메뉴 건너뛰기




Volumn 31, Issue 1, 2013, Pages 1-13

Comparative genomic insights into the biosynthesis and regulation of mycobacterial siderophores

Author keywords

Anti tuberculosis; Biosynthesis; Mycobacteria; Siderophore

Indexed keywords

EXOCHELIN; IRON; MYCOBACTIN; NONRIBOSOMAL PEPTIDE SYNTHETASE; POLYKETIDE SYNTHASE; SIDEROPHORE; UNCLASSIFIED DRUG;

EID: 84872801360     PISSN: 10158987     EISSN: 14219778     Source Type: Journal    
DOI: 10.1159/000343343     Document Type: Review
Times cited : (13)

References (72)
  • 2
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C, Dover LG: Iron metabolism in pathogenic bacteria. Annu Rev Microbiol 2000;54:881-941.
    • (2000) Annu Rev Microbiol , vol.54 , pp. 881-941
    • Ratledge, C.1    Dover, L.G.2
  • 4
    • 0027256664 scopus 로고
    • Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase
    • Kjeldsen L, Johnsen AH, Sengelov H, Borregaard N: Isolation and primary structure of NGAL, a novel protein associated with human neutrophil gelatinase. J Biol Chem 1993;268:10425-10432.
    • (1993) J Biol Chem , vol.268 , pp. 10425-10432
    • Kjeldsen, L.1    Johnsen, A.H.2    Sengelov, H.3    Borregaard, N.4
  • 5
    • 34247893749 scopus 로고    scopus 로고
    • Host-pathogen interactions: The role of iron
    • Doherty CP: Host-pathogen interactions: the role of iron. J Nutr 2007;137:1341-1344.
    • (2007) J Nutr , vol.137 , pp. 1341-1344
    • Doherty, C.P.1
  • 8
    • 0347722524 scopus 로고    scopus 로고
    • Iron, mycobacteria and tuberculosis
    • Ratledge C: Iron, mycobacteria and tuberculosis. Tuberculosis (Edinb) 2004;84:110-130.
    • (2004) Tuberculosis (Edinb) , vol.84 , pp. 110-130
    • Ratledge, C.1
  • 9
    • 0014803645 scopus 로고
    • Mycobactins: Iron-chelating growth factors from mycobacteria
    • Snow GA: Mycobactins: iron-chelating growth factors from mycobacteria. Bacteriol Rev 1970;34:99-125.
    • (1970) Bacteriol Rev , vol.34 , pp. 99-125
    • Snow, G.A.1
  • 10
    • 51849155973 scopus 로고    scopus 로고
    • Inhibition of siderophore biosynthesis in Mycobacterium tuberculosis with nucleoside bisubstrate analogues: Structure-activity relationships of the nucleobase domain of 5'-O-[N-(salicyl)sulfamoyl] adenosine
    • Neres J, Labello NP, Somu RV, Boshoff HI, Wilson DJ, Vannada J, Chen L, Barry CE, 3rd, Bennett EM, Aldrich CC: Inhibition of siderophore biosynthesis in Mycobacterium tuberculosis with nucleoside bisubstrate analogues: structure-activity relationships of the nucleobase domain of 5'-O-[N-(salicyl)sulfamoyl] adenosine. J Med Chem 2008;51:5349-5370.
    • (2008) J Med Chem , vol.51 , pp. 5349-5370
    • Neres, J.1    Labello, N.P.2    Somu, R.V.3    Boshoff, H.I.4    Wilson, D.J.5    Vannada, J.6    Chen, L.7    Barry, C.E.8    Bennett, E.M.9    Aldrich, C.C.10
  • 12
    • 33750378701 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of beta-ketosulfonamide adenylation inhibitors as potential antitubercular agents
    • Vannada J, Bennett EM, Wilson DJ, Boshoff HI, Barry CE, 3rd, Aldrich CC: Design, synthesis, and biological evaluation of beta-ketosulfonamide adenylation inhibitors as potential antitubercular agents. Org Lett 2006;8:4707-4710.
