메뉴 건너뛰기




Volumn 153, Issue 1-2, 2011, Pages 89-98

The Ins and Outs of siderophore mediated iron uptake by extra-intestinal pathogenic Escherichia coli

Author keywords

Colibacillosis; Escherichia coli; Extraintestinal infection; Iron; Urinary tract infection; Vaccine

Indexed keywords

AEROBACTIN; ENTEROCHELIN; SALMOCHELIN; SIDEROPHORE; UNCLASSIFIED DRUG; YERSINIABACTIN;

EID: 80052539413     PISSN: 03781135     EISSN: 18732542     Source Type: Journal    
DOI: 10.1016/j.vetmic.2011.05.023     Document Type: Review
Times cited : (102)

References (120)
  • 1
    • 70349680258 scopus 로고    scopus 로고
    • Mucosal immunization with iron receptor antigens protects against urinary tract infection
    • Alteri C.J., Hagan E.C., Sivick K.E., Smith S.N., Mobley H.L. Mucosal immunization with iron receptor antigens protects against urinary tract infection. PLoS Pathog. 2009, 5:e1000586.
    • (2009) PLoS Pathog. , vol.5
    • Alteri, C.J.1    Hagan, E.C.2    Sivick, K.E.3    Smith, S.N.4    Mobley, H.L.5
  • 3
    • 73449084865 scopus 로고    scopus 로고
    • Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin
    • Bachman M.A., Miller V.L., Weiser J.N. Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin. PLoS Pathog. 2009, 5:e1000622.
    • (2009) PLoS Pathog. , vol.5
    • Bachman, M.A.1    Miller, V.L.2    Weiser, J.N.3
  • 6
    • 0022358804 scopus 로고
    • The ability of Salmonella typhimurium to produce the siderophore enterobactin is not a virulence factor in mouse typhoid
    • Benjamin W.H., Turnbough C.L., Posey B.S., Briles D.E. The ability of Salmonella typhimurium to produce the siderophore enterobactin is not a virulence factor in mouse typhoid. Infect. Immun. 1985, 50:392-397.
    • (1985) Infect. Immun. , vol.50 , pp. 392-397
    • Benjamin, W.H.1    Turnbough, C.L.2    Posey, B.S.3    Briles, D.E.4
  • 9
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun V., Braun M. Iron transport and signaling in Escherichia coli. FEBS Lett. 2002, 529:78-85.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 10
    • 0034999145 scopus 로고    scopus 로고
    • Functional analysis of yersiniabactin transport genes of Yersinia enterocolitica
    • Brem D., Pelludat C., Rakin A., Jacobi C.A., Heesemann J. Functional analysis of yersiniabactin transport genes of Yersinia enterocolitica. Microbiology 2001, 147:1115-1127.
    • (2001) Microbiology , vol.147 , pp. 1115-1127
    • Brem, D.1    Pelludat, C.2    Rakin, A.3    Jacobi, C.A.4    Heesemann, J.5
  • 11
    • 0023388247 scopus 로고
    • Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins
    • Burkhardt R., Braun V. Nucleotide sequence of the fhuC and fhuD genes involved in iron (III) hydroxamate transport: domains in FhuC homologous to ATP-binding proteins. Mol. Gen. Genet. 1987, 209:49-55.
    • (1987) Mol. Gen. Genet. , vol.209 , pp. 49-55
    • Burkhardt, R.1    Braun, V.2
  • 12
    • 0021179611 scopus 로고
    • A cluster of five genes specifying the aerobactin iron uptake system of plasmid ColV-K30
    • Carbonetti N.H., Williams P.H. A cluster of five genes specifying the aerobactin iron uptake system of plasmid ColV-K30. Infect. Immun. 1984, 46:7-12.
    • (1984) Infect. Immun. , vol.46 , pp. 7-12
    • Carbonetti, N.H.1    Williams, P.H.2
  • 13
    • 79953033922 scopus 로고    scopus 로고
    • Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extra-intestinal pathogenic Escherichia coli
    • doi:10.1111/j.1365-2958.2011.07570.x [Epub ahead of print]
    • Caza M., Lépine F., Dozois C.M. Secretion, but not overall synthesis, of catecholate siderophores contributes to virulence of extra-intestinal pathogenic Escherichia coli. Mol. Microbiol. 2011, doi:10.1111/j.1365-2958.2011.07570.x [Epub ahead of print].
    • (2011) Mol. Microbiol.
    • Caza, M.1    Lépine, F.2    Dozois, C.M.3
  • 14
    • 48849096801 scopus 로고    scopus 로고
    • Specific roles of the iroBCDEN genes in virulence of an avian pathogenic Escherichia coli O78 strain and in production of salmochelins
    • Caza M., Lepine F., Milot S., Dozois C.M. Specific roles of the iroBCDEN genes in virulence of an avian pathogenic Escherichia coli O78 strain and in production of salmochelins. Infect. Immun. 2008, 76:3539-3549.
    • (2008) Infect. Immun. , vol.76 , pp. 3539-3549
    • Caza, M.1    Lepine, F.2    Milot, S.3    Dozois, C.M.4
  • 15
    • 3242771398 scopus 로고    scopus 로고
    • Sequencing and analysis of the large virulence plasmid pLVPK of Klebsiella pneumoniae CG43
    • Chen Y.T., Chang H.Y., Lai Y.C., Pan C.C., Tsai S.F., Peng H.L. Sequencing and analysis of the large virulence plasmid pLVPK of Klebsiella pneumoniae CG43. Gene 2004, 337:189-198.
    • (2004) Gene , vol.337 , pp. 189-198
    • Chen, Y.T.1    Chang, H.Y.2    Lai, Y.C.3    Pan, C.C.4    Tsai, S.F.5    Peng, H.L.6
  • 16
    • 0025770263 scopus 로고
    • Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease
    • Chenault S.S., Earhart C.F. Organization of genes encoding membrane proteins of the Escherichia coli ferrienterobactin permease. Mol. Microbiol. 1991, 5:1405-1413.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1405-1413
    • Chenault, S.S.1    Earhart, C.F.2
  • 17
    • 0026713762 scopus 로고
    • Identification of hydrophobic proteins FepD and FepG of the Escherichia coli ferrienterobactin permease
    • Chenault S.S., Earhart C.F. Identification of hydrophobic proteins FepD and FepG of the Escherichia coli ferrienterobactin permease. J. Gen. Microbiol. 1992, 138:2167-2171.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 2167-2171
    • Chenault, S.S.1    Earhart, C.F.2
  • 19
    • 0023043186 scopus 로고
    • Isolation and properties of N epsilon-hydroxylysine:acetyl coenzyme A N epsilon-transacetylase from Escherichia coli pABN11
    • Coy M., Paw B.H., Bindereif A., Neilands J.B. Isolation and properties of N epsilon-hydroxylysine:acetyl coenzyme A N epsilon-transacetylase from Escherichia coli pABN11. Biochemistry 1986, 25:2485-2489.
