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Volumn 78, Issue 5, 2010, Pages 1841-1849

Unique host iron utilization mechanisms of Helicobacter pylori revealed with iron-deficient chemically defined media

Author keywords

[No Author keywords available]

Indexed keywords

HEMOGLOBIN; IRON; LACTOFERRIN; TRANSFERRIN;

EID: 77951229636     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.01258-09     Document Type: Article
Times cited : (50)

References (41)
  • 2
    • 0026461376 scopus 로고
    • Lactoferrin binding properties of Vibrio cholerae
    • Ascencio, F., A. Ljungh, and T. Wadstrom. 1992. Lactoferrin binding properties of Vibrio cholerae. Microbios 70:103-117.
    • (1992) Microbios , vol.70 , pp. 103-117
    • Ascencio, F.1    Ljungh, A.2    Wadstrom, T.3
  • 4
    • 0038397746 scopus 로고    scopus 로고
    • Iron acquisition by Actinobacillus suis: Identification and characterization of transferrin receptor proteins and encoding genes
    • Bahrami, F., A. Elkins, and D. F. Niven. 2003. Iron acquisition by Actinobacillus suis: identification and characterization of transferrin receptor proteins and encoding genes. Vet. Microbiol. 94:79-92.
    • (2003) Vet. Microbiol. , vol.94 , pp. 79-92
    • Bahrami, F.1    Elkins, A.2    Niven, D.F.3
  • 5
    • 0032528861 scopus 로고    scopus 로고
    • Transferrin-binding protein B isolated from Neisseria meningitidis discriminates between apo and diferric human transferrin
    • Boulton, I. C., A. R. Gorringe, N. Allison, A. Robinson, B. Gorinsky, C. L. Joannou, and R. W. Evans. 1998. Transferrin-binding protein B isolated from Neisseria meningitidis discriminates between apo and diferric human transferrin. Biochem. J. 334:269-273.
    • (1998) Biochem. J. , vol.334 , pp. 269-273
    • Boulton, I.C.1    Gorringe, A.R.2    Allison, N.3    Robinson, A.4    Gorinsky, B.5    Joannou, C.L.6    Evans, R.W.7
  • 7
    • 38449109207 scopus 로고    scopus 로고
    • Expanding the Helicobacter pylori genetic toolbox: Modification of an endogenous plasmid for use as a transcriptional reporter and complementation vector
    • Carpenter, B. M., T. K. McDaniel, J. M. Whitmire, H. Gancz, S. Guidotti, S. Censini, and D. S. Merrell. 2007. Expanding the Helicobacter pylori genetic toolbox: modification of an endogenous plasmid for use as a transcriptional reporter and complementation vector. Appl. Environ. Microbiol. 73:7506-7514.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 7506-7514
    • Carpenter, B.M.1    McDaniel, T.K.2    Whitmire, J.M.3    Gancz, H.4    Guidotti, S.5    Censini, S.6    Merrell, D.S.7
  • 8
    • 0028073695 scopus 로고
    • Iron piracy: Acquisition of transferrin-bound iron by bacterial pathogens
    • Cornelissen, C. N., and P. F. Sparling. 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
  • 9
    • 0023730583 scopus 로고
    • Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface
    • Dalmastri, C., P. Valenti, P. Visca, P. Vittorioso, and N. Orsi. 1988. Enhanced antimicrobial activity of lactoferrin by binding to the bacterial surface. Microbiologica 11:225-230.
    • (1988) Microbiologica , vol.11 , pp. 225-230
    • Dalmastri, C.1    Valenti, P.2    Visca, P.3    Vittorioso, P.4    Orsi, N.5
  • 10
    • 0042810743 scopus 로고    scopus 로고
    • Results of long term iron chelation treatment with deferoxamine
    • Davis, B. A., and J. B. Porter. 2002. Results of long term iron chelation treatment with deferoxamine. Adv. Exp. Med. Biol. 509:91-125.
    • (2002) Adv. Exp. Med. Biol. , vol.509 , pp. 91-125
    • Davis, B.A.1    Porter, J.B.2
  • 13
    • 0031115106 scopus 로고    scopus 로고
    • Antibacterial Peptides of Bovine Lactoferrin: Purification and Characterization
    • Dionysius, D. A., and J. M. Milne. 1997. Antibacterial peptides of bovine lactoferrin: purification and characterization. J. Dairy Sci. 80:667-674. (Pubitemid 127446978)
    • (1997) Journal of Dairy Science , vol.80 , Issue.4 , pp. 667-674
    • Dionysius, D.A.1    Milne, J.M.2
  • 14
    • 0028625324 scopus 로고
    • The effects of lactoferrin on gram-negative bacteria
    • Ellison, R. T., III. 1994. The effects of lactoferrin on gram-negative bacteria. Adv. Exp. Med. Biol. 357:71-90.
