial genomic DNA by agarose blocks with combination of lysozyme and N-acetylglucosaminidase. BioTechniques 20 (1996) 547-552
19. Harboe M., Oettinger T., Wiker H.G., Rosenkrands I., and Andersen P. Evidence for occurrence of the ESAT-6 protein in Mycobacterium tuberculosis and virulent Mycobacterium bovis and for its absence in Mycobacterium bovis BCG. Infect. Immun. 64 (1996) 16-22
20. Kang T.J., You J.C., and Chae G.T. Identification of catalase-like activity from Mycobacterium leprae and the relationship between catalase and isonicotinic acid hydrazide (INH). J. Med. Microbiol. 50 (2001) 675-681
21. Lowry O.H., Rosebrugh N.J., Farr A.L., and Randal R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
22. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227 (1970) 680-685
23. Bollag D.M., and Edelstein S.T. Protein Method (1991), WILLEY-LISS, USA 143-160
24. Gianazza E., Gelfi C., and Righetti P.G. Isoelectric focusing following by electrophoresis of proteins for visualizing their titration curves by zymogram and immunofixation. J. Biochem. Biophys. Methods 3 (1980) 65-75
25. Diaz G.A., and Wayne L.G. Isolation and characterization of catalase produced by Mycobacterium tuberculosis. Am. Rev. Respir. Dis. 110 (1974) 312-319
26. Magliozzo R.S., and Marcinkeviciene J.A. Evidence for isoniazid oxidation by oxyferrous mycobacterial catalase-peroxidase. J. Am. Chem. Soc. 118 (1996) 11303-11304
27. Chouchane S., Girotto S., Yu S., and Magliozzo R.S. Identification and characterization of tyrosyl radical formation in Mycobacterium tuberculosis catalase-peroxidase (KatG). J. Biol. Chem. 277 (2002) 42633-42638
28. Ghiladi R.A., Knudsen G.M., Medzihradszky K.F., and de Montellano P.R. The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties. J. Biol. Chem. 280 (2005) 22651-22663
29. Quemard A., Dessen A., Sugantino M., Jacobs Jr. W.R., Sacchettini J.C., and Blanchard J.S. Binding of catalase-peroxidase-activated isoniazid to wild-type and mutant Mycobacterium tuberculosis Enoyl-ACP reductases. J. Am. Chem. Soc. 118 (1996) 1561-1562
30. Wengenack N.L., Uhl J.R., Amand A.L., Tomlinson A.J., Benson L.M., Naylor S., Kline B.C., Cockerill III F.R., and Rusnak F. Recombinant Mycobacterium tuberculosis KatG(S315T) is a competent catalase-peroxidase with reduced activity toward isoniazid. J. Infect. Dis. 176 (1997) 722-727
31. Johnsson K., and Schultz P.G. Mechanistic studies of the oxidation of isoniazid by the catalase peroxidase from Mycobacterium tuberculosis. J. Am. Chem. Soc. 116 (1994) 7425-7426
32. de Montellan O. Oxidation of hydrazines and hydrazides can lead to the inactivation of catalase-peroxidases and cytochrome P450., P. R. In: Ortiz de Montellano P.R. (Ed). Cytochrome P450 (1986), Plenum Publishing Corp, New York 273-314
33. Ogata S., Takeuchi M., Okumura K., and Taguchi H. Apoptosis induced by niacin-related compounds in HL-60 cells. Biosci. Biotechnol. Biochem. 62 (1998) 2351-2356
34. Luo Y., Chen X., Downs T.M., DeWolf W.C., and O'Donnell M.A. IFN-alpha 2B enhances Th1 cytokine responses in bladder cancer patients receiving Mycobacterium bovis bacillus calmette-Guérin immunotherapy. J. Immunol. 162 (1999) 2399-2405
35. Stassa M.J., Vegt P.D., Steerenberg P.A., van der Meijden A.P., Meiring H.D., Dessens-Kroon M., Geertzen H.G., and den Otter W. Effects of isoniazid (INH) on the BCG-induced local immune response after intravesical BCG therapy for superficial bladder cancer. Urol. Res. 22 (1994) 177-184
36. Sasaki A., Kudoh S., Mori K., Takahashi N., and Suzuki T. Are BCG effects against urinary bladder carcinoma cell line T24 correlated with apoptosis in vitro?. Urol. Int. 59 (1997) 142-148
37. Wang R., Klegerman M.E., Marsden I., Sinnott M., and Groves M.J. An anti-neoplastic glycan isolated from Mycobacterium bovis (BCG vaccine). Biochem. J. 331 (1995) 867-872
38. Gloves M.J. Pharmaceutical characterization of Mycobacterium bovis bacillus Calmette-Guerin (BCG) vaccine used for the treatment of superficial bladder cancer. J. Pharm. Sci. 82 (1993) 555-562
39. Armbruster C., Junker W., Vetter N., and Jaksch G. Disseminated bacille Calmette-Guerin infection in an AIDS patient 30 years after BCG vaccination. J. infect. Dis. 162 (1990) 1216
40. Casanova J.L. Idiopathic disseminated infection by BCG or atypical mycobacteria. Arch. Pediatr. 4 (1997) 883-885
41. Aungst C.W., Sokal J.E., and Jager B.V. Complications of BCG vaccination in neoplastic disease. Ann. Intern. Med. 82 (1975) 666-669