    • (1986) Biochemistry , vol.25 , pp. 2485-2489
    • Coy, M.1    Paw, B.H.2    Bindereif, A.3    Neilands, J.B.4
  • 20
    • 0036280341 scopus 로고    scopus 로고
    • Genetics and assembly line enzymology of siderophore biosynthesis in bacteria
    • Crosa J.H., Walsh C.T. 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
  • 21
    • 38849128160 scopus 로고    scopus 로고
    • Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium
    • Crouch M.L., Castor M., Karlinsey J.E., Kalhorn T., Fang F.C. Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium. Mol. Microbiol. 2008, 67:971-983.
    • (2008) Mol. Microbiol. , vol.67 , pp. 971-983
    • Crouch, M.L.1    Castor, M.2    Karlinsey, J.E.3    Kalhorn, T.4    Fang, F.C.5
  • 22
    • 0022443738 scopus 로고
    • Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12
    • de Lorenzo V., Bindereif A., Paw B.H., Neilands J.B. Aerobactin biosynthesis and transport genes of plasmid ColV-K30 in Escherichia coli K-12. J. Bacteriol. 1986, 165:570-578.
    • (1986) J. Bacteriol. , vol.165 , pp. 570-578
    • de Lorenzo, V.1    Bindereif, A.2    Paw, B.H.3    Neilands, J.B.4
  • 23
    • 0022483081 scopus 로고
    • Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli
    • de Lorenzo V., Neilands J.B. Characterization of iucA and iucC genes of the aerobactin system of plasmid ColV-K30 in Escherichia coli. J. Bacteriol. 1986, 167:350-355.
    • (1986) J. Bacteriol. , vol.167 , pp. 350-355
    • de Lorenzo, V.1    Neilands, J.B.2
  • 24
    • 0023258960 scopus 로고
    • Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor
    • de Lorenzo V., Wee S., Herrero M., Neilands J.B. Operator sequences of the aerobactin operon of plasmid ColV-K30 binding the ferric uptake regulation (fur) repressor. J. Bacteriol. 1987, 169:2624-2630.
    • (1987) J. Bacteriol. , vol.169 , pp. 2624-2630
    • de Lorenzo, V.1    Wee, S.2    Herrero, M.3    Neilands, J.B.4
  • 25
    • 0033088883 scopus 로고    scopus 로고
    • Avian pathogenic Escherichia coli (APEC)
    • Dho-Moulin M., Fairbrother J.M. Avian pathogenic Escherichia coli (APEC). Vet. Res. 1999, 30:299-316.
    • (1999) Vet. Res. , vol.30 , pp. 299-316
    • Dho-Moulin, M.1    Fairbrother, J.M.2
  • 26
    • 0033093714 scopus 로고    scopus 로고
    • Pathogenic diversity of Escherichia coli and the emergence of 'exotic' islands in the gene stream
    • Dozois C.M., Curtiss R. Pathogenic diversity of Escherichia coli and the emergence of 'exotic' islands in the gene stream. Vet. Res. 1999, 30:157-179.
    • (1999) Vet. Res. , vol.30 , pp. 157-179
    • Dozois, C.M.1    Curtiss, R.2
  • 27
    • 0037422561 scopus 로고    scopus 로고
    • Identification of pathogen-specific and conserved genes expressed in vivo by an avian pathogenic Escherichia coli strain
    • Dozois C.M., Daigle F., Curtiss R. Identification of pathogen-specific and conserved genes expressed in vivo by an avian pathogenic Escherichia coli strain. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:247-252.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 247-252
    • Dozois, C.M.1    Daigle, F.2    Curtiss, R.3
  • 28
    • 0026647784 scopus 로고
    • Pap-and pil-related DNA sequences and other virulence determinants associated with Escherichia coli isolated from septicemic chickens and turkeys
    • Dozois C.M., Fairbrother J.M., Harel J., Bosse M. pap-and pil-related DNA sequences and other virulence determinants associated with Escherichia coli isolated from septicemic chickens and turkeys. Infect. Immun. 1992, 60:2648-2656.
    • (1992) Infect. Immun. , vol.60 , pp. 2648-2656
    • Dozois, C.M.1    Fairbrother, J.M.2    Harel, J.3    Bosse, M.4
  • 29
    • 0034646227 scopus 로고    scopus 로고
    • The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates
    • Ehmann D.E., Shaw-Reid C.A., Losey H.C., Walsh C.T. The EntF and EntE adenylation domains of Escherichia coli enterobactin synthetase: sequestration and selectivity in acyl-AMP transfers to thiolation domain cosubstrates. Proc. Natl. Acad. Sci. U.S.A. 2000, 97:2509-2514.
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 2509-2514
    • Ehmann, D.E.1    Shaw-Reid, C.A.2    Losey, H.C.3    Walsh, C.T.4
  • 30
    • 0344172832 scopus 로고    scopus 로고
    • Opening the iron box: transcriptional metalloregulation by the Fur protein
    • Escolar L., Perez-Martin J., de Lorenzo V. Opening the iron box: transcriptional metalloregulation by the Fur protein. J. Bacteriol. 1999, 181:6223-6229.
    • (1999) J. Bacteriol. , vol.181 , pp. 6223-6229
    • Escolar, L.1    Perez-Martin, J.2    de Lorenzo, V.3
  • 32
    • 0025786078 scopus 로고
    • Oxidative stress responses in Escherichia coli and Salmonella typhimurium
    • Farr S.B., Kogoma T. Oxidative stress responses in Escherichia coli and Salmonella typhimurium. Microbiol. Rev. 1991, 55:561-585.
