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Volumn 16, Issue 8, 2007, Pages 1617-1627

Probing mechanisms of resistance to the tuberculosis drug isoniazid: Conformational changes caused by inhibition of InhA, the enoyl reductase from Mycobacterium tuberculosis

Author keywords

Enoyl reductase; Fatty acid synthesis; InhA; Isoniazid; Mycobacterium tuberculosis

Indexed keywords

ISONIAZID; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 34547576168     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062749007     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 33745094315 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid
    • Argyrou, A., Vetting, M.W., Aladegbami, B., and Blanchard, J.S. 2006. Mycobacterium tuberculosis dihydrofolate reductase is a target for isoniazid. Nat. Struct. Mol. Biol. 13: 408-413.
    • (2006) Nat. Struct. Mol. Biol , vol.13 , pp. 408-413
    • Argyrou, A.1    Vetting, M.W.2    Aladegbami, B.3    Blanchard, J.S.4
  • 3
    • 0031689089 scopus 로고    scopus 로고
    • Mechanisms of isoniazid resistance in Mycobacterium tuberculosis: Enzymatic characterization of enoyl reductase mutants identified in isoniazid-resistant clinical isolates
    • Basso, L.A., Zheng, R., Musser, J.M., Jacobs Jr., W.R., and Blanchard, J.S. 1998. Mechanisms of isoniazid resistance in Mycobacterium tuberculosis: Enzymatic characterization of enoyl reductase mutants identified in isoniazid-resistant clinical isolates. J. Infect. Dis. 178: 769-775.
    • (1998) J. Infect. Dis , vol.178 , pp. 769-775
    • Basso, L.A.1    Zheng, R.2    Musser, J.M.3    Jacobs Jr., W.R.4    Blanchard, J.S.5
  • 4
    • 1842428822 scopus 로고    scopus 로고
    • Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles
    • Dam, J. and Schuck, P. 2004. Calculating sedimentation coefficient distributions by direct modeling of sedimentation velocity concentration profiles. Methods Enzymol. 384: 185-212.
    • (2004) Methods Enzymol , vol.384 , pp. 185-212
    • Dam, J.1    Schuck, P.2
  • 5
    • 0028988237 scopus 로고
    • Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis
    • Dessen, A., Quemard, A., Blanchard, J.S., Jacobs Jr., W.R., and Sacchettini, J.C. 1995. Crystal structure and function of the isoniazid target of Mycobacterium tuberculosis. Science 267: 1638-1641.
    • (1995) Science , vol.267 , pp. 1638-1641
    • Dessen, A.1    Quemard, A.2    Blanchard, J.S.3    Jacobs Jr., W.R.4    Sacchettini, J.C.5
  • 6
    • 32944482036 scopus 로고    scopus 로고
    • Resistance to anti-infective drugs and the threat to public health
    • Heymann, D.L. 2006. Resistance to anti-infective drugs and the threat to public health. Cell 124: 671-675.
    • (2006) Cell , vol.124 , pp. 671-675
    • Heymann, D.L.1
  • 9
    • 0033962136 scopus 로고    scopus 로고
    • InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II
    • Marrakchi, H., Laneelle, G., and Quemard, A. 2000. InhA, a target of the antituberculous drug isoniazid, is involved in a mycobacterial fatty acid elongation system, FAS-II. Microbiol. 146: 289-296.
    • (2000) Microbiol , vol.146 , pp. 289-296
    • Marrakchi, H.1    Laneelle, G.2    Quemard, A.3
  • 11
    • 0029859098 scopus 로고    scopus 로고
    • Biochemical and genetic data suggest that InhA is not the primary target for activated isoniazid in Mycobacterium tuberculosis
    • Mdluli, K., Sherman, D.R., Hickey, M.J., Kreiswirth, B.N., Morris, S., Stover, C.K., and Barry 3rd, C.E. 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.
    • (1996) J. Infect. Dis , vol.174 , pp. 1085-1090
    • Mdluli, K.1    Sherman, D.R.2    Hickey, M.J.3    Kreiswirth, B.N.4    Morris, S.5    Stover, C.K.6    Barry 3rd, C.E.7
  • 13
    • 0001293738 scopus 로고
    • Sterilization of tubercle bacilli by isonicotinic acid hydrazide and the incidence of variants resistant to the drug in vitro
    • Middlebrook, G. 1952. Sterilization of tubercle bacilli by isonicotinic acid hydrazide and the incidence of variants resistant to the drug in vitro. Am. Rev. Tuberc. 65: 765-767.
    • (1952) Am. Rev. Tuberc , vol.65 , pp. 765-767
    • Middlebrook, G.1
  • 14
    • 0017654536 scopus 로고
    • Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system
    • Odriozola, J.M., Ramos, J.A., and Bloch, K. 1977. Fatty acid synthetase activity in Mycobacterium smegmatis. Characterization of the acyl carrier protein-dependent elongating system. Biochim. Biophys. Acta 488: 207-217.
    • (1977) Biochim. Biophys. Acta , vol.488 , pp. 207-217
    • Odriozola, J.M.1    Ramos, J.A.2    Bloch, K.3
  • 15
    • 0033550048 scopus 로고    scopus 로고
    • Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis
    • Parikh, S., Moynihan, D.P., Xiao, G., and Tonge, P.J. 1999. Roles of tyrosine 158 and lysine 165 in the catalytic mechanism of InhA, the enoyl-ACP reductase from Mycobacterium tuberculosis. Biochemistry 38: 13623-13634.
    • (1999) Biochemistry , vol.38 , pp. 13623-13634
