메뉴 건너뛰기




Volumn 91, Issue 1, 2014, Pages 98-109

IdeR is required for iron homeostasis and virulence in Mycobacterium tuberculosis

Author keywords

[No Author keywords available]

Indexed keywords

DOXYCYCLINE; IRON; RUFOCROMOMYCIN; SIDEROPHORE; BACTERIAL PROTEIN; IDER PROTEIN, MYCOBACTERIUM TUBERCULOSIS; REACTIVE NITROGEN SPECIES; REPRESSOR PROTEIN; VIRULENCE FACTOR;

EID: 84891166287     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/mmi.12441     Document Type: Article
Times cited : (77)

References (36)
  • 1
    • 77955074030 scopus 로고    scopus 로고
    • Development of a repressible mycobacterial promoter system based on two transcriptional repressors
    • Boldrin, F., Casonato, S., Dainese, E., Sala, C., Dhar, N., Palu, G., etal. (2010) Development of a repressible mycobacterial promoter system based on two transcriptional repressors. Nucleic Acids Res 38: e134.
    • (2010) Nucleic Acids Res , vol.38
    • Boldrin, F.1    Casonato, S.2    Dainese, E.3    Sala, C.4    Dhar, N.5    Palu, G.6
  • 2
    • 0028936417 scopus 로고
    • Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis
    • Chan, J., Tanaka, K., Carroll, D., Flynn, J., and Bloom, B.R. (1995) Effects of nitric oxide synthase inhibitors on murine infection with Mycobacterium tuberculosis. Infect Immun 63: 736-740.
    • (1995) Infect Immun , vol.63 , pp. 736-740
    • Chan, J.1    Tanaka, K.2    Carroll, D.3    Flynn, J.4    Bloom, B.R.5
  • 4
    • 0029905151 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin
    • Clemens, D.L., and Horwitz, M.A. (1996) The Mycobacterium tuberculosis phagosome interacts with early endosomes and is accessible to exogenously administered transferrin. J Exp Med 184: 1349-1355.
    • (1996) J Exp Med , vol.184 , pp. 1349-1355
    • Clemens, D.L.1    Horwitz, M.A.2
  • 5
    • 0032508046 scopus 로고    scopus 로고
    • Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
    • Cole, S.T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., etal. (1998) Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence. Nature 393: 537-544.
    • (1998) Nature , vol.393 , pp. 537-544
    • Cole, S.T.1    Brosch, R.2    Parkhill, J.3    Garnier, T.4    Churcher, C.5    Harris, D.6
  • 6
    • 0029151576 scopus 로고
    • Nitric oxide: biochemistry, physiology and pathophysiology
    • Acompanion to Methods Enzymol :
    • Conner, E.M., and Grisham, M.B. (1995) Nitric oxide: biochemistry, physiology and pathophysiology. Methods Acompanion to Methods Enzymol 7: 3-13.
    • (1995) Methods , vol.7 , pp. 3-13
    • Conner, E.M.1    Grisham, M.B.2
  • 7
    • 0033973479 scopus 로고    scopus 로고
    • The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
    • De Voss, J.J., Rutter, K., Schroeder, B.G., Su, H., Zhu, Y., III, and Barry, C.E., III (2000) The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc Natl Acad Sci USA 97: 1252-1257.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1252-1257
    • De Voss, J.J.1    Rutter, K.2    Schroeder, B.G.3    Su, H.4    Zhu III, Y.5    III Barry, C.E.6
  • 8
    • 0035937172 scopus 로고    scopus 로고
    • Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain
    • Feese, M.D., Ingason, B.P., Goranson-Siekierke, J., Holmes, R.K., and Hol, W.G. (2001) Crystal structure of the iron-dependent regulator from Mycobacterium tuberculosis at 2.0-A resolution reveals the Src homology domain 3-like fold and metal binding function of the third domain. J Biol Chem 276: 5959-5966.
    • (2001) J Biol Chem , vol.276 , pp. 5959-5966
    • Feese, M.D.1    Ingason, B.P.2    Goranson-Siekierke, J.3    Holmes, R.K.4    Hol, W.G.5
  • 9
    • 0031985277 scopus 로고    scopus 로고
    • Rapid, low-technology MIC determination with clinical Mycobacterium tuberculosis isolates by using the microplate Alamar Blue assay
    • Franzblau, S.G., Witzig, R.S., McLaughlin, J.C., Torres, P., Madico, G., Hernandez, A., etal. (1998) Rapid, low-technology MIC determination with clinical Mycobacterium tuberculosis isolates by using the microplate Alamar Blue assay. J Clin Microbiol 36: 362-366.