    • (1991) Microbiol. Rev. , vol.55 , pp. 561-585
    • Farr, S.B.1    Kogoma, T.2
  • 33
    • 0021071840 scopus 로고
    • Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli
    • Fecker L., Braun V. Cloning and expression of the fhu genes involved in iron(III)-hydroxamate uptake by Escherichia coli. J. Bacteriol. 1983, 156:1301-1314.
    • (1983) J. Bacteriol. , vol.156 , pp. 1301-1314
    • Fecker, L.1    Braun, V.2
  • 34
    • 34249893071 scopus 로고    scopus 로고
    • The salmochelin siderophore receptor IroN contributes to invasion of urothelial cells by extraintestinal pathogenic Escherichia coli in vitro
    • Feldmann F., Sorsa L.J., Hildinger K., Schubert S. The salmochelin siderophore receptor IroN contributes to invasion of urothelial cells by extraintestinal pathogenic Escherichia coli in vitro. Infect. Immun. 2007, 75:3183-3187.
    • (2007) Infect. Immun. , vol.75 , pp. 3183-3187
    • Feldmann, F.1    Sorsa, L.J.2    Hildinger, K.3    Schubert, S.4
  • 35
    • 0032921490 scopus 로고    scopus 로고
    • YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis
    • Fetherston J.D., Bertolino V.J., Perry R.D. YbtP and YbtQ: two ABC transporters required for iron uptake in Yersinia pestis. Mol. Microbiol. 1999, 32:289-299.
    • (1999) Mol. Microbiol. , vol.32 , pp. 289-299
    • Fetherston, J.D.1    Bertolino, V.J.2    Perry, R.D.3
  • 36
    • 77951242175 scopus 로고    scopus 로고
    • The yersiniabactin transport system is critical for the pathogenesis of bubonic and pneumonic plague
    • Fetherston J.D., Kirillina O., Bobrov A.G., Paulley J.T., Perry R.D. The yersiniabactin transport system is critical for the pathogenesis of bubonic and pneumonic plague. Infect. Immun. 2010, 78:2045-2052.
    • (2010) Infect. Immun. , vol.78 , pp. 2045-2052
    • Fetherston, J.D.1    Kirillina, O.2    Bobrov, A.G.3    Paulley, J.T.4    Perry, R.D.5
  • 37
    • 14144253168 scopus 로고    scopus 로고
    • In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase
    • Fischbach M.A., Lin H., Liu D.R., Walsh C.T. In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:571-576.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 571-576
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 39
    • 0000027080 scopus 로고
    • Isolation from acid-fast bacteria of a growth-factor for Mycobacterium johnei and of a precursor of phthiocol
    • Francis J., Madinaveitia J., et al. Isolation from acid-fast bacteria of a growth-factor for Mycobacterium johnei and of a precursor of phthiocol. Nature 1949, 163:365.
    • (1949) Nature , vol.163 , pp. 365
    • Francis, J.1    Madinaveitia, J.2
  • 42
    • 0036015639 scopus 로고    scopus 로고
    • Export of the siderophore enterobactin in Escherichia coli: involvement of a 43kDa membrane exporter
    • Furrer J.L., Sanders D.N., Hook-Barnard I.G., McIntosh M.A. Export of the siderophore enterobactin in Escherichia coli: involvement of a 43kDa membrane exporter. Mol. Microbiol. 2002, 44:1225-1234.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1225-1234
    • Furrer, J.L.1    Sanders, D.N.2    Hook-Barnard, I.G.3    McIntosh, M.A.4
  • 43
    • 79952306781 scopus 로고    scopus 로고
    • Redundancy and specificity of Escherichia coli iron acquisition systems during urinary tract infection
    • Garcia E.C., Brumbaugh A.R., Mobley H.L. Redundancy and specificity of Escherichia coli iron acquisition systems during urinary tract infection. Infect. Immun 2011.
    • (2011) Infect. Immun
    • Garcia, E.C.1    Brumbaugh, A.R.2    Mobley, H.L.3
  • 44
    • 0030738431 scopus 로고    scopus 로고
    • Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate
    • Gehring A.M., Bradley K.A., Walsh C.T. Enterobactin biosynthesis in Escherichia coli: isochorismate lyase (EntB) is a bifunctional enzyme that is phosphopantetheinylated by EntD and then acylated by EntE using ATP and 2,3-dihydroxybenzoate. Biochemistry 1997, 36:8495-8503.
    • (1997) Biochemistry , vol.36 , pp. 8495-8503
    • Gehring, A.M.1    Bradley, K.A.2    Walsh, C.T.3
  • 45
    • 0032562142 scopus 로고    scopus 로고
    • Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF
    • Gehring A.M., Mori I., Walsh C.T. Reconstitution and characterization of the Escherichia coli enterobactin synthetase from EntB, EntE, and EntF. Biochemistry 1998, 37:2648-2659.
    • (1998) Biochemistry , vol.37 , pp. 2648-2659
    • Gehring, A.M.1    Mori, I.2    Walsh, C.T.3
  • 46
    • 0014683627 scopus 로고
    • The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I
    • Gibson F., Magrath D.I. The isolation and characterization of a hydroxamic acid (aerobactin) formed by Aerobacter aerogenes 62-I. Biochim. Biophys. Acta 1969, 192:175-184.
    • (1969) Biochim. Biophys. Acta , vol.192 , pp. 175-184
    • Gibson, F.1    Magrath, D.I.2
  • 47
    • 58149139031 scopus 로고    scopus 로고
    • Haem acquisition is facilitated by a novel receptor Hma and required by uropathogenic Escherichia coli for kidney infection
    • Hagan E.C., Mobley H.L. Haem acquisition is facilitated by a novel receptor Hma and required by uropathogenic Escherichia coli for kidney infection. Mol. Microbiol. 2009, 71:79-91.
    • (2009) Mol. Microbiol. , vol.71 , pp. 79-91
    • Hagan, E.C.1    Mobley, H.L.2
  • 48
    • 38849195550 scopus 로고    scopus 로고
    • The ferric yersiniabactin uptake receptor FyuA is required for efficient biofilm formation by urinary tract infectious Escherichia coli in human urine
    • Hancock V., Ferrieres L., Klemm P. The ferric yersiniabactin uptake receptor FyuA is required for efficient biofilm formation by urinary tract infectious Escherichia coli in human urine. Microbiology 2008, 154:167-175.
