메뉴 건너뛰기




Volumn 7, Issue 11, 2012, Pages

Role of Catecholate Siderophores in Gram-Negative Bacterial Colonization of the Mouse Gut

Author keywords

[No Author keywords available]

Indexed keywords

ENTEROCHELIN; IRON COMPLEX; PROTEIN TONB; SIDEROPHORE;

EID: 84870502694     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0050020     Document Type: Article
Times cited : (42)

References (61)
  • 3
    • 0023759161 scopus 로고
    • The spectroelectrochemical determination of the reduction potential of diferric serum transferrin
    • Kretchmar SA, Reyes ZE, Raymond KN, (1988) The spectroelectrochemical determination of the reduction potential of diferric serum transferrin. Biochim Biophys Acta 956: 85-94.
    • (1988) Biochim Biophys Acta , vol.956 , pp. 85-94
    • Kretchmar, S.A.1    Reyes, Z.E.2    Raymond, K.N.3
  • 5
    • 0030841393 scopus 로고    scopus 로고
    • Iron, infections, and anemia of inflammation
    • Jurado RL, (1997) Iron, infections, and anemia of inflammation. Clin Infect Dis 25: 888-895.
    • (1997) Clin Infect Dis , vol.25 , pp. 888-895
    • Jurado, R.L.1
  • 6
    • 0017618295 scopus 로고
    • Virulence-associated acquisition of iron in mammalian serum by Escherichia coli
    • Kochan I, Kvach JT, Wiles TI, (1977) Virulence-associated acquisition of iron in mammalian serum by Escherichia coli. J Infect Dis 135: 623-632.
    • (1977) J Infect Dis , vol.135 , pp. 623-632
    • Kochan, I.1    Kvach, J.T.2    Wiles, T.I.3
  • 7
    • 0021688952 scopus 로고
    • Anaerobic iron uptake by Escherichia coli
    • Lodge JS, Emery T, (1984) Anaerobic iron uptake by Escherichia coli. J Bacteriol 160: 801-804.
    • (1984) J Bacteriol , vol.160 , pp. 801-804
    • Lodge, J.S.1    Emery, T.2
  • 8
    • 0027487221 scopus 로고
    • Characterization of the ferrous iron uptake system of Escherichia coli
    • Kammler M, Schon C, Hantke K, (1993) Characterization of the ferrous iron uptake system of Escherichia coli. J Bacteriol 175: 6212-6219.
    • (1993) J Bacteriol , vol.175 , pp. 6212-6219
    • Kammler, M.1    Schon, C.2    Hantke, K.3
  • 9
    • 0028850367 scopus 로고
    • Siderophores: structure and function of microbial iron transport compounds
    • Neilands JB, (1995) Siderophores: structure and function of microbial iron transport compounds. J Biol Chem 270: 26723-26726.
    • (1995) J Biol Chem , vol.270 , pp. 26723-26726
    • Neilands, J.B.1
  • 10
    • 0028073695 scopus 로고
    • Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens
    • Cornelissen CN, Sparling PF, (1994) Iron piracy: acquisition of transferrin-bound iron by bacterial pathogens. Mol Microbiol 14: 843-850.
    • (1994) Mol Microbiol , vol.14 , pp. 843-850
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 11
    • 0028222440 scopus 로고
    • Identification of receptor-mediated transferrin-iron uptake mechanism in Neisseria gonorrhoeae
    • Cornelissen CN, Sparling PF, (1994) Identification of receptor-mediated transferrin-iron uptake mechanism in Neisseria gonorrhoeae. Methods Enzymol 235: 356-363.
    • (1994) Methods Enzymol , vol.235 , pp. 356-363
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 12
    • 79958795022 scopus 로고    scopus 로고
    • Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes
    • Xiao Q, Jiang X, Moore KJ, Shao Y, Pi H, et al. (2011) Sortase independent and dependent systems for acquisition of haem and haemoglobin in Listeria monocytogenes. Mol Microbiol 80: 1581-97.
