Iron enhances the susceptibility of pathogenic mycobacteria to isoniazid, an antitubercular drug

World Journal of Microbiology and Biotechnology

Volumn 22, Issue 12, 2006, Pages 1357-1364

  Sritharan, Manjula ^a   Yeruva, Veena C ^a   Sivasailappan, Sivagamisundaram C ^a   Duggirala, Sridevi ^a  

^a UNIVERSITY OF HYDERABAD   (India)

Author keywords

Alamar Blue assay; Catalase peroxidases; Iron; Isoniazid; Mycobacteria

Indexed keywords

BACTERIA; BIOASSAY; ENZYME KINETICS; GELS; GROWTH KINETICS; IRON; MICROBIOLOGY;

ANTITUBERCULAR DRUG; IRON DEPRIVATION; MYCOBACTERIA; PEROXIDASE ACTIVITIES;

DRUG PRODUCTS;

BACTERIA (MICROORGANISMS); CORYNEBACTERINEAE; MYCOBACTERIUM; MYCOBACTERIUM BOVIS; MYCOBACTERIUM BOVIS BCG; MYCOBACTERIUM TUBERCULOSIS;

EID: 33748188139     PISSN: 09593993     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11274-006-9183-8     Document Type: Article

References (39)

1. Banerjee A, Dubnau E, Quemard A, Balasubramanian V, Um KS, Wilson T, Collins D, de Lisle G., Jacobs WR Jr (1994). InhA, a gene encoding a target for isoniazid and ethionamide in Mycobacterium tuberculosis. Science 263:227-230
2. Bartos M, Falkinham III JO, Pavlik I (2004). Mycobacterial catalases, peroxidases, and superoxide dismutases and their effects on virulence and isoniazid-susceptibility in mycobacteria - a review. Vet Med (Czech) 49:161-170
3. Braun V, Hantke K, Koster W (1998) Bacterial iron transport: mechanisms, genetics and regulation. In: Sigel A, Sigel H (eds) Metal Ions in Biological systems. Iron transport and storage in Microorganisms, Plants and Animals. Marcel Dekker, New York pp. 67-145 ISBN 0-8247-9984-4
4. Beers RF, Sizer IW (1952) A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem 195:133-140
5. Chipperfield JR, Ratledge C (2000) Salicylate is not a bacterial siderophore: a theoretical study. Biometals 13:165-168
6. Cole ST et al (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete sequence. Nature 393:537-544
7. Chouchane S, Girotto S, Kapetanaki S, Schelvis JPM, Yu S, Magliozzo RS (2003) Analysis of heme structural heterogeneity in Mycobacterium tuberculosis catalase-peroxidase (KatG). J Biol Chem 278:8154-8162
8. Dussurget O, Rodriguez M, Smith I (1996) An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative stress response. Mol Microbiol 22:535-544
9. Dussurget O., Smith I (1998) Interdependence of mycobacterial iron regulation, oxidative-stress response and isoniazid resistance. Trends Microbiol 6:354-358
10. Franzblau SG, Witzig RS, McLaughlin JC, Torres P, Madico G, Hernandez A, Degnan MT, Cook MB, Quenzer VK, Ferguson RM, Gilman RH (1998) Rapid, low-technology MIC determination with clinical Mycobacterium tuberculosis isolates by using the microplate Alamar Blue assay. J Clin Microbiol 36:362-366
11. Hall RM, Sritharan M, Messenger AJM, Ratledge C (1987) Iron transport in Mycobacterium smegmatis, occurrence of iron-regulated envelope proteins as potential receptors for iron uptake. J Gen Microbiol 133:2107-2114
12. Heym B, Alzari PM, Honore N, Cole ST (1995) Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis. Mol Microbiol 15:235-245
13. Heym B, Honore N, Truffot-Pernot C, Banerjee A, Schurra C, Jacobs Jr. WR, van Embden JDA, Grosset JH, Cole ST (1994) The implications of multidrug resistance for the future of short course chemotherapy of tuberculosis: a molecular study. Lancet 344:293-298
14. Heym B, Stavropoulos E, Honore N, Domenech P, Saint-Joanis B, Wilson TM, Collins DM, Colston MJ, Cole ST (1997) Effects of over expression of the alkyl hydroperoxide reductase AhpC on the virulence and isoniazid resistance of Mycobacterium tuberculosis. Infect Immun 65:1395-1401