    • (1998) J Clin Microbiol , vol.36 , pp. 362-366
    • Franzblau, S.G.1    Witzig, R.S.2    McLaughlin, J.C.3    Torres, P.4    Madico, G.5    Hernandez, A.6
  • 10
    • 0028999977 scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins
    • Gobin, J., Moore, C.H., Reeve, J.R., Jr, Wong, D.K., Gibson, B.W., and Horwitz, M.A. (1995) Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc Natl Acad Sci USA 92: 5189-5193.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5189-5193
    • Gobin, J.1    Moore, C.H.2    Reeve Jr., J.R.3    Wong, D.K.4    Gibson, B.W.5    Horwitz, M.A.6
  • 11
    • 0035169902 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages
    • Gold, B., Rodriguez, G.M., Marras, M.P., Pentecost, M., and Smith, I. (2001) The Mycobacterium tuberculosis IdeR is a dual functional regulator that controls transcription of genes involved in iron acquisition, iron storage and survival in macrophages. Mol Microbiol 42: 851-865.
    • (2001) Mol Microbiol , vol.42 , pp. 851-865
    • Gold, B.1    Rodriguez, G.M.2    Marras, M.P.3    Pentecost, M.4    Smith, I.5
  • 12
    • 0036263753 scopus 로고    scopus 로고
    • Use of an arrayed promoter-probe library for the identification of macrophage-regulated genes in Mycobacterium tuberculosis
    • Hobson, R.J., McBride, A.J.A., Kempsell, K.E., and Dale, J.W. (2002) Use of an arrayed promoter-probe library for the identification of macrophage-regulated genes in Mycobacterium tuberculosis. Microbiology 148: 1571-1579.
    • (2002) Microbiology , vol.148 , pp. 1571-1579
    • Hobson, R.J.1    McBride, A.J.A.2    Kempsell, K.E.3    Dale, J.W.4
  • 13
    • 77957671514 scopus 로고    scopus 로고
    • Functional genetic diversity among Mycobacterium tuberculosis complex clinical isolates: delineation of conserved core and lineage-specific transcriptomes during intracellular survival
    • Homolka, S., Niemann, S., Russell, D.G., and Rohde, K.H. (2010) Functional genetic diversity among Mycobacterium tuberculosis complex clinical isolates: delineation of conserved core and lineage-specific transcriptomes during intracellular survival. PLoS Pathog 6: e1000988.
    • (2010) PLoS Pathog , vol.6
    • Homolka, S.1    Niemann, S.2    Russell, D.G.3    Rohde, K.H.4
  • 14
    • 0023905646 scopus 로고
    • Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro
    • Imlay, J.A., Chin, S.M., and Linn, S. (1988) Toxic DNA damage by hydrogen peroxide through the Fenton reaction in vivo and in vitro. Science 240: 640-642.
    • (1988) Science , vol.240 , pp. 640-642
    • Imlay, J.A.1    Chin, S.M.2    Linn, S.3
  • 15
    • 0030465238 scopus 로고    scopus 로고
    • Superoxide accelerates DNA damage by elevating free iron levels
    • Keyer, K., and Imlay, J.A. (1996) Superoxide accelerates DNA damage by elevating free iron levels. Proc Natl Acad Sci USA 193: 13635-13640.
    • (1996) Proc Natl Acad Sci USA , vol.193 , pp. 13635-13640
    • Keyer, K.1    Imlay, J.A.2
  • 16
    • 79959435715 scopus 로고    scopus 로고
    • Spontaneous phthiocerol dimycocerosate-deficient variants of Mycobacterium tuberculosis are susceptible to gamma interferon-mediated immunity
    • Kirksey, M.A., Tischler, A.D., Simeone, R., Hisert, K.B., Uplekar, S., Guilhot, C., and McKinney, J.D. (2011) Spontaneous phthiocerol dimycocerosate-deficient variants of Mycobacterium tuberculosis are susceptible to gamma interferon-mediated immunity. Infect Immun 79: 2829-2838.
    • (2011) Infect Immun , vol.79 , pp. 2829-2838
    • Kirksey, M.A.1    Tischler, A.D.2    Simeone, R.3    Hisert, K.B.4    Uplekar, S.5    Guilhot, C.6    McKinney, J.D.7
  • 17
    • 58449097413 scopus 로고    scopus 로고
    • Mycobacterium tubeculosis expresses methionine sulpoxide reductases A and B that protect from killing by nitrite and hypochlorite
    • Lee, W.L., Gold, B., Darby, C., Brot, N., Jiang, X., Carvalho, L.P.S., etal. (2009) Mycobacterium tubeculosis expresses methionine sulpoxide reductases A and B that protect from killing by nitrite and hypochlorite. Mol Microbiol 71: 583-593.