    • (2011) Mol Microbiol , vol.80 , pp. 1581-1597
    • Xiao, Q.1    Jiang, X.2    Moore, K.J.3    Shao, Y.4    Pi, H.5
  • 13
    • 34248642257 scopus 로고    scopus 로고
    • Intracellular metalloporphyrin metabolism in Staphylococcus aureus
    • Reniere ML, Torres VJ, Skaar EP, (2007) Intracellular metalloporphyrin metabolism in Staphylococcus aureus. Biometals 20: 333-345.
    • (2007) Biometals , vol.20 , pp. 333-345
    • Reniere, M.L.1    Torres, V.J.2    Skaar, E.P.3
  • 14
    • 34249826339 scopus 로고    scopus 로고
    • Heme and virulence: how bacterial pathogens regulate, transport and utilize heme
    • Wilks A, Burkhard KA, (2007) Heme and virulence: how bacterial pathogens regulate, transport and utilize heme. Nat Prod Rep 24: 511-522.
    • (2007) Nat Prod Rep , vol.24 , pp. 511-522
    • Wilks, A.1    Burkhard, K.A.2
  • 15
    • 9244234392 scopus 로고    scopus 로고
    • Bacterial iron sources: from siderophores to hemophores
    • Wandersman C, Delepelaire P, (2004) Bacterial iron sources: from siderophores to hemophores. Annu Rev Microbiol 58: 611-647.
    • (2004) Annu Rev Microbiol , vol.58 , pp. 611-647
    • Wandersman, C.1    Delepelaire, P.2
  • 16
    • 67349234858 scopus 로고    scopus 로고
    • Iron availability and infection
    • Weinberg ED, (2009) Iron availability and infection. Biochim Biophys Acta 1790: 600-605.
    • (2009) Biochim Biophys Acta , vol.1790 , pp. 600-605
    • Weinberg, E.D.1
  • 17
    • 33646160817 scopus 로고    scopus 로고
    • Catecholate receptor proteins in Salmonella enterica: role in virulence and implications for vaccine development
    • Williams PH, Rabsch W, Methner U, Voigt W, Tschape H, et al. (2006) Catecholate receptor proteins in Salmonella enterica: role in virulence and implications for vaccine development. Vaccine 24: 3840-3844.
    • (2006) Vaccine , vol.24 , pp. 3840-3844
    • Williams, P.H.1    Rabsch, W.2    Methner, U.3    Voigt, W.4    Tschape, H.5
  • 18
    • 0015217637 scopus 로고
    • An additional step in the transport of iron defined by the tonB locus of Escherichia coli
    • Wang CC, Newton A, (1971) An additional step in the transport of iron defined by the tonB locus of Escherichia coli. J Biol Chem 246: 2147-2151.
    • (1971) J Biol Chem , vol.246 , pp. 2147-2151
    • Wang, C.C.1    Newton, A.2
  • 19
    • 0034612342 scopus 로고    scopus 로고
    • One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
    • Datsenko KA, Wanner BL, (2000) One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products. Proc Natl Acad Sci U S A 97: 6640-6645.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 6640-6645
    • Datsenko, K.A.1    Wanner, B.L.2
  • 20
    • 33846948630 scopus 로고    scopus 로고
    • Evidence of ball-and-chain transport of ferric enterobactin through FepA
    • Ma L, Kaserer W, Annamalai R, Scott DC, Jin B, et al. (2007) Evidence of ball-and-chain transport of ferric enterobactin through FepA. J Biol Chem 282: 397-406 Epub 2006 Oct 2020.
    • (2007) J Biol Chem , vol.282 , pp. 397-406
    • Ma, L.1    Kaserer, W.2    Annamalai, R.3    Scott, D.C.4    Jin, B.5
  • 21
    • 67650080596 scopus 로고    scopus 로고
    • Precolonized human commensal Escherichia coli strains serve as a barrier to E. coli O157:H7 growth in the streptomycin-treated mouse intestine
    • Leatham MP, Banerjee S, Autieri SM, Mercado-Lubo R, Conway T, et al. (2009) Precolonized human commensal Escherichia coli strains serve as a barrier to E. coli O157:H7 growth in the streptomycin-treated mouse intestine. Infect Immun 77: 2876-2886.