    • (2006) Org Lett , vol.8 , pp. 4707-4710
    • Vannada, J.1    Bennett, E.M.2    Wilson, D.J.3    Boshoff, H.I.4    Barry, C.E.5    Aldrich, C.C.6
  • 14
    • 41849151739 scopus 로고    scopus 로고
    • Small molecules with structural similarities to siderophores as novel antimicrobials against Mycobacterium tuberculosis and Yersinia pestis
    • Stirrett KL, Ferreras JA, Jayaprakash V, Sinha BN, Ren T, Quadri LE: Small molecules with structural similarities to siderophores as novel antimicrobials against Mycobacterium tuberculosis and Yersinia pestis. Bioorg Med Chem Lett 2008;18:2662-2668.
    • (2008) Bioorg Med Chem Lett , vol.18 , pp. 2662-2668
    • Stirrett, K.L.1    Ferreras, J.A.2    Jayaprakash, V.3    Sinha, B.N.4    Ren, T.5    Quadri, L.E.6
  • 15
    • 0008938031 scopus 로고
    • How Microorganisms Transport Iron: In the midst of plenty, microorganisms are often in danger of iron-starvation; The mechanism by which they transport iron has now been elucidated
    • Lewin R: How Microorganisms Transport Iron: In the midst of plenty, microorganisms are often in danger of iron-starvation; the mechanism by which they transport iron has now been elucidated. Science 1984;225:401-402.
    • (1984) Science , vol.225 , pp. 401-402
    • Lewin, R.1
  • 17
    • 0030795074 scopus 로고    scopus 로고
    • Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis
    • Lundrigan MD, Arceneaux JE, Zhu W, Byers BR: Enhanced hydrogen peroxide sensitivity and altered stress protein expression in iron-starved Mycobacterium smegmatis. Biometals 1997;10:215-225.
    • (1997) Biometals , vol.10 , pp. 215-225
    • Lundrigan, M.D.1    Arceneaux, J.E.2    Zhu, W.3    Byers, B.R.4
  • 18
    • 0031783529 scopus 로고    scopus 로고
    • Analysis of the exochelin locus in Mycobacterium smegmatis: Biosynthesis genes have homology with genes of the peptide synthetase family
    • Yu S, Fiss E, Jacobs WR Jr: Analysis of the exochelin locus in Mycobacterium smegmatis: biosynthesis genes have homology with genes of the peptide synthetase family. J Bacteriol 1998;180:4676-4685.
    • (1998) J Bacteriol , vol.180 , pp. 4676-4685
    • Yu, S.1    Fiss, E.2    Jacobs, W.R.3
  • 19
    • 34748861878 scopus 로고    scopus 로고
    • The role of iron in Mycobacterium smegmatis biofilm formation: The exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth
    • Ojha A, Hatfull GF: The role of iron in Mycobacterium smegmatis biofilm formation: the exochelin siderophore is essential in limiting iron conditions for biofilm formation but not for planktonic growth. Mol Microbiol 2007;66:468-483.
    • (2007) Mol Microbiol , vol.66 , pp. 468-483
    • Ojha, A.1    Hatfull, G.F.2
  • 20
    • 0028999977 scopus 로고
    • Iron acquisition by Mycobacterium tuberculosis: Isolation and characterization of a family of iron-binding exochelins
    • Gobin J, Moore CH, Reeve JR Jr, Wong DK, Gibson BW, Horwitz MA: Iron acquisition by Mycobacterium tuberculosis: isolation and characterization of a family of iron-binding exochelins. Proc Natl Acad Sci U S A 1995;92:5189-5193.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5189-5193
    • Gobin, J.1    Moore, C.H.2    Reeve, J.R.3    Wong, D.K.4    Gibson, B.W.5    Horwitz, M.A.6
  • 21
    • 0000153193 scopus 로고
    • Isolation and structure of mycobactin T, a growth factor from Mycobacterium tuberculosis
    • Snow GA: Isolation and structure of mycobactin T, a growth factor from Mycobacterium tuberculosis. Biochem J 1965;97:166-175.
    • (1965) Biochem J , vol.97 , pp. 166-175
    • Snow, G.A.1
  • 22
    • 0029839633 scopus 로고    scopus 로고
    • The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis
    • Ratledge C, Ewing M: The occurrence of carboxymycobactin, the siderophore of pathogenic mycobacteria, as a second extracellular siderophore in Mycobacterium smegmatis. Microbiology 1996;142:2207-2212.