    • (1994) Adv. Exp. Med. Biol. , vol.357 , pp. 71-90
    • Ellison III, R.T.1
  • 15
    • 0035181250 scopus 로고    scopus 로고
    • Emerging strategies in microbial haem capture
    • Genco, C. A., and D. W. Dixon. 2001. Emerging strategies in microbial haem capture. Mol. Microbiol. 39:1-11.
    • (2001) Mol. Microbiol. , vol.39 , pp. 1-11
    • Genco, C.A.1    Dixon, D.W.2
  • 16
    • 71349086687 scopus 로고    scopus 로고
    • The gene frpB2 of Helicobacter pylori encodes an hemoglobin-binding protein involved in iron acquisition
    • Gonzalez-Lopez, M. A., and J. J. Olivares-Trejo. 2009. The gene frpB2 of Helicobacter pylori encodes an hemoglobin-binding protein involved in iron acquisition. Biometals 22:889-894.
    • (2009) Biometals , vol.22 , pp. 889-894
    • Gonzalez-Lopez, M.A.1    Olivares-Trejo, J.J.2
  • 17
    • 0021916461 scopus 로고
    • Haemophilus influenzae can use human transferrin as a sole source for required iron
    • Herrington, D. A., and P. F. Sparling. 1985. Haemophilus influenzae can use human transferrin as a sole source for required iron. Infect. Immun. 48:248-251.
    • (1985) Infect. Immun. , vol.48 , pp. 248-251
    • Herrington, D.A.1    Sparling, P.F.2
  • 18
    • 0027276444 scopus 로고
    • Iron acquisition by Helicobacter pylori: Importance of human lactoferrin
    • Husson, M. O., D. Legrand, G. Spik, and H. Leclerc. 1993. Iron acquisition by Helicobacter pylori: importance of human lactoferrin. Infect. Immun. 61:2694-2697.
    • (1993) Infect. Immun. , vol.61 , pp. 2694-2697
    • Husson, M.O.1    Legrand, D.2    Spik, G.3    Leclerc, H.4
  • 19
    • 64849084958 scopus 로고    scopus 로고
    • Lactoferrin and desferrioxamine are ineffective in the treatment of Helicobacter pylori infection and may enhance H. pylori growth and gastric inflammation in mice
    • Huynh, H. Q., M. A. Campbell, R. T. Couper, C. D. Tran, A. Lawrence, and R. N. Butler. 2009. Lactoferrin and desferrioxamine are ineffective in the treatment of Helicobacter pylori infection and may enhance H. pylori growth and gastric inflammation in mice. Lett. Appl. Microbiol. 48:517-522.
    • (2009) Lett. Appl. Microbiol. , vol.48 , pp. 517-522
    • Huynh, H.Q.1    Campbell, M.A.2    Couper, R.T.3    Tran, C.D.4    Lawrence, A.5    Butler, R.N.6
  • 20
    • 11144252331 scopus 로고    scopus 로고
    • The effect of Helicobacter pylori infection and dietary iron deficiency on host iron homeostasis: A study in mice
    • Keenan, J. I., R. A. Peterson, R. Fraser, C. M. Frampton, T. A. Walmsley, R. A. Allardyce, and J. A. Roake. 2004. The effect of Helicobacter pylori infection and dietary iron deficiency on host iron homeostasis: a study in mice. Helicobacter 9:643-650.
    • (2004) Helicobacter , vol.9 , pp. 643-650
    • Keenan, J.I.1    Peterson, R.A.2    Fraser, R.3    Frampton, C.M.4    Walmsley, T.A.5    Allardyce, R.A.6    Roake, J.A.7
  • 22
    • 4544300772 scopus 로고    scopus 로고
    • Growth phase regulation of flaA expression in Helicobacter pylori is luxS dependent
    • Loh, J. T., M. H. Forsyth, and T. L. Cover. 2004. Growth phase regulation of flaA expression in Helicobacter pylori is luxS dependent. Infect. Immun. 72:5506-5510.
    • (2004) Infect. Immun. , vol.72 , pp. 5506-5510
    • Loh, J.T.1    Forsyth, M.H.2    Cover, T.L.3
  • 23
    • 0035111890 scopus 로고    scopus 로고
    • Helicobacter pylori pore-forming cytolysin orthologue TlyA possesses in vitro hemolytic activity and has a role in colonization of the gastric mucosa
    • Martino, M. C., R. A. Stabler, Z. W. Zhang, M. J. Farthing, B. W. Wren, and N. Dorrell. 2001. Helicobacter pylori pore-forming cytolysin orthologue TlyA possesses in vitro hemolytic activity and has a role in colonization of the gastric mucosa. Infect. Immun. 69:1697-1703.
    • (2001) Infect. Immun. , vol.69 , pp. 1697-1703
    • Martino, M.C.1    Stabler, R.A.2    Zhang, Z.W.3    Farthing, M.J.4    Wren, B.W.5    Dorrell, N.6
  • 24
    • 0020960235 scopus 로고
    • Comparative study of the iron-binding properties of human transferrins. II. Electron paramagnetic resonance of mixed metal complexes of human lactotransferrin