    • (2009) Infect Immun , vol.77 , pp. 2876-2886
    • Leatham, M.P.1    Banerjee, S.2    Autieri, S.M.3    Mercado-Lubo, R.4    Conway, T.5
  • 24
    • 0023877734 scopus 로고
    • Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: role of growth in mucus
    • Wadolkowski EA, Laux DC, Cohen PS, (1988) Colonization of the streptomycin-treated mouse large intestine by a human fecal Escherichia coli strain: role of growth in mucus. Infect Immun 56: 1030-1035.
    • (1988) Infect Immun , vol.56 , pp. 1030-1035
    • Wadolkowski, E.A.1    Laux, D.C.2    Cohen, P.S.3
  • 25
    • 0021957663 scopus 로고
    • Effect of streptomycin administration on colonization resistance to Salmonella typhimurium in mice
    • Que JU, Hentges DJ, (1985) Effect of streptomycin administration on colonization resistance to Salmonella typhimurium in mice. Infect Immun 48: 169-174.
    • (1985) Infect Immun , vol.48 , pp. 169-174
    • Que, J.U.1    Hentges, D.J.2
  • 26
    • 0020046909 scopus 로고
    • Kinetics of biosynthesis of iron-regulated membrane proteins in Escherichia coli
    • Klebba PE, McIntosh MA, Neilands JB, (1982) Kinetics of biosynthesis of iron-regulated membrane proteins in Escherichia coli. J Bacteriol 149: 880-888.
    • (1982) J Bacteriol , vol.149 , pp. 880-888
    • Klebba, P.E.1    McIntosh, M.A.2    Neilands, J.B.3
  • 27
    • 0016441805 scopus 로고
    • Evidence for common binding sites for ferrichrome compounds and bacteriophage phi 80 in the cell envelope of Escherichia coli
    • Wayne R, Neilands JB, (1975) Evidence for common binding sites for ferrichrome compounds and bacteriophage phi 80 in the cell envelope of Escherichia coli. J Bacteriol 121: 497-503.
    • (1975) J Bacteriol , vol.121 , pp. 497-503
    • Wayne, R.1    Neilands, J.B.2
  • 28
    • 0021265129 scopus 로고
    • Effect of serum albumin on siderophore-mediated utilization of transferrin iron
    • Konopka K, Neilands JB, (1984) Effect of serum albumin on siderophore-mediated utilization of transferrin iron. Biochemistry 23: 2122-2127.
    • (1984) Biochemistry , vol.23 , pp. 2122-2127
    • Konopka, K.1    Neilands, J.B.2
  • 29
    • 11144314814 scopus 로고    scopus 로고
    • Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron
    • Flo TH, Smith KD, Sato S, Rodriguez DJ, Holmes MA, et al. (2004) Lipocalin 2 mediates an innate immune response to bacterial infection by sequestrating iron. Nature 432: 917-921.
    • (2004) Nature , vol.432 , pp. 917-921
    • Flo, T.H.1    Smith, K.D.2    Sato, S.3    Rodriguez, D.J.4    Holmes, M.A.5
  • 30
    • 0036865552 scopus 로고    scopus 로고
    • The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition
    • Goetz DH, Holmes MA, Borregaard N, Bluhm ME, Raymond KN, et al. (2002) The neutrophil lipocalin NGAL is a bacteriostatic agent that interferes with siderophore-mediated iron acquisition. Mol Cell 10: 1033-1043.
    • (2002) Mol Cell , vol.10 , pp. 1033-1043
    • Goetz, D.H.1    Holmes, M.A.2    Borregaard, N.3    Bluhm, M.E.4    Raymond, K.N.5
  • 32
    • 0017082075 scopus 로고
    • Preparation of enterochelin from Escherichia coli
    • Young IG, (1976) Preparation of enterochelin from Escherichia coli,. Prep Biochem 6: 123-31.
    • (1976) Prep Biochem , vol.6 , pp. 123-131
    • Young, I.G.1
  • 34
    • 0020448368 scopus 로고
    • Aerobactin-mediated utilization of transferrin iron
    • Konopka K, Bindereif A, Neilands JB, (1982) Aerobactin-mediated utilization of transferrin iron. Biochemistry 21: 6503-6508.