    • (2009) Mol Microbiol , vol.71 , pp. 583-593
    • Lee, W.L.1    Gold, B.2    Darby, C.3    Brot, N.4    Jiang, X.5    Carvalho, L.P.S.6
  • 18
    • 0026034432 scopus 로고
    • Role of nitric oxide synthesis in macrophage antimicrobial activity
    • Nathan, C.F., and Hibbs, J.B., Jr. (1991) Role of nitric oxide synthesis in macrophage antimicrobial activity. Curr Opin Immunol 3: 65.
    • (1991) Curr Opin Immunol , vol.3 , pp. 65
    • Nathan, C.F.1    Hibbs Jr., J.B.2
  • 19
    • 84891157416 scopus 로고    scopus 로고
    • Intraphagosomal Mycobacterium tuberculosis acquires iron from both extracellular transferrin and intracellular iron pools: impact of interferon-gamma and hemochromatosis
    • Olakanmi, O., Schlesinger, L.S., Ahmed, A., and Britigan, B.E. (2002) Intraphagosomal Mycobacterium tuberculosis acquires iron from both extracellular transferrin and intracellular iron pools: impact of interferon-gamma and hemochromatosis. J Biol Chem 23: 23.
    • (2002) J Biol Chem , vol.23 , pp. 23
    • Olakanmi, O.1    Schlesinger, L.S.2    Ahmed, A.3    Britigan, B.E.4
  • 20
    • 0028821822 scopus 로고
    • Nitric oxide potentiates hydrogen peroxide-induced killing of Escherichia coli
    • Pacelli, R., Wink, D.A., Cook, J.A., Krishna, M.C., DeGraff, W., and Friedman, N. (1995) Nitric oxide potentiates hydrogen peroxide-induced killing of Escherichia coli. J Exp Med 182: 1469-1479.
    • (1995) J Exp Med , vol.182 , pp. 1469-1479
    • Pacelli, R.1    Wink, D.A.2    Cook, J.A.3    Krishna, M.C.4    DeGraff, W.5    Friedman, N.6
  • 21
    • 84867584201 scopus 로고    scopus 로고
    • A ferritin mutant of Mycobacterium tuberculosis is highly suceptible to killing by antibiotics and is unable to establish a chronic infection in mice
    • Pandey, R., and Rodriguez, G.M. (2012) A ferritin mutant of Mycobacterium tuberculosis is highly suceptible to killing by antibiotics and is unable to establish a chronic infection in mice. Infect Immun 80: 3650-3659.
    • (2012) Infect Immun , vol.80 , pp. 3650-3659
    • Pandey, R.1    Rodriguez, G.M.2
  • 22
    • 0032211974 scopus 로고    scopus 로고
    • Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin
    • Quadri, L.E.N., Sello, J., Keating, T.A., Weinreb, P.H., and Walsh, C.T. (1998) Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem Biol 5: 631-645.
    • (1998) Chem Biol , vol.5 , pp. 631-645
    • Quadri, L.E.N.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 23
    • 3242657100 scopus 로고    scopus 로고
    • Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells
    • Riemer, J., Hoepken, H.H., Czerwinska, H., Robinson, S.R., and Drigen, R. (2004) Colorimetric ferrozine-based assay for the quantitation of iron in cultured cells. Anal Biochem 331: 370-375.
    • (2004) Anal Biochem , vol.331 , pp. 370-375
    • Riemer, J.1    Hoepken, H.H.2    Czerwinska, H.3    Robinson, S.R.4    Drigen, R.5
  • 24
    • 30744441922 scopus 로고    scopus 로고
    • Identification of an ABC Transporter Required for Iron Acquisition and Virulence in Mycobacterium tuberculosis
    • Rodriguez, G.M., and Smith, I. (2006) Identification of an ABC Transporter Required for Iron Acquisition and Virulence in Mycobacterium tuberculosis. J Bacteriol 188: 424-430.
    • (2006) J Bacteriol , vol.188 , pp. 424-430
    • Rodriguez, G.M.1    Smith, I.2
  • 25
    • 0036081140 scopus 로고    scopus 로고
    • ideR, An essential gene in Mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response
    • Rodriguez, G.M., Voskuil, M.I., Gold, B., Schoolnik, G.K., and 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.
    • (2002) Infect Immun , vol.70 , pp. 3371-3381
    • Rodriguez, G.M.1    Voskuil, M.I.2    Gold, B.3    Schoolnik, G.K.4    Smith, I.5
  • 26
    • 75149120767 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain
    • Ryndak, M.B., Wang, S., Smith, I., and Rodriguez, G.M. (2010) The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain. J Bacteriol 192: 861-869.