    • (2008) Microbiology , vol.154 , pp. 167-175
    • Hancock, V.1    Ferrieres, L.2    Klemm, P.3
  • 49
    • 0019447069 scopus 로고
    • Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant
    • Hantke K. Regulation of ferric iron transport in Escherichia coli K12: isolation of a constitutive mutant. Mol. Gen. Genet. 1981, 182:288-292.
    • (1981) Mol. Gen. Genet. , vol.182 , pp. 288-292
    • Hantke, K.1
  • 50
    • 0025707199 scopus 로고
    • Dihydroxybenzoylserine - a siderophore for E. coli
    • Hantke K. Dihydroxybenzoylserine - a siderophore for E. coli. FEMS Microbiol. Lett. 1990, 55:5-8.
    • (1990) FEMS Microbiol. Lett. , vol.55 , pp. 5-8
    • Hantke, K.1
  • 51
    • 0037388150 scopus 로고    scopus 로고
    • Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
    • Hantke K., Nicholson G., Rabsch W., Winkelmann G. Salmochelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc. Natl. Acad. Sci. U.S.A. 2003, 100:3677-3682.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 52
    • 0027238303 scopus 로고
    • Virulence of Yersinia enterocolitica is closely associated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000Da and pesticin sensitivity
    • Heesemann J., Hantke K., Vocke T., Saken E., Rakin A., Stojiljkovic I., Berner R. Virulence of Yersinia enterocolitica is closely associated with siderophore production, expression of an iron-repressible outer membrane polypeptide of 65,000Da and pesticin sensitivity. Mol. Microbiol. 1993, 8:397-408.
    • (1993) Mol. Microbiol. , vol.8 , pp. 397-408
    • Heesemann, J.1    Hantke, K.2    Vocke, T.3    Saken, E.4    Rakin, A.5    Stojiljkovic, I.6    Berner, R.7
  • 53
    • 0036231227 scopus 로고    scopus 로고
    • Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA
    • Higgs P.I., Larsen R.A., Postle K. Quantification of known components of the Escherichia coli TonB energy transduction system: TonB, ExbB, ExbD and FepA. Mol. Microbiol. 2002, 44:271-281.
    • (2002) Mol. Microbiol. , vol.44 , pp. 271-281
    • Higgs, P.I.1    Larsen, R.A.2    Postle, K.3
  • 54
    • 62749143005 scopus 로고    scopus 로고
    • Virulence genotypes and phylogenetic background of fluoroquinolone-resistant and susceptible Escherichia coli urine isolates from dogs with urinary tract infection
    • Johnson J.R., Kuskowski M.A., Owens K., Clabots C., Singer R.S. Virulence genotypes and phylogenetic background of fluoroquinolone-resistant and susceptible Escherichia coli urine isolates from dogs with urinary tract infection. Vet. Microbiol. 2009, 136:108-114.
    • (2009) Vet. Microbiol. , vol.136 , pp. 108-114
    • Johnson, J.R.1    Kuskowski, M.A.2    Owens, K.3    Clabots, C.4    Singer, R.S.5
  • 55
    • 39149095620 scopus 로고    scopus 로고
    • Escherichia coli colonization patterns among human household members and pets, with attention to acute urinary tract infection
    • Johnson J.R., Owens K., Gajewski A., Clabots C. Escherichia coli colonization patterns among human household members and pets, with attention to acute urinary tract infection. J. Infect. Dis. 2008, 197:218-224.
    • (2008) J. Infect. Dis. , vol.197 , pp. 218-224
    • Johnson, J.R.1    Owens, K.2    Gajewski, A.3    Clabots, C.4
  • 56
    • 0036010036 scopus 로고    scopus 로고
    • Extraintestinal pathogenic Escherichia coli: " the other bad E coli"
    • Johnson J.R., Russo T.A. Extraintestinal pathogenic Escherichia coli: " the other bad E coli" J. Lab. Clin. Med. 2002, 139:155-162.
    • (2002) J. Lab. Clin. Med. , vol.139 , pp. 155-162
    • Johnson, J.R.1    Russo, T.A.2
  • 57
    • 0034019899 scopus 로고    scopus 로고
    • Molecular epidemiological and phylogenetic associations of two novel putative virulence genes, iha and iroN (E. coli), among Escherichia coli isolates from patients with urosepsis
    • Johnson J.R., Russo T.A., Tarr P.I., Carlino U., Bilge S.S., Vary J.C., Stell A.L. Molecular epidemiological and phylogenetic associations of two novel putative virulence genes, iha and iroN (E. coli), among Escherichia coli isolates from patients with urosepsis. Infect. Immun. 2000, 68:3040-3047.
    • (2000) Infect. Immun. , vol.68 , pp. 3040-3047
    • Johnson, J.R.1    Russo, T.A.2    Tarr, P.I.3    Carlino, U.4    Bilge, S.S.5    Vary, J.C.6    Stell, A.L.7
  • 58
    • 30744441214 scopus 로고    scopus 로고
    • DNA sequence of a ColV plasmid and prevalence of selected plasmid-encoded virulence genes among avian Escherichia coli strains
    • Johnson T.J., Siek K.E., Johnson S.J., Nolan L.K. DNA sequence of a ColV plasmid and prevalence of selected plasmid-encoded virulence genes among avian Escherichia coli strains. J. Bacteriol. 2006, 188:745-758.
    • (2006) J. Bacteriol. , vol.188 , pp. 745-758
    • Johnson, T.J.1    Siek, K.E.2    Johnson, S.J.3    Nolan, L.K.4
  • 60
    • 0027487221 scopus 로고
    • Characterization of the ferrous iron uptake system of Escherichia coli
    • Kammler M., Schon C., Hantke K. Characterization of the ferrous iron uptake system of Escherichia coli. J. Bacteriol. 1993, 175:6212-6219.
    • (1993) J. Bacteriol. , vol.175 , pp. 6212-6219
    • Kammler, M.1    Schon, C.2    Hantke, K.3
  • 62
    • 0034684233 scopus 로고    scopus 로고
    • Human neutrophil gelatinase-associated lipocalin and homologous proteins in rat and mouse
    • Kjeldsen L., Cowland J.B., Borregaard N. Human neutrophil gelatinase-associated lipocalin and homologous proteins in rat and mouse. Biochim. Biophys. Acta 2000, 1482:272-283.
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 272-283
    • Kjeldsen, L.1    Cowland, J.B.2    Borregaard, N.3
  • 63
    • 0020448368 scopus 로고
    • Aerobactin-mediated utilization of transferrin iron
    • Konopka K., Bindereif A., Neilands J.B. Aerobactin-mediated utilization of transferrin iron. Biochemistry 1982, 21:6503-6508.