    • (1996) Microbiology , vol.142 , pp. 2207-2212
    • Ratledge, C.1    Ewing, M.2
  • 23
    • 0028854121 scopus 로고
    • Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis
    • Sharman GJ, Williams DH, Ewing DF, Ratledge C: Isolation, purification and structure of exochelin MS, the extracellular siderophore from Mycobacterium smegmatis. Biochem J 1995;305:187-196.
    • (1995) Biochem J , vol.305 , pp. 187-196
    • Sharman, G.J.1    Williams, D.H.2    Ewing, D.F.3    Ratledge, C.4
  • 24
    • 0029058855 scopus 로고
    • Novel Extracellular Mycobactins, the Carboxymycobactins from Mycobacterium avium
    • Lane SJ, Marshall PS, Upton RJ: Novel Extracellular Mycobactins, the Carboxymycobactins from Mycobacterium avium. Tetrahedron Letters 1995;36:4129-4132.
    • (1995) Tetrahedron Letters , vol.36 , pp. 4129-4132
    • Lane, S.J.1    Marshall, P.S.2    Upton, R.J.3
  • 25
    • 0029347184 scopus 로고
    • Determination of the structure of exochelin MN, the extracellular siderophore from Mycobacterium neoaurum
    • Sharman GJ, Williams DH, Ewing DF, Ratledge C: Determination of the structure of exochelin MN, the extracellular siderophore from Mycobacterium neoaurum. Chem Biol 1995;2:553-561.
    • (1995) Chem Biol , vol.2 , pp. 553-561
    • Sharman, G.J.1    Williams, D.H.2    Ewing, D.F.3    Ratledge, C.4
  • 26
    • 1642484975 scopus 로고    scopus 로고
    • Microbial growth promotion studies of exochelin MN and analogues thereof
    • Dong L, Miller MJ, Mollmann U: Microbial growth promotion studies of exochelin MN and analogues thereof. Biometals 2004;17:99-104.
    • (2004) Biometals , vol.17 , pp. 99-104
    • Dong, L.1    Miller, M.J.2    Mollmann, U.3
  • 27
    • 0023142668 scopus 로고
    • Exochelin-mediated iron acquisition by the leprosy bacillus, Mycobacterium leprae
    • Hall RM, Ratledge C: Exochelin-mediated iron acquisition by the leprosy bacillus, Mycobacterium leprae. J Gen Microbiol 1987;133:193-199.
    • (1987) J Gen Microbiol , vol.133 , pp. 193-199
    • Hall, R.M.1    Ratledge, C.2
  • 28
    • 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 LE, Sello J, Keating TA, Weinreb PH, Walsh CT: Identification of a Mycobacterium tuberculosis gene cluster encoding the biosynthetic enzymes for assembly of the virulence-conferring siderophore mycobactin. Chem Biol 1998;5:631-645.
    • (1998) Chem Biol , vol.5 , pp. 631-645
    • Quadri, L.E.1    Sello, J.2    Keating, T.A.3    Weinreb, P.H.4    Walsh, C.T.5
  • 31
    • 33344470984 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic analysis of MbtI, a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis
    • Harrison AJ, Ramsay RJ, Baker EN, Lott JS: Crystallization and preliminary X-ray crystallographic analysis of MbtI, a protein essential for siderophore biosynthesis in Mycobacterium tuberculosis. Acta Crystallogr Sect F Struct Biol Cryst Commun 2005;61:121-123.
    • (2005) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.61 , pp. 121-123
    • Harrison, A.J.1    Ramsay, R.J.2    Baker, E.N.3    Lott, J.S.4
  • 32
    • 33749033361 scopus 로고    scopus 로고
    • The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase
    • Harrison AJ, Yu M, Gardenborg T, Middleditch M, Ramsay RJ, Baker EN, Lott JS: The structure of MbtI from Mycobacterium tuberculosis, the first enzyme in the biosynthesis of the siderophore mycobactin, reveals it to be a salicylate synthase. J Bacteriol 2006;188:6081-6091.