15. Kochan I. (1973) The role of iron in bacterial infections with special consideration of host-tubercle bacillus interaction. Curr Top Microbiol Immunol 60:1-30
16. Middlebrook G (1954) Isoniazid resistance and catalase activities of tubercle bacilli - a preliminary report. Am Rev Tuberc 69:471-472
17. Milano A, Forti F, Sala C, Riccardi G, Ghisotti D (2001) Transcriptional regulation of furA and katG upon oxidative stress in Mycobacterium smegmatis. J Bacteriol 183:6801-6806
18. Pym AS, Domenech P, Honore N, Song J, Deretic V, Cole ST (2001) Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol Microbiol 40:879-889
19. Ratledge C, Dover LG (2000) Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 54:881-941
20. Ratledge C (2004) Iron, mycobacteria and tuberculosis. Tuberculosis 84:110-130
21. Rodriguez GM, Voskuil MI, Gold B, Schoolnik GK, Smith I (2002) IdeR, an essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect Immun 70:3371-3381
22. Saint-Joanis B, Souchon H, Wilming M, Johnsson K, Alzar PM, Cole ST (1999) Use of site-directed mutagenesis to probe the structure, function and isoniazid activation of the catalase/peroxidase, KatG from Mycobacterium tuberculosis. Biochem J 338:753-760
23. Schwyn B, Neilands JB (1987) Universal chemical assay for the detection and determination of siderophores. Anal Biochem 160:47-55
24. Shoeb HA, Bowman JBU, Ottolenghi AC, Merola AJ (1985a) Evidence for the generation of active oxygen by isoniazid treatment of extracts of Mycobacterium tuberculosis H37Ra. Antimicrob Agents Chemother 27:399-403
25. Shoeb HA, Bowman Jr, BU, Ottolenghi AC, Merola AJ (1985b) Peroxidase-mediated oxidation of isoniazid. Antimicrob Agents Chemother 27:404-407
26. Sritharan M (2000) Iron as a candidate in virulence and pathogenesis in mycobacteria and other microorganisms. World J Microbiol Biotechnol 16:769-780
27. Sritharan M, Ratledge C (1990) Iron-regulated envelope proteins of mycobacteria grown in vitro and their occurrence in Mycobacterium leprae grown in vivo. Biol Met 2:203-208
28. Sritharan M, Sritharan V (2002) Microbial pathogenesis: an insight into Mycobacterium tuberculosis. Indian J Med Microbiol 20:61-68
29. Sherman DR, Mdluli K, Hickey MJ, Arain TM, Morris SL, Barry CE III, Stover CK (1996) Compensatory ahpC gene expression in isoniazid-resistant Mycobacterium tuberculosis. Science 272:1641-1643
30. Somoskovi A, Wade MM, Sun Z, Zhang Y (2004) Iron enhances the antituberculous activity of pyrazinamide. J Antimicrob Chemother 53:192-196
31. Wayne LG, Diaz GA (1986) A double staining method for differentiating between two classes of mycobacterial catalase in polyacrylamide electrophoresis gels. Anal Biochem 157:89-92
32. Weinberg ED (1999) Iron loading and disease surveillance. Emerg Infect Dis 5:346-352
33. Weinberg ED (2002) Therapeutic potential of human transferrin and lactoferrin. ASM News 68:65-69
34. Yeruva VC, Sivagami sundaram CAS, Sritharan M (2005) Effect of iron concentration on the expression and activity of catalase-peroxidases in mycobacteria. Indian J Biochem Biophys 42:28-33
35. Zámocký M, Regelsberger G, Jakopitsch C, Obinger C (2001) The molecular peculiarities of catalase-peroxidases. FEBS Lett 492:177-182
36. Zámocký M (2004) Phylogenetic relationships in class I of the superfamily of bacterial, fungal and plant peroxidases. Eur J Biochem 271:3297-3309
37. Zahrt TC, Song J, Siple J, Deretic V (2001) Mycobacterial FurA is a negative regulator of catalase-peroxidase gene katG. Mol Microbiol 39:1174-1185
38. Zhang Y (1996) Life without KatG. Trends Microbiol 4:415-417
39. Zhang Y, Heym B, Allen B, Young D, Cole S (1992) The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis. Nature 358:591-593