    • (1982) Biochemistry , vol.21 , pp. 6503-6508
    • Konopka, K.1    Bindereif, A.2    Neilands, J.B.3
  • 64
    • 0021265129 scopus 로고
    • Effect of serum albumin on siderophore-mediated utilization of transferrin iron
    • Konopka K., Neilands J.B. Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry 1984, 23:2122-2127.
    • (1984) Biochemistry , vol.23 , pp. 2122-2127
    • Konopka, K.1    Neilands, J.B.2
  • 65
    • 0025689163 scopus 로고
    • Iron (III) hydroxamate transport into Escherichia coli. Substrate binding to the periplasmic FhuD protein
    • Koster W., Braun V. Iron (III) hydroxamate transport into Escherichia coli. Substrate binding to the periplasmic FhuD protein. J. Biol. Chem. 1990, 265:21407-21410.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21407-21410
    • Koster, W.1    Braun, V.2
  • 66
    • 0023067036 scopus 로고
    • Presence and expression of aerobactin genes in virulent avian strains of Escherichia coli
    • Lafont J.P., Dho M., D'Hauteville H.M., Bree A., Sansonetti P.J. Presence and expression of aerobactin genes in virulent avian strains of Escherichia coli. Infect. Immun. 1987, 55:193-197.
    • (1987) Infect. Immun. , vol.55 , pp. 193-197
    • Lafont, J.P.1    Dho, M.2    D'Hauteville, H.M.3    Bree, A.4    Sansonetti, P.J.5
  • 67
    • 0015467311 scopus 로고
    • Enterochelin system of iron transport in Escherichia coli: mutations affecting ferric-enterochelin esterase
    • Langman L., Young I.G., Frost G.E., Rosenberg H., Gibson F. Enterochelin system of iron transport in Escherichia coli: mutations affecting ferric-enterochelin esterase. J. Bacteriol. 1972, 112:1142-1149.
    • (1972) J. Bacteriol. , vol.112 , pp. 1142-1149
    • Langman, L.1    Young, I.G.2    Frost, G.E.3    Rosenberg, H.4    Gibson, F.5
  • 68
    • 0037381732 scopus 로고    scopus 로고
    • Architecture of a fur binding site: a comparative analysis
    • Lavrrar J.L., McIntosh M.A. Architecture of a fur binding site: a comparative analysis. J. Bacteriol. 2003, 185:2194-2202.
    • (2003) J. Bacteriol. , vol.185 , pp. 2194-2202
    • Lavrrar, J.L.1    McIntosh, M.A.2
  • 69
    • 23744479843 scopus 로고    scopus 로고
    • In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes
    • Lin H., Fischbach M.A., Liu D.R., Walsh C.T. In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes. J. Am. Chem. Soc. 2005, 127:11075-11084.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 11075-11084
    • Lin, H.1    Fischbach, M.A.2    Liu, D.R.3    Walsh, C.T.4
  • 70
    • 0023184276 scopus 로고
    • Incidence of the aerobactin iron uptake system among Escherichia coli isolates from infections of farm animals
    • Linggood M.A., Roberts M., Ford S., Parry S.H., Williams P.H. Incidence of the aerobactin iron uptake system among Escherichia coli isolates from infections of farm animals. J. Gen. Microbiol. 1987, 133:835-842.
    • (1987) J. Gen. Microbiol. , vol.133 , pp. 835-842
    • Linggood, M.A.1    Roberts, M.2    Ford, S.3    Parry, S.H.4    Williams, P.H.5
  • 71
    • 0024616004 scopus 로고
    • Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase
    • Liu J., Duncan K., Walsh C.T. Nucleotide sequence of a cluster of Escherichia coli enterobactin biosynthesis genes: identification of entA and purification of its product 2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase. J. Bacteriol. 1989, 171:791-798.
    • (1989) J. Bacteriol. , vol.171 , pp. 791-798
    • Liu, J.1    Duncan, K.2    Walsh, C.T.3
  • 72
    • 0025096785 scopus 로고
    • Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate
    • Liu J., Quinn N., Berchtold G.A., Walsh C.T. Overexpression, purification, and characterization of isochorismate synthase (EntC), the first enzyme involved in the biosynthesis of enterobactin from chorismate. Biochemistry 1990, 29:1417-1425.
    • (1990) Biochemistry , vol.29 , pp. 1417-1425
    • Liu, J.1    Quinn, N.2    Berchtold, G.A.3    Walsh, C.T.4
  • 73
    • 75449095223 scopus 로고    scopus 로고
    • Avian colibacillosis and salmonellosis: a closer look at epidemiology, pathogenesis, diagnosis, control and public health concerns
    • Lutful Kabir S.M. Avian colibacillosis and salmonellosis: a closer look at epidemiology, pathogenesis, diagnosis, control and public health concerns. Int. J. Environ. Res. Public Health 2010, 7:89-114.
    • (2010) Int. J. Environ. Res. Public Health , vol.7 , pp. 89-114
    • Lutful Kabir, S.M.1
  • 74
    • 33947373640 scopus 로고    scopus 로고
    • Initial steps of colicin E1 import across the outer membrane of Escherichia coli
    • Masi M., Vuong P., Humbard M., Malone K., Misra R. Initial steps of colicin E1 import across the outer membrane of Escherichia coli. J. Bacteriol. 2007, 189:2667-2676.
    • (2007) J. Bacteriol. , vol.189 , pp. 2667-2676
    • Masi, M.1    Vuong, P.2    Humbard, M.3    Malone, K.4    Misra, R.5
  • 75
    • 0141860088 scopus 로고    scopus 로고
    • Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli
    • Masse E., Escorcia F.E., Gottesman S. Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli. Genes Dev. 2003, 17:2374-2383.