    • (1982) Biochemistry , vol.21 , pp. 6503-6508
    • Konopka, K.1    Bindereif, A.2    Neilands, J.B.3
  • 35
    • 79953323853 scopus 로고    scopus 로고
    • Structural variations within the transferrin binding site on transferrin-binding protein B, TbpB
    • Calmettes C, Yu RH, Silva LP, Curran D, Schriemer DC, et al. (2011) Structural variations within the transferrin binding site on transferrin-binding protein B, TbpB. J Biol Chem 286: 12683-12692.
    • (2011) J Biol Chem , vol.286 , pp. 12683-12692
    • Calmettes, C.1    Yu, R.H.2    Silva, L.P.3    Curran, D.4    Schriemer, D.C.5
  • 36
    • 0026768392 scopus 로고
    • Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors
    • Cornelissen CN, Biswas GD, Tsai J, Paruchuri DK, Thompson SA, et al. (1992) Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors. J Bacteriol 174: 5788-5797.
    • (1992) J Bacteriol , vol.174 , pp. 5788-5797
    • Cornelissen, C.N.1    Biswas, G.D.2    Tsai, J.3    Paruchuri, D.K.4    Thompson, S.A.5
  • 37
    • 0031974549 scopus 로고    scopus 로고
    • The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers
    • Cornelissen CN, Kelley M, Hobbs MM, Anderson JE, Cannon JG, et al. (1998) The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers. Mol Microbiol 27: 611-616.
    • (1998) Mol Microbiol , vol.27 , pp. 611-616
    • Cornelissen, C.N.1    Kelley, M.2    Hobbs, M.M.3    Anderson, J.E.4    Cannon, J.G.5
  • 38
    • 0037423231 scopus 로고    scopus 로고
    • Passage of heme-iron across the envelope of Staphylococcus aureus
    • Mazmanian SK, Skaar EP, Gaspar AH, Humayun M, Gornicki P, et al. (2003) Passage of heme-iron across the envelope of Staphylococcus aureus. Science 299: 906-909.
    • (2003) Science , vol.299 , pp. 906-909
    • Mazmanian, S.K.1    Skaar, E.P.2    Gaspar, A.H.3    Humayun, M.4    Gornicki, P.5
  • 39
    • 0028968322 scopus 로고
    • The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence
    • Stojiljkovic I, Hwa V, de Saint Martin L, O'Gaora P, Nassif X, et al. (1995) The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence. Mol Microbiol 15: 531-541.
    • (1995) Mol Microbiol , vol.15 , pp. 531-541
    • Stojiljkovic, I.1    Hwa, V.2    de Saint Martin, L.3    O'Gaora, P.4    Nassif, X.5
  • 40
    • 0029765788 scopus 로고    scopus 로고
    • HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation
    • Stojiljkovic I, Larson J, Hwa V, Anic S, So M, (1996) HmbR outer membrane receptors of pathogenic Neisseria spp.: iron-regulated, hemoglobin-binding proteins with a high level of primary structure conservation. J Bacteriol 178: 4670-4678.
    • (1996) J Bacteriol , vol.178 , pp. 4670-4678
    • Stojiljkovic, I.1    Larson, J.2    Hwa, V.3    Anic, S.4    So, M.5
  • 41
    • 0022607252 scopus 로고
    • Salmonella typhimurium virulence genes necessary to exploit the Itys/s genotype of the mouse
    • Benjamin WH Jr, Turnbough CL Jr, Posey BS, Briles DE, (1986) Salmonella typhimurium virulence genes necessary to exploit the Itys/s genotype of the mouse. Infect Immun 51: 872-878.
    • (1986) Infect Immun , vol.51 , pp. 872-878
    • Benjamin Jr., W.H.1    Turnbough Jr., C.L.2    Posey, B.S.3    Briles, D.E.4
  • 42
    • 0027394158 scopus 로고
    • Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine
    • Stojiljkovic I, Cobeljic M, Hantke K, (1993) Escherichia coli K-12 ferrous iron uptake mutants are impaired in their ability to colonize the mouse intestine. FEMS Microbiol Lett 108: 111-115.