    • Parikh, S.1    Moynihan, D.P.2    Xiao, G.3    Tonge, P.J.4
  • 17
    • 0345133299 scopus 로고    scopus 로고
    • The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance
    • Rawat, R., Whitty, A., and Tonge, P.J. 2003. The isoniazid-NAD adduct is a slow, tight-binding inhibitor of InhA, the Mycobacterium tuberculosis enoyl reductase: Adduct affinity and drug resistance. Proc. Natl. Acad. Sci. 100: 13881-13886.
    • (2003) Proc. Natl. Acad. Sci , vol.100 , pp. 13881-13886
    • Rawat, R.1    Whitty, A.2    Tonge, P.J.3
  • 18
    • 0040017633 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis enoyl-ACP reductase, InhA, in complex with NAD+ and a C16 fatty acyl substrate
    • Rozwarski, D.A., Vilcheze, C., Sugantino, M., Bittman, R., and Sacchettini, J.C. 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.
    • (1999) J. Biol. Chem , vol.274 , pp. 15582-15589
    • Rozwarski, D.A.1    Vilcheze, C.2    Sugantino, M.3    Bittman, R.4    Sacchettini, J.C.5
  • 20
    • 0031688168 scopus 로고    scopus 로고
    • Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation
    • Schuck, P. 1998. Sedimentation analysis of noninteracting and self-associating solutes using numerical solutions to the Lamm equation. Biophys. J. 75: 1503-1512.
    • (1998) Biophys. J , vol.75 , pp. 1503-1512
    • Schuck, P.1
  • 21
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. 2000. Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling. Biophys. J. 78: 1606-1619.
    • (2000) Biophys. J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 22
    • 0033709606 scopus 로고    scopus 로고
    • Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis
    • Slayden, R.A., Lee, R.E., and Barry 3rd, C.E. 2000. Isoniazid affects multiple components of the type II fatty acid synthase system of Mycobacterium tuberculosis. Mol. Microbiol. 38: 514-525.
    • (2000) Mol. Microbiol , vol.38 , pp. 514-525
    • Slayden, R.A.1    Lee, R.E.2    Barry 3rd, C.E.3
  • 23
    • 0016529811 scopus 로고
    • Site of inhibitory action of isoniazid in the synthesis of mycolic acids in Mycobacterium tuberculosis
    • Takayama, K., Schnoes, H.K., Armstrong, E.L., and Boyle, R.W. 1975. Site of inhibitory action of isoniazid in the synthesis of mycolic acids in Mycobacterium tuberculosis. J. Lipid Res. 16: 308-317.
    • (1975) J. Lipid Res , vol.16 , pp. 308-317
    • Takayama, K.1    Schnoes, H.K.2    Armstrong, E.L.3    Boyle, R.W.4
  • 24
    • 9644257517 scopus 로고    scopus 로고
    • Protein-protein interactions within the fatty acid synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability
    • Veyron-Churlet, R., Guerrini, O., Mourey, L., Daffe, M., and Zerbib, D. 2004. Protein-protein interactions within the fatty acid synthase-II system of Mycobacterium tuberculosis are essential for mycobacterial viability. Mol. Microbiol. 54: 1161-1172.
    • (2004) Mol. Microbiol , vol.54 , pp. 1161-1172
    • Veyron-Churlet, R.1    Guerrini, O.2    Mourey, L.3    Daffe, M.4    Zerbib, D.5
  • 25
    • 26844537406 scopus 로고    scopus 로고
    • The biosynthesis of mycolic acids in Mycobacterium tuberculosis relies on multiple specialized elongation complexes interconnected by specific protein-protein interactions
    • Veyron-Churlet, R., Bigot, S., Guerrini, O., Verdoux, S., Malaga, W., Daffe, M., and Zerbib, D. 2005. The biosynthesis of mycolic acids in Mycobacterium tuberculosis relies on multiple specialized elongation complexes interconnected by specific protein-protein interactions. J. Mol. Biol. 353: 847-858.
    • (2005) J. Mol. Biol , vol.353 , pp. 847-858
    • Veyron-Churlet, R.1    Bigot, S.2    Guerrini, O.3    Verdoux, S.4    Malaga, W.5    Daffe, M.6    Zerbib, D.7
  • 26
    • 0038410325 scopus 로고    scopus 로고
    • Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis
    • Vilcheze, C., Morbidoni, H.R., Weisbrod, T.R., Iwamoto, H., Kuo, M., Sacchettini, J.C., and Jacobs Jr., W.R. 2000. Inactivation of the inhA-encoded fatty acid synthase II (FASII) enoyl-acyl carrier protein reductase induces accumulation of the FASI end products and cell lysis of Mycobacterium smegmatis. J. Bacteriol. 182: 4059-4067.
    • (2000) J. Bacteriol , vol.182 , pp. 4059-4067
    • Vilcheze, C.1    Morbidoni, H.R.2    Weisbrod, T.R.3    Iwamoto, H.4    Kuo, M.5    Sacchettini, J.C.6    Jacobs Jr., W.R.7
  • 28
    • 15244363788 scopus 로고    scopus 로고
    • World Health Organization, World Health Organization, Geneva, Switzerland
    • World Health Organization. 2003. Global TB Control Report. World Health Organization, Geneva, Switzerland.
    • (2003) Global TB Control Report
  • 29
    • 0026705772 scopus 로고
    • The catalase-peroxidase gene and isoniazid resistance of Mycobacterium tuberculosis
    • 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.
    • (1992) Nature , vol.358 , pp. 591-593
    • Zhang, Y.1    Heym, B.2    Allen, B.3    Young, D.4    Cole, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.