    • (2003) Genes Dev. , vol.17 , pp. 2374-2383
    • Masse, E.1    Escorcia, F.E.2    Gottesman, S.3
  • 76
    • 0037007078 scopus 로고    scopus 로고
    • A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli
    • Masse E., Gottesman S. A small RNA regulates the expression of genes involved in iron metabolism in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:4620-4625.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 4620-4625
    • Masse, E.1    Gottesman, S.2
  • 78
    • 34548739613 scopus 로고    scopus 로고
    • Siderophore-based iron acquisition and pathogen control
    • Miethke M., Marahiel M.A. 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
  • 79
    • 77954584742 scopus 로고    scopus 로고
    • Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis
    • Miller M.C., Fetherston J.D., Pickett C.L., Bobrov A.G., Weaver R.H., DeMoll E., Perry R.D. Reduced synthesis of the Ybt siderophore or production of aberrant Ybt-like molecules activates transcription of yersiniabactin genes in Yersinia pestis. Microbiology 2010, 156:2226-2238.
    • (2010) Microbiology , vol.156 , pp. 2226-2238
    • Miller, M.C.1    Fetherston, J.D.2    Pickett, C.L.3    Bobrov, A.G.4    Weaver, R.H.5    DeMoll, E.6    Perry, R.D.7
  • 80
    • 64649089196 scopus 로고    scopus 로고
    • Assembly and transport mechanism of tripartite drug efflux systems
    • Misra R., Bavro V.N. Assembly and transport mechanism of tripartite drug efflux systems. Biochim. Biophys. Acta 2009, 1794:817-825.
    • (2009) Biochim. Biophys. Acta , vol.1794 , pp. 817-825
    • Misra, R.1    Bavro, V.N.2
  • 81
    • 0031803840 scopus 로고    scopus 로고
    • TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport
    • Moeck G.S., Coulton J.W. TonB-dependent iron acquisition: mechanisms of siderophore-mediated active transport. Mol. Microbiol. 1998, 28:675-681.
    • (1998) Mol. Microbiol. , vol.28 , pp. 675-681
    • Moeck, G.S.1    Coulton, J.W.2
  • 82
    • 0842347870 scopus 로고    scopus 로고
    • The siderophore receptor IroN, but not the high-pathogenicity island or the hemin receptor ChuA, contributes to the bacteremic step of Escherichia coli neonatal meningitis
    • Negre V.L., Bonacorsi S., Schubert S., Bidet P., Nassif X., Bingen E. The siderophore receptor IroN, but not the high-pathogenicity island or the hemin receptor ChuA, contributes to the bacteremic step of Escherichia coli neonatal meningitis. Infect. Immun. 2004, 72:1216-1220.
    • (2004) Infect. Immun. , vol.72 , pp. 1216-1220
    • Negre, V.L.1    Bonacorsi, S.2    Schubert, S.3    Bidet, P.4    Nassif, X.5    Bingen, E.6
  • 83
    • 0015236316 scopus 로고
    • Enterochelin hydrolysis and iron metabolism in Escherichia coli
    • O'Brien I.G., Cox G.B., Gibson F. Enterochelin hydrolysis and iron metabolism in Escherichia coli. Biochim. Biophys. Acta 1971, 237:537-549.
    • (1971) Biochim. Biophys. Acta , vol.237 , pp. 537-549
    • O'Brien, I.G.1    Cox, G.B.2    Gibson, F.3
  • 84
    • 0014945206 scopus 로고
    • The structure of enterochelin and related 2,3-dihydroxy-N-benzoylserine conjugates from Escherichia coli
    • O'Brien I.G., Gibson F. The structure of enterochelin and related 2,3-dihydroxy-N-benzoylserine conjugates from Escherichia coli. Biochim. Biophys. Acta 1970, 215:393-402.
    • (1970) Biochim. Biophys. Acta , vol.215 , pp. 393-402
    • O'Brien, I.G.1    Gibson, F.2
  • 86
    • 33845510309 scopus 로고    scopus 로고
    • Identification and characterization of a novel ABC iron transport system, fit, in Escherichia coli
    • Ouyang Z., Isaacson R. Identification and characterization of a novel ABC iron transport system, fit, in Escherichia coli. Infect. Immun. 2006, 74:6949-6956.
    • (2006) Infect. Immun. , vol.74 , pp. 6949-6956
    • Ouyang, Z.1    Isaacson, R.2
  • 87
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis
    • Oves-Costales D., Kadi N., Challis G.L. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb) 2009, 6530-6541.
    • (2009) Chem. Commun. (Camb) , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 88
    • 0024617003 scopus 로고
    • Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC and evolutionary relationship of isochorismate synthetase and other chorismate-utilizing enzymes
    • Ozenberger B.A., Brickman T.J., McIntosh M.A. Nucleotide sequence of Escherichia coli isochorismate synthetase gene entC and evolutionary relationship of isochorismate synthetase and other chorismate-utilizing enzymes. J. Bacteriol. 1989, 171:775-783.
    • (1989) J. Bacteriol. , vol.171 , pp. 775-783
    • Ozenberger, B.A.1    Brickman, T.J.2    McIntosh, M.A.3
  • 90
    • 66549100507 scopus 로고    scopus 로고
    • The plasmid of Escherichia coli strain S88 (O45:K1:H7) that causes neonatal meningitis is closely related to avian pathogenic E. coli plasmids and is associated with high-level bacteremia in a neonatal rat meningitis model
    • Peigne C., Bidet P., Mahjoub-Messai F., Plainvert C., Barbe V., Medigue C., Frapy E., Nassif X., Denamur E., Bingen E., Bonacorsi S. The plasmid of Escherichia coli strain S88 (O45:K1:H7) that causes neonatal meningitis is closely related to avian pathogenic E. coli plasmids and is associated with high-level bacteremia in a neonatal rat meningitis model. Infect. Immun. 2009, 77:2272-2284.
    • (2009) Infect. Immun. , vol.77 , pp. 2272-2284
    • Peigne, C.1    Bidet, P.2    Mahjoub-Messai, F.3    Plainvert, C.4    Barbe, V.5    Medigue, C.6    Frapy, E.7    Nassif, X.8    Denamur, E.9    Bingen, E.10    Bonacorsi, S.11
  • 91
    • 33747154459 scopus 로고    scopus 로고
    • Multidrug-resistance efflux pumps - not just for resistance
    • Piddock L.J. Multidrug-resistance efflux pumps - not just for resistance. Nat. Rev. Microbiol. 2006, 4:629-636.
    • (2006) Nat. Rev. Microbiol. , vol.4 , pp. 629-636
    • Piddock, L.J.1
  • 92
    • 0014942235 scopus 로고
    • Enterobactin, an iron transport compound from Salmonella typhimurium
    • Pollack J.R., Neilands J.B. Enterobactin, an iron transport compound from Salmonella typhimurium. Biochem. Biophys. Res. Commun. 1970, 38:989-992.