    • (2006) J Bacteriol , vol.188 , pp. 6081-6091
    • Harrison, A.J.1    Yu, M.2    Gardenborg, T.3    Middleditch, M.4    Ramsay, R.J.5    Baker, E.N.6    Lott, J.S.7
  • 33
    • 0346024114 scopus 로고    scopus 로고
    • Participation of fad and mbt genes in synthesis of mycobactin in Mycobacterium smegmatis
    • LaMarca BB, Zhu W, Arceneaux JE, Byers BR, Lundrigan MD: Participation of fad and mbt genes in synthesis of mycobactin in Mycobacterium smegmatis. J Bacteriol 2004;186:374-382.
    • (2004) J Bacteriol , vol.186 , pp. 374-382
    • Lamarca, B.B.1    Zhu, W.2    Arceneaux, J.E.3    Byers, B.R.4    Lundrigan, M.D.5
  • 34
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa JH, Walsh CT: Genetics and assembly line enzymology of siderophore biosynthesis in bacteria. Microbiol Mol Biol Rev 2002;66:223-249.
    • (2002) Microbiol Mol Biol Rev , vol.66 , pp. 223-249
    • Crosa, J.H.1    Walsh, C.T.2
  • 36
    • 1842577641 scopus 로고    scopus 로고
    • Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria
    • Trivedi OA, Arora P, Sridharan V, Tickoo R, Mohanty D, Gokhale RS: Enzymic activation and transfer of fatty acids as acyl-adenylates in mycobacteria. Nature 2004;428:441-445.
    • (2004) Nature , vol.428 , pp. 441-445
    • Trivedi, O.A.1    Arora, P.2    Sridharan, V.3    Tickoo, R.4    Mohanty, D.5    Gokhale, R.S.6
  • 37
    • 0842330598 scopus 로고    scopus 로고
    • Acyl-CoA dehydrogenases. A mechanistic overview
    • Ghisla S, Thorpe C: Acyl-CoA dehydrogenases. A mechanistic overview. Eur J Biochem 2004, 271:494-508.
    • (2004) Eur J Biochem , vol.271 , pp. 494-508
    • Ghisla, S.1    Thorpe, C.2
  • 39
    • 0028127357 scopus 로고
    • Identification of genes involved in the sequestration of iron in mycobacteria: The ferric exochelin biosynthetic and uptake pathways
    • Fiss EH, Yu S, Jacobs WR Jr: Identification of genes involved in the sequestration of iron in mycobacteria: the ferric exochelin biosynthetic and uptake pathways. Mol Microbiol 1994;14:557-569.
    • (1994) Mol Microbiol , vol.14 , pp. 557-569
    • Fiss, E.H.1    Yu, S.2    Jacobs, W.R.3
  • 40
    • 0031820390 scopus 로고    scopus 로고
    • Exochelin genes in Mycobacterium smegmatis: Identification of an ABC transporter and two non-ribosomal peptide synthetase genes
    • Zhu W, Arceneaux JE, Beggs ML, Byers BR, Eisenach KD, Lundrigan MD: Exochelin genes in Mycobacterium smegmatis: identification of an ABC transporter and two non-ribosomal peptide synthetase genes. Mol Microbiol 1998;29:629-639.
    • (1998) Mol Microbiol , vol.29 , pp. 629-639
    • Zhu, W.1    Arceneaux, J.E.2    Beggs, M.L.3    Byers, B.R.4    Eisenach, K.D.5    Lundrigan, M.D.6
  • 42
    • 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 GM, Voskuil MI, Gold B, Schoolnik GK, Smith I: ideR, An essential gene in mycobacterium tuberculosis: role of IdeR in iron-dependent gene expression, iron metabolism, and oxidative stress response. Infect Immun 2002;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
  • 43
    • 0029809920 scopus 로고    scopus 로고
    • An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response
    • Dussurget O, Rodriguez M, Smith I: An ideR mutant of Mycobacterium smegmatis has derepressed siderophore production and an altered oxidative-stress response. Mol Microbiol 1996;22:535-544.