    • (1993) FEMS Microbiol Lett , vol.108 , pp. 111-115
    • Stojiljkovic, I.1    Cobeljic, M.2    Hantke, K.3
  • 43
    • 0026426108 scopus 로고
    • The ability of rifampin-resistant Escherichia coli to colonize the mouse intestine is enhanced by the presence of a plasmid-encoded aerobactin-iron(III) uptake system
    • Stojiljkovic I, Cobeljic M, Trgovcevic Z, Salaj-Smic E, (1991) The ability of rifampin-resistant Escherichia coli to colonize the mouse intestine is enhanced by the presence of a plasmid-encoded aerobactin-iron(III) uptake system. FEMS Microbiol Lett 69: 89-93.
    • (1991) FEMS Microbiol Lett , vol.69 , pp. 89-93
    • Stojiljkovic, I.1    Cobeljic, M.2    Trgovcevic, Z.3    Salaj-Smic, E.4
  • 44
    • 0025707199 scopus 로고
    • Dihydroxybenzoylserine-a siderophore for E. coli
    • Hantke K, (1990) Dihydroxybenzoylserine-a siderophore for E. coli. FEMS Microbiol Lett 55: 5-8.
    • (1990) FEMS Microbiol Lett , vol.55 , pp. 5-8
    • Hantke, K.1
  • 45
    • 0024495271 scopus 로고
    • Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2
    • Jalal MA, van der Helm D, (1989) Purification and crystallization of ferric enterobactin receptor protein, FepA, from the outer membranes of Escherichia coli UT5600/pBB2. FEBS Lett 243: 366-370.
    • (1989) FEBS Lett , vol.243 , pp. 366-370
    • Jalal, M.A.1    van der Helm, D.2
  • 46
    • 0025219010 scopus 로고
    • Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups
    • Nikaido H, Rosenberg EY, (1990) Cir and Fiu proteins in the outer membrane of Escherichia coli catalyze transport of monomeric catechols: study with beta-lactam antibiotics containing catechol and analogous groups. J Bacteriol 172: 1361-1367.
    • (1990) J Bacteriol , vol.172 , pp. 1361-1367
    • Nikaido, H.1    Rosenberg, E.Y.2
  • 47
    • 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, (2003) 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 100: 3677-3682 Epub 2003 Mar 3624.
    • (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
  • 48
    • 73449084865 scopus 로고    scopus 로고
    • Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin
    • Bachman MA, Miller VL, Weiser JN, (2009) Mucosal lipocalin 2 has pro-inflammatory and iron-sequestering effects in response to bacterial enterobactin. PLoS Pathog 5: e1000622.
    • (2009) PLoS Pathog , vol.5
    • Bachman, M.A.1    Miller, V.L.2    Weiser, J.N.3
  • 49
    • 38849128160 scopus 로고    scopus 로고
    • Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium
    • Crouch ML, Castor M, Karlinsey JE, Kalhorn T, Fang FC, (2008) Biosynthesis and IroC-dependent export of the siderophore salmochelin are essential for virulence of Salmonella enterica serovar Typhimurium. Mol Microbiol 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
  • 50
    • 0037422561 scopus 로고    scopus 로고
    • Identification of pathogen-specific and conserved genes expressed in vivo by an avian pathogenic Escherichia coli strain
    • Dozois CM, Daigle F, Curtiss R 3rd, (2003) Identification of pathogen-specific and conserved genes expressed in vivo by an avian pathogenic Escherichia coli strain. Proc Natl Acad Sci U S A 100: 247-252.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 247-252
    • Dozois, C.M.1    Daigle, F.2    Curtiss 3rd, R.3
  • 51
    • 0026633892 scopus 로고
    • Role of aerobactin in systemic spread of an opportunistic strain of Escherichia coli from the intestinal tract of gnotobiotic lambs
    • Der Vartanian M, Jaffeux B, Contrepois M, Chavarot M, Girardeau JP, et al. (1992) Role of aerobactin in systemic spread of an opportunistic strain of Escherichia coli from the intestinal tract of gnotobiotic lambs. Infect Immun 60: 2800-2807.
    • (1992) Infect Immun , vol.60 , pp. 2800-2807
    • der Vartanian, M.1    Jaffeux, B.2    Contrepois, M.3    Chavarot, M.4    Girardeau, J.P.5
  • 52
    • 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 CM, (2008) Specific roles of the iroBCDEN genes in virulence of an avian pathogenic Escherichia coli O78 strain and in production of salmochelins. Infect Immun 76: 3539-3549.