    • (1970) Biochem. Biophys. Res. Commun. , vol.38 , pp. 989-992
    • Pollack, J.R.1    Neilands, J.B.2
  • 93
    • 0028291473 scopus 로고
    • The pesticin receptor of Yersinia enterocolitica: a novel virulence factor with dual function
    • Rakin A., Saken E., Harmsen D., Heesemann J. The pesticin receptor of Yersinia enterocolitica: a novel virulence factor with dual function. Mol. Microbiol. 1994, 13:253-263.
    • (1994) Mol. Microbiol. , vol.13 , pp. 253-263
    • Rakin, A.1    Saken, E.2    Harmsen, D.3    Heesemann, J.4
  • 94
    • 0033759220 scopus 로고    scopus 로고
    • Iron metabolism in pathogenic bacteria
    • Ratledge C., Dover L.G. 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
  • 96
    • 34547121698 scopus 로고    scopus 로고
    • Functional genomic studies of uropathogenic Escherichia coli and host urothelial cells when intracellular bacterial communities are assembled
    • Reigstad C.S., Hultgren S.J., Gordon J.I. Functional genomic studies of uropathogenic Escherichia coli and host urothelial cells when intracellular bacterial communities are assembled. J. Biol. Chem. 2007, 282:21259-21267.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21259-21267
    • Reigstad, C.S.1    Hultgren, S.J.2    Gordon, J.I.3
  • 97
    • 0037431961 scopus 로고    scopus 로고
    • Dissection of the EntF condensation domain boundary and active site residues in nonribosomal peptide synthesis
    • Roche E.D., Walsh C.T. Dissection of the EntF condensation domain boundary and active site residues in nonribosomal peptide synthesis. Biochemistry 2003, 42:1334-1344.
    • (2003) Biochemistry , vol.42 , pp. 1334-1344
    • Roche, E.D.1    Walsh, C.T.2
  • 98
    • 77955552106 scopus 로고    scopus 로고
    • Distribution and evolution of virulence factors in septicemic Escherichia coli
    • Ron E.Z. Distribution and evolution of virulence factors in septicemic Escherichia coli. Int. J. Med. Microbiol. 2010, 300:367-370.
    • (2010) Int. J. Med. Microbiol. , vol.300 , pp. 367-370
    • Ron, E.Z.1
  • 99
    • 0024420904 scopus 로고
    • Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product
    • Rusnak F., Faraci W.S., Walsh C.T. Subcloning, expression, and purification of the enterobactin biosynthetic enzyme 2,3-dihydroxybenzoate-AMP ligase: demonstration of enzyme-bound (2,3-dihydroxybenzoyl)adenylate product. Biochemistry 1989, 28:6827-6835.
    • (1989) Biochemistry , vol.28 , pp. 6827-6835
    • Rusnak, F.1    Faraci, W.S.2    Walsh, C.T.3
  • 100
    • 0025162272 scopus 로고
    • Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase
    • Rusnak F., Liu J., Quinn N., Berchtold G.A., Walsh C.T. Subcloning of the enterobactin biosynthetic gene entB: expression, purification, characterization, and substrate specificity of isochorismatase. Biochemistry 1990, 29:1425-1435.
    • (1990) Biochemistry , vol.29 , pp. 1425-1435
    • Rusnak, F.1    Liu, J.2    Quinn, N.3    Berchtold, G.A.4    Walsh, C.T.5
  • 101
    • 0036893698 scopus 로고    scopus 로고
    • IroN functions as a siderophore receptor and is a urovirulence factor in an extraintestinal pathogenic isolate of Escherichia coli
    • Russo T.A., McFadden C.D., Carlino-MacDonald U.B., Beanan J.M., Barnard T.J., Johnson J.R. IroN functions as a siderophore receptor and is a urovirulence factor in an extraintestinal pathogenic isolate of Escherichia coli. Infect. Immun. 2002, 70:7156-7160.
    • (2002) Infect. Immun. , vol.70 , pp. 7156-7160
    • Russo, T.A.1    McFadden, C.D.2    Carlino-MacDonald, U.B.3    Beanan, J.M.4    Barnard, T.J.5    Johnson, J.R.6
  • 102
    • 0345283049 scopus 로고    scopus 로고
    • The Siderophore receptor IroN of extraintestinal pathogenic Escherichia coli is a potential vaccine candidate
    • Russo T.A., McFadden C.D., Carlino-MacDonald U.B., Beanan J.M., Olson R., Wilding G.E. The Siderophore receptor IroN of extraintestinal pathogenic Escherichia coli is a potential vaccine candidate. Infect. Immun. 2003, 71:7164-7169.
    • (2003) Infect. Immun. , vol.71 , pp. 7164-7169
    • Russo, T.A.1    McFadden, C.D.2    Carlino-MacDonald, U.B.3    Beanan, J.M.4    Olson, R.5    Wilding, G.E.6
  • 103
    • 39149115716 scopus 로고    scopus 로고
    • Contribution of the SitABCD, MntH, and FeoB metal transporters to the virulence of avian pathogenic Escherichia coli O78 strain chi7122
    • Sabri M., Caza M., Proulx J., Lymberopoulos M.H., Bree A., Moulin-Schouleur M., Curtiss R., Dozois C.M. Contribution of the SitABCD, MntH, and FeoB metal transporters to the virulence of avian pathogenic Escherichia coli O78 strain chi7122. Infect. Immun. 2008, 76:601-611.
    • (2008) Infect. Immun. , vol.76 , pp. 601-611
    • Sabri, M.1    Caza, M.2    Proulx, J.3    Lymberopoulos, M.H.4    Bree, A.5    Moulin-Schouleur, M.6    Curtiss, R.7    Dozois, C.M.8
  • 104
    • 0025322829 scopus 로고
    • Mechanistic studies on trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (Ent A) in the biosynthesis of the iron chelator enterobactin
    • Sakaitani M., Rusnak F., Quinn N.R., Tu C., Frigo T.B., Berchtold G.A., Walsh C.T. Mechanistic studies on trans-2,3-dihydro-2,3-dihydroxybenzoate dehydrogenase (Ent A) in the biosynthesis of the iron chelator enterobactin. Biochemistry 1990, 29:6789-6798.