    • (2010) J Bacteriol , vol.192 , pp. 861-869
    • Ryndak, M.B.1    Wang, S.2    Smith, I.3    Rodriguez, G.M.4
  • 27
    • 0032998791 scopus 로고    scopus 로고
    • Antimicrobial activities of benzoxazinorifamycin (KRM-1648) and clarithromycin against Mycobacterium avium-intracellular complex within murine peritoneal macrophages, human macrophage-like cells and human alveolar epithelial cells
    • Sato, K., and Tomioka, H. (1999) Antimicrobial activities of benzoxazinorifamycin (KRM-1648) and clarithromycin against Mycobacterium avium-intracellular complex within murine peritoneal macrophages, human macrophage-like cells and human alveolar epithelial cells. J Antimicrob Chemother 43: 351-357.
    • (1999) J Antimicrob Chemother , vol.43 , pp. 351-357
    • Sato, K.1    Tomioka, H.2
  • 28
    • 33750068255 scopus 로고    scopus 로고
    • Metal-linked dimerization in the iron dependent regulator from Mycobacterium tuberculosis
    • Semavina, M., Beckett, D., and Logan, T.M. (2006) Metal-linked dimerization in the iron dependent regulator from Mycobacterium tuberculosis. Biochemistry 45: 12480-12490.
    • (2006) Biochemistry , vol.45 , pp. 12480-12490
    • Semavina, M.1    Beckett, D.2    Logan, T.M.3
  • 29
    • 0014803645 scopus 로고
    • Mycobactins: iron chelating growth factors from mycobacteria
    • Snow, G.A. (1970) Mycobactins: iron chelating growth factors from mycobacteria. Bacteriol Rev 34: 99-125.
    • (1970) Bacteriol Rev , vol.34 , pp. 99-125
    • Snow, G.A.1
  • 30
    • 84875459549 scopus 로고    scopus 로고
    • Z(II) stimulation of Fe(II)-activated repression in the iron-dependent repressor from Mycobacterium tuberculosis
    • Stapleton, B., Walker, L., and Logan, T.M. (2013) Z(II) stimulation of Fe(II)-activated repression in the iron-dependent repressor from Mycobacterium tuberculosis. Biochemistry 19: 1927-1938.
    • (2013) Biochemistry , vol.19 , pp. 1927-1938
    • Stapleton, B.1    Walker, L.2    Logan, T.M.3
  • 32
    • 12444344631 scopus 로고    scopus 로고
    • Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system
    • Wagner, D., Maser, J., Lai, B., Cai, Z., Barry, C.E., 3rd, Honer Zu Bentrup, K., etal. (2005) Elemental analysis of Mycobacterium avium-, Mycobacterium tuberculosis-, and Mycobacterium smegmatis-containing phagosomes indicates pathogen-induced microenvironments within the host cell's endosomal system. J Immunol 174: 1491-1500.
    • (2005) J Immunol , vol.174 , pp. 1491-1500
    • Wagner, D.1    Maser, J.2    Lai, B.3    Cai, Z.4    Barry 3rd, C.E.5    Honer Zu Bentrup, K.6
  • 33
    • 57649207910 scopus 로고    scopus 로고
    • How do bacterial cells ensure that metalloproteins get the correct metal?
    • Waldron, K., and Robinson, N. (2009) How do bacterial cells ensure that metalloproteins get the correct metal? Nat Rev 6: 25-36.
    • (2009) Nat Rev , vol.6 , pp. 25-36
    • Waldron, K.1    Robinson, N.2
  • 34
    • 0021356806 scopus 로고
    • Iron withholding: a defense against infection and neoplasia
    • Weinberg, E.D. (1984) Iron withholding: a defense against infection and neoplasia. Physiol Rev 64: 65-102.
    • (1984) Physiol Rev , vol.64 , pp. 65-102
    • Weinberg, E.D.1
  • 35
    • 0038046842 scopus 로고    scopus 로고
    • A mechanism by which nitric oxide accelerates the rate of oxidative DNA damge in Excherichia coli
    • Woodmansee, A.N., and Imlay, J.A. (2003) A mechanism by which nitric oxide accelerates the rate of oxidative DNA damge in Excherichia coli. Mol Microbiol 49: 11-22.
    • (2003) Mol Microbiol , vol.49 , pp. 11-22
    • Woodmansee, A.N.1    Imlay, J.A.2
  • 36
    • 0020358807 scopus 로고
    • Iron requirement in the bactericidal mechanism of streptonigrin
    • Yeowell, H.N., and White, J.R. (1982) Iron requirement in the bactericidal mechanism of streptonigrin. Antimicrob Agents Chemother 22: 961-968.
    • (1982) Antimicrob Agents Chemother , vol.22 , pp. 961-968
    • Yeowell, H.N.1    White, J.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.