    • (2008) Infect Immun , vol.76 , pp. 3539-3549
    • Caza, M.1    Lepine, F.2    Milot, S.3    Dozois, C.M.4
  • 53
    • 0037092054 scopus 로고    scopus 로고
    • Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition
    • Cowart RE, (2002) Reduction of iron by extracellular iron reductases: implications for microbial iron acquisition. Arch Biochem Biophys 400: 273-281.
    • (2002) Arch Biochem Biophys , vol.400 , pp. 273-281
    • Cowart, R.E.1
  • 54
    • 0017885589 scopus 로고
    • Stoichiometric and site characteristics of the binding of iron to human transferrin
    • Aisen P, Leibman A, Zweier J, (1978) Stoichiometric and site characteristics of the binding of iron to human transferrin. J Biol Chem 253: 1930-1937.
    • (1978) J Biol Chem , vol.253 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 55
    • 0019153180 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin
    • Mazurier J, Spik G, (1980) Comparative study of the iron-binding properties of human transferrins. I. Complete and sequential iron saturation and desaturation of the lactotransferrin. Biochim Biophys Acta 629: 399-408.
    • (1980) Biochim Biophys Acta , vol.629 , pp. 399-408
    • Mazurier, J.1    Spik, G.2
  • 56
    • 0021686564 scopus 로고
    • Inflammation triggers hypoferremia and de novo synthesis of serum transferrin and ceruloplasmin in mice
    • Beaumier DL, Caldwell MA, Holbein BE, (1984) Inflammation triggers hypoferremia and de novo synthesis of serum transferrin and ceruloplasmin in mice. Infect Immun 46: 489-494.
    • (1984) Infect Immun , vol.46 , pp. 489-494
    • Beaumier, D.L.1    Caldwell, M.A.2    Holbein, B.E.3
  • 57
    • 0030826095 scopus 로고    scopus 로고
    • Does occupational exposure to iron promote infection?
    • Palmer K, Coggon D, (1997) Does occupational exposure to iron promote infection? Occup Environ Med 54: 529-534.
    • (1997) Occup Environ Med , vol.54 , pp. 529-534
    • Palmer, K.1    Coggon, D.2
  • 58
    • 0344837300 scopus 로고    scopus 로고
    • An Escherichia coli MG1655 lipopolysaccharide deep-rough core mutant grows and survives in mouse cecal mucus but fails to colonize the mouse large intestine
    • Moller AK, Leatham MP, Conway T, Nuijten PJ, de Haan LA, et al. (2003) An Escherichia coli MG1655 lipopolysaccharide deep-rough core mutant grows and survives in mouse cecal mucus but fails to colonize the mouse large intestine. Infect Immun 71: 2142-2152.
    • (2003) Infect Immun , vol.71 , pp. 2142-2152
    • Moller, A.K.1    Leatham, M.P.2    Conway, T.3    Nuijten, P.J.4    de Haan, L.A.5
  • 59
    • 0017341656 scopus 로고
    • Microbial ecology of the gastrointestinal tract
    • Savage DC, (1977) Microbial ecology of the gastrointestinal tract. Annu Rev Microbiol 31: 107-133.
    • (1977) Annu Rev Microbiol , vol.31 , pp. 107-133
    • Savage, D.C.1
  • 60
    • 0018368759 scopus 로고
    • Isolation of enterochelin from Escherichia coli
    • Young IG, Gibson F, (1979) Isolation of enterochelin from Escherichia coli,. Methods Enzymol 56: 394-8.
    • (1979) Methods Enzymol , vol.56 , pp. 394-398
    • Young, I.G.1    Gibson, F.2
  • 61
    • 0027475330 scopus 로고
    • Production of the siderophore enterobactin: use of four different fermentation systems and identification of the compound by HPLC
    • Seiffert A, Goeke K, Fielder HP, Zhner H, (1993) Production of the siderophore enterobactin: use of four different fermentation systems and identification of the compound by HPLC. Biotechnol Bioeng 41: 237-44.
    • (1993) Biotechnol Bioeng , vol.41 , pp. 237-244
    • Seiffert, A.1    Goeke, K.2    Fielder, H.P.3    Zhner, H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.