    • (1996) Mol Microbiol , vol.22 , pp. 535-544
    • Dussurget, O.1    Rodriguez, M.2    Smith, I.3
  • 45
    • 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 GM, Marras SA, Pentecost M, Smith I: 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 2001;42:851-865.
    • (2001) Mol Microbiol , vol.42 , pp. 851-865
    • Gold, B.1    Rodriguez, G.M.2    Marras, S.A.3    Pentecost, M.4    Smith, I.5
  • 46
    • 33750309104 scopus 로고    scopus 로고
    • Identification and characterization of a major cell wall-associated iron-regulated envelope protein (Irep-28) in Mycobacterium tuberculosis
    • Yeruva VC, Duggirala S, Lakshmi V, Kolarich D, Altmann F, Sritharan M: Identification and characterization of a major cell wall-associated iron-regulated envelope protein (Irep-28) in Mycobacterium tuberculosis. Clin Vaccine Immunol 2006;13:1137-1142.
    • (2006) Clin Vaccine Immunol , vol.13 , pp. 1137-1142
    • Yeruva, V.C.1    Duggirala, S.2    Lakshmi, V.3    Kolarich, D.4    Altmann, F.5    Sritharan, M.6
  • 47
    • 0031932979 scopus 로고    scopus 로고
    • Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems
    • Calder KM, Horwitz MA: Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microbial Pathogenesis 1998;24:133-143.
    • (1998) Microbial Pathogenesis , vol.24 , pp. 133-143
    • Calder, K.M.1    Horwitz, M.A.2
  • 48
    • 0024970937 scopus 로고
    • Co-ordinated expression of the components of iron transport (mycobactin, exochelin and envelope proteins) in Mycobacterium neoaurum
    • Sritharan M, Ratledge C: Co-ordinated expression of the components of iron transport (mycobactin, exochelin and envelope proteins) in Mycobacterium neoaurum. FEMS Microbiol Lett 1989;51:183-185.
    • (1989) FEMS Microbiol Lett , vol.51 , pp. 183-185
    • Sritharan, M.1    Ratledge, C.2
  • 49
    • 0033986292 scopus 로고    scopus 로고
    • Mutational analysis of a role for salicylic acid in iron metabolism of Mycobacterium smegmatis
    • Adilakshmi T, Ayling PD, Ratledge C: Mutational analysis of a role for salicylic acid in iron metabolism of Mycobacterium smegmatis. J Bacteriol 2000;182:264-271.
    • (2000) J Bacteriol , vol.182 , pp. 264-271
    • Adilakshmi, T.1    Ayling, P.D.2    Ratledge, C.3
  • 50
    • 0029913805 scopus 로고    scopus 로고
    • Exochelins of mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. Tuberculosis cell wall
    • Gobin J, Horwitz MA: Exochelins of Mycobacterium tuberculosis remove iron from human iron-binding proteins and donate iron to mycobactins in the M. tuberculosis cell wall. J Exp Med 1996;183:1527-1532.
    • (1996) J Exp Med , vol.183 , pp. 1527-1532
    • Gobin, J.1    Horwitz, M.A.2
  • 51
    • 47749094684 scopus 로고    scopus 로고
    • Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron
    • Farhana A, Kumar S, Rathore SS, Ghosh PC, Ehtesham NZ, Tyagi AK, Hasnain SE: Mechanistic insights into a novel exporter-importer system of Mycobacterium tuberculosis unravel its role in trafficking of iron. PLoS One 2008; 3:e2087.
    • (2008) PLoS One , vol.3 , pp. e2087
    • Farhana, A.1    Kumar, S.2    Rathore, S.S.3    Ghosh, P.C.4    Ehtesham, N.Z.5    Tyagi, A.K.6    Hasnain, S.E.7
  • 52
    • 0023388769 scopus 로고
    • Iron transport in Mycobacterium smegmatis: Occurrence of iron-regulated envelope proteins as potential receptors for iron uptake
    • Hall RM, Sritharan M, Messenger AJ, Ratledge C: Iron transport in Mycobacterium smegmatis: occurrence of iron-regulated envelope proteins as potential receptors for iron uptake. J Gen Microbiol 1987;133:2107-2114.