    • (1990) Biochemistry , vol.29 , pp. 6789-6798
    • Sakaitani, M.1    Rusnak, F.2    Quinn, N.R.3    Tu, C.4    Frigo, T.B.5    Berchtold, G.A.6    Walsh, C.T.7
  • 106
    • 0025915699 scopus 로고
    • Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli
    • Shea C.M., McIntosh M.A. Nucleotide sequence and genetic organization of the ferric enterobactin transport system: homology to other periplasmic binding protein-dependent systems in Escherichia coli. Mol. Microbiol. 1991, 5:1415-1428.
    • (1991) Mol. Microbiol. , vol.5 , pp. 1415-1428
    • Shea, C.M.1    McIntosh, M.A.2
  • 108
    • 77958143617 scopus 로고    scopus 로고
    • The battle for iron between bacterial pathogens and their vertebrate hosts
    • Skaar E.P. The battle for iron between bacterial pathogens and their vertebrate hosts. PLoS Pathog. 2010, 6.
    • (2010) PLoS Pathog. , pp. 6
    • Skaar, E.P.1
  • 110
    • 0027447472 scopus 로고
    • Construction and biochemical characterization of recombinant cytoplasmic forms of the IucD protein (lysine:N6-hydroxylase) encoded by the pColV-K30 aerobactin gene cluster
    • Thariath A., Socha D., Valvano M.A., Viswanatha T. Construction and biochemical characterization of recombinant cytoplasmic forms of the IucD protein (lysine:N6-hydroxylase) encoded by the pColV-K30 aerobactin gene cluster. J. Bacteriol. 1993, 175:589-596.
    • (1993) J. Bacteriol. , vol.175 , pp. 589-596
    • Thariath, A.1    Socha, D.2    Valvano, M.A.3    Viswanatha, T.4
  • 111
    • 0034818457 scopus 로고    scopus 로고
    • TonB-dependent systems of uropathogenic Escherichia coli: aerobactin and heme transport and TonB are required for virulence in the mouse
    • Torres A.G., Redford P., Welch R.A., Payne S.M. TonB-dependent systems of uropathogenic Escherichia coli: aerobactin and heme transport and TonB are required for virulence in the mouse. Infect. Immun. 2001, 69:6179-6185.
    • (2001) Infect. Immun. , vol.69 , pp. 6179-6185
    • Torres, A.G.1    Redford, P.2    Welch, R.A.3    Payne, S.M.4
  • 112
    • 33750622338 scopus 로고    scopus 로고
    • Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain Nissle 1917
    • Valdebenito M., Crumbliss A.L., Winkelmann G., Hantke K. Environmental factors influence the production of enterobactin, salmochelin, aerobactin, and yersiniabactin in Escherichia coli strain Nissle 1917. Int. J. Med. Microbiol. 2006, 296:513-520.
    • (2006) Int. J. Med. Microbiol. , vol.296 , pp. 513-520
    • Valdebenito, M.1    Crumbliss, A.L.2    Winkelmann, G.3    Hantke, K.4
  • 113
    • 67650177056 scopus 로고    scopus 로고
    • Identification of uropathogenic Escherichia coli surface proteins by shotgun proteomics
    • Walters M.S., Mobley H.L. Identification of uropathogenic Escherichia coli surface proteins by shotgun proteomics. J. Microbiol. Methods 2009, 78:131-135.
    • (2009) J. Microbiol. Methods , vol.78 , pp. 131-135
    • Walters, M.S.1    Mobley, H.L.2
  • 114
    • 0025372570 scopus 로고
    • TolC, an Escherichia coli outer membrane protein required for hemolysin secretion
    • Wandersman C., Delepelaire P. TolC, an Escherichia coli outer membrane protein required for hemolysin secretion. Proc. Natl. Acad. Sci. U.S.A. 1990, 87:4776-4780.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4776-4780
    • Wandersman, C.1    Delepelaire, P.2
  • 115
    • 0022576611 scopus 로고
    • IroN, siderophores, and the pursuit of virulence: independence of the aerobactin and enterochelin iron uptake systems in Escherichia coli
    • Williams P.H., Carbonetti N.H. IroN, siderophores, and the pursuit of virulence: independence of the aerobactin and enterochelin iron uptake systems in Escherichia coli. Infect. Immun. 1986, 51:942-947.
    • (1986) Infect. Immun. , vol.51 , pp. 942-947
    • Williams, P.H.1    Carbonetti, N.H.2
  • 116
    • 0026579656 scopus 로고
    • Transport of ferric-aerobactin into the periplasm and cytoplasm of Escherichia coli K12: role of envelope-associated proteins and effect of endogenous siderophores
    • Wooldridge K.G., Morrissey J.A., Williams P.H. Transport of ferric-aerobactin into the periplasm and cytoplasm of Escherichia coli K12: role of envelope-associated proteins and effect of endogenous siderophores. J. Gen. Microbiol. 1992, 138:597-603.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 597-603
    • Wooldridge, K.G.1    Morrissey, J.A.2    Williams, P.H.3
  • 117
    • 57349141498 scopus 로고    scopus 로고
    • MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II
    • Yamanaka H., Kobayashi H., Takahashi E., Okamoto K. MacAB is involved in the secretion of Escherichia coli heat-stable enterotoxin II. J. Bacteriol. 2008, 190:7693-7698.
    • (2008) J. Bacteriol. , vol.190 , pp. 7693-7698
    • Yamanaka, H.1    Kobayashi, H.2    Takahashi, E.3    Okamoto, K.4
  • 118
    • 0018417401 scopus 로고
    • Enterochelin (enterobactin): virulence factor for Salmonella typhimurium
    • Yancey R.J., Breeding S.A., Lankford C.E. Enterochelin (enterobactin): virulence factor for Salmonella typhimurium. Infect. Immun. 1979, 24:174-180.
    • (1979) Infect. Immun. , vol.24 , pp. 174-180
    • Yancey, R.J.1    Breeding, S.A.2    Lankford, C.E.3
  • 120
    • 22144439383 scopus 로고    scopus 로고
    • Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization
    • Zhu M., Valdebenito M., Winkelmann G., Hantke K. Functions of the siderophore esterases IroD and IroE in iron-salmochelin utilization. Microbiology 2005, 151:2363-2372.
    • (2005) Microbiology , vol.151 , pp. 2363-2372
    • Zhu, M.1    Valdebenito, M.2    Winkelmann, G.3    Hantke, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.