    • (1987) J Gen Microbiol , vol.133 , pp. 2107-2114
    • Hall, R.M.1    Sritharan, M.2    Messenger, A.J.3    Ratledge, C.4
  • 53
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M, Marahiel MA: Siderophore-based iron acquisition and pathogen control. Microbiol Mol Biol Rev 2007;71:413-451.
    • (2007) Microbiol Mol Biol Rev , vol.71 , pp. 413-451
    • Miethke, M.1    Marahiel, M.A.2
  • 54
    • 75149120767 scopus 로고    scopus 로고
    • The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain
    • Ryndak MB, Wang S, Smith I, Rodriguez GM: The Mycobacterium tuberculosis high-affinity iron importer, IrtA, contains an FAD-binding domain. J Bacteriol 2010;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
  • 55
    • 30744441922 scopus 로고    scopus 로고
    • Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis
    • Rodriguez GM, Smith I: Identification of an ABC transporter required for iron acquisition and virulence in Mycobacterium tuberculosis. J Bacteriol 2006;188:424-430.
    • (2006) J Bacteriol , vol.188 , pp. 424-430
    • Rodriguez, G.M.1    Smith, I.2
  • 58
    • 0031932979 scopus 로고    scopus 로고
    • Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems
    • Calder KM, Horwitz MA: Identification of iron-regulated proteins of Mycobacterium tuberculosis and cloning of tandem genes encoding a low iron-induced protein and a metal transporting ATPase with similarities to two-component metal transport systems. Microb Pathog 1998;24:133-143.
    • (1998) Microb Pathog , vol.24 , pp. 133-143
    • Calder, K.M.1    Horwitz, M.A.2
  • 59
    • 0032718515 scopus 로고    scopus 로고
    • Porins in the cell wall of Mycobacterium tuberculosis
    • Kartmann B, Stenger S, Niederweis M: Porins in the cell wall of Mycobacterium tuberculosis. J Bacteriol 1999;181:6543-6546.
    • (1999) J Bacteriol , vol.181 , pp. 6543-6546
    • Kartmann, B.1    Stenger, S.2    Niederweis, M.3
  • 60
    • 78649662340 scopus 로고    scopus 로고
    • Role of Porins in Iron Uptake by Mycobacterium smegmatis
    • Jones CM NM: Role of Porins in Iron Uptake by Mycobacterium smegmatis. J Bacteriol 2010;192:6411-6417.
    • (2010) J Bacteriol , vol.192 , pp. 6411-6417
    • Jones, C.M.N.M.1
  • 61
    • 30444432680 scopus 로고    scopus 로고
    • Mycobactin-mediated iron acquisition within macrophages
    • Luo M, Fadeev EA, Groves JT: Mycobactin-mediated iron acquisition within macrophages. Nat Chem Biol 2005;1:149-153.
    • (2005) Nat Chem Biol , vol.1 , pp. 149-153
    • Luo, M.1    Fadeev, E.A.2    Groves, J.T.3
  • 62
    • 0021083544 scopus 로고
    • Lipid bodies: Cytoplasmic organelles important to arachidonate metabolism in macrophages and mast cells
    • Dvorak AM: Lipid bodies: cytoplasmic organelles important to arachidonate metabolism in macrophages and mast cells. J Immunol 1983;131:2965-2976.
    • (1983) J Immunol , vol.131 , pp. 2965-2976
    • Dvorak, A.M.1
  • 63
    • 0034903123 scopus 로고    scopus 로고
    • The biogenesis and functions of lipid bodies in animals, plants and microorganisms
    • Murphy DJ: The biogenesis and functions of lipid bodies in animals, plants and microorganisms. Lipid Res 2001;40:325-438.
    • (2001) Lipid Res , vol.40 , pp. 325-438
    • Murphy, D.J.1
  • 64
    • 0033973479 scopus 로고    scopus 로고
    • The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages
    • De Voss JJ, Rutter K, Schroeder BG, Su H, Zhu Y, Barry CE 3rd: The salicylate-derived mycobactin siderophores of Mycobacterium tuberculosis are essential for growth in macrophages. Proc Natl Acad Sci USA 2000;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, Y.5    Barry, C.E.6
  • 65
    • 55849112610 scopus 로고    scopus 로고
    • A Replication-Limited Recombinant Mycobacterium bovis BCG vaccine against tuberculosis designed for human immunodeficiency viruspositive persons is safer and more efficacious than BCG
    • Tullius MV, Harth G, Maslesa-Galic S, Dillon BJ, Horwitz MA: A Replication-Limited Recombinant Mycobacterium bovis BCG vaccine against tuberculosis designed for human immunodeficiency viruspositive persons is safer and more efficacious than BCG. Infect Immun 2008;76:5200-5214.
    • (2008) Infect Immun , vol.76 , pp. 5200-5214
    • Tullius, M.V.1    Harth, G.2    Maslesa-Galic, S.3    Dillon, B.J.4    Horwitz, M.A.5
  • 66
    • 37849036789 scopus 로고    scopus 로고
    • 5'-O-[(N-acyl) sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: An adenylation enzyme required for siderophore biosynthesis of the mycobactins
    • Qiao C, Gupte A, Boshoff HI, Wilson DJ, Bennett EM, Somu RV, Barry CE, 3rd, Aldrich CC: 5'-O-[(N-acyl) sulfamoyl]adenosines as antitubercular agents that inhibit MbtA: an adenylation enzyme required for siderophore biosynthesis of the mycobactins. J Med Chem 2007;50:6080-6094.
    • (2007) J Med Chem , vol.50 , pp. 6080-6094
    • Qiao, C.1    Gupte, A.2    Boshoff, H.I.3    Wilson, D.J.4    Bennett, E.M.5    Somu, R.V.6    Barry, C.E.7    Aldrich, C.C.8
  • 67
    • 30444445995 scopus 로고    scopus 로고
    • Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis
    • Somu RV, Boshoff H, Qiao C, Bennett EM, Barry CE, 3rd, Aldrich CC: Rationally designed nucleoside antibiotics that inhibit siderophore biosynthesis of Mycobacterium tuberculosis. J Med Chem 2006;49:31-34.
    • (2006) J Med Chem , vol.49 , pp. 31-34
    • Somu, R.V.1    Boshoff, H.2    Qiao, C.3    Bennett, E.M.4    Barry, C.E.5    Aldrich, C.C.6
  • 68
    • 19544383636 scopus 로고    scopus 로고
    • Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames
    • Prakash P, Yellaboina S, Ranjan A, Hasnain SE: Computational prediction and experimental verification of novel IdeR binding sites in the upstream sequences of Mycobacterium tuberculosis open reading frames. Bioinformatics 2005;21:2161-2166.
    • (2005) Bioinformatics , vol.21 , pp. 2161-2166
    • Prakash, P.1    Yellaboina, S.2    Ranjan, A.3    Hasnain, S.E.4
  • 69
    • 19744376797 scopus 로고    scopus 로고
    • Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance
    • Domenech P, Reed MB, Barry CE 3rd: Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance. Infect Immun 2005;73:3492-3501.
    • (2005) Infect Immun , vol.73 , pp. 3492-3501
    • Domenech, P.1    Reed, M.B.2    Barry, C.E.3
  • 70
    • 0037849870 scopus 로고    scopus 로고
    • Analysis of virulence plasmid gene expression of intra-macrophage and in vitro grown Rhodococcus equi ATCC 33701
    • Ren J, Prescott JF: Analysis of virulence plasmid gene expression of intra-macrophage and in vitro grown Rhodococcus equi ATCC 33701. Vet Microbiol 2003;94:167-182.
    • (2003) Vet Microbiol , vol.94 , pp. 167-182
    • Ren, J.1    Prescott, J.F.2
  • 72
    • 84867584201 scopus 로고    scopus 로고
    • A ferritin mutant of Mycobacterium tuberculosis is highly susceptible to killing by antibiotics and is unable to establish a chronic infection in mice
    • Pandey R, Rodriguez GM: A ferritin mutant of Mycobacterium tuberculosis is highly susceptible to killing by antibiotics and is unable to establish a chronic infection in mice. Infect Immun 2012;80:3650-3659.
    • (2012) Infect Immun , vol.80 , pp. 3650-3659
    • Pandey, R.1    Rodriguez, G.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.