    • Mazurier, J., J. M. Lhoste, J. Montreuil, and G. Spik. 1983. Comparative study of the iron-binding properties of human transferrins. II. Electron paramagnetic resonance of mixed metal complexes of human lactotransferrin. Biochim. Biophys. Acta 745:44-49.
    • (1983) Biochim. Biophys. Acta , vol.745 , pp. 44-49
    • Mazurier, J.1    Lhoste, J.M.2    Montreuil, J.3    Spik, G.4
  • 25
    • 0036840033 scopus 로고    scopus 로고
    • The Helicobacter pylori flbA flagellar biosynthesis and regulatory gene is required for motility and virulence and modulates urease of H. pylori and Proteus mirabilis
    • McGee, D. J., C. Coker, T. L. Testerman, J. M. Harro, S. V. Gibson, and H. L. Mobley. 2002. The Helicobacter pylori flbA flagellar biosynthesis and regulatory gene is required for motility and virulence and modulates urease of H. pylori and Proteus mirabilis. J. Med. Microbiol. 51:958-970.
    • (2002) J. Med. Microbiol. , vol.51 , pp. 958-970
    • McGee, D.J.1    Coker, C.2    Testerman, T.L.3    Harro, J.M.4    Gibson, S.V.5    Mobley, H.L.6
  • 27
    • 49749118809 scopus 로고    scopus 로고
    • Helicobacter pylori infection and iron stores: A systematic review and meta-analysis
    • Muhsen, K., and D. Cohen. 2008. Helicobacter pylori infection and iron stores: a systematic review and meta-analysis. Helicobacter 13:323-340.
    • (2008) Helicobacter , vol.13 , pp. 323-340
    • Muhsen, K.1    Cohen, D.2
  • 28
  • 29
    • 0025303119 scopus 로고
    • Iron acquisition in Pasteurella haemolytica: Expression and identification of a bovine-specific transferrin receptor
    • Ogunnariwo, J. A., and A. B. Schryvers. 1990. Iron acquisition in Pasteurella haemolytica: expression and identification of a bovine-specific transferrin receptor. Infect. Immun. 58:2091-2097.
    • (1990) Infect. Immun. , vol.58 , pp. 2091-2097
    • Ogunnariwo, J.A.1    Schryvers, A.B.2
  • 30
    • 0026596453 scopus 로고
    • Transferrins and heme-compounds as iron sources for pathogenic bacteria
    • Otto, B. R., A. M. Verweij-van Vught, and D. M. MacLaren. 1992. Transferrins and heme-compounds as iron sources for pathogenic bacteria. Crit. Rev. Microbiol. 18:217-233.
    • (1992) Crit. Rev. Microbiol. , vol.18 , pp. 217-233
    • Otto, B.R.1    Verweij-van Vught, A.M.2    MacLaren, D.M.3
  • 31
    • 0031727167 scopus 로고    scopus 로고
    • Discrimination between apo and iron-loaded forms of transferring by transferrin binding protein B and its N-terminal subfragment
    • Retzer, M. D., R. Yu, Y. Zhang, G. C. Gonzalez, and A. B. Schryvers. 1998. Discrimination between apo and iron-loaded forms of transferring by transferrin binding protein B and its N-terminal subfragment. Microb. Pathog. 25:175-180.
    • (1998) Microb. Pathog. , vol.25 , pp. 175-180
    • Retzer, M.D.1    Yu, R.2    Zhang, Y.3    Gonzalez, G.C.4    Schryvers, A.B.5
  • 32
    • 0032937984 scopus 로고    scopus 로고
    • Non-iron metalloporphyrins: Potent antibacterial compounds that exploit haem/Hb uptake systems of pathogenic bacteria
    • Stojiljkovic, I., V. Kumar, and N. Srinivasan. 1999. Non-iron metalloporphyrins: potent antibacterial compounds that exploit haem/Hb uptake systems of pathogenic bacteria. Mol. Microbiol. 31:429-442.
    • (1999) Mol. Microbiol. , vol.31 , pp. 429-442
    • Stojiljkovic, I.1    Kumar, V.2    Srinivasan, N.3
  • 33
    • 33646554792 scopus 로고    scopus 로고
    • Nutritional requirements and antibiotic resistance patterns of Helicobacter species in chemically defined media
    • Testerman, T. L., P. B. Conn, H. L. Mobley, and D. J. McGee. 2006. Nutritional requirements and antibiotic resistance patterns of Helicobacter species in chemically defined media. J. Clin. Microbiol. 44:1650-1658.
    • (2006) J. Clin. Microbiol. , vol.44 , pp. 1650-1658
    • Testerman, T.L.1    Conn, P.B.2    Mobley, H.L.3    McGee, D.J.4
  • 34
    • 34147170948 scopus 로고    scopus 로고
    • Effect of lactoferrin supplementation on the effectiveness and tolerability of a 7-day quadruple therapy after failure of a first attempt to cure Helicobacter pylori infection
    • Tursi, A., W. Elisei, G. Brandimarte, G. M. Giorgetti, M. E. Modeo, and F. Aiello. 2007. Effect of lactoferrin supplementation on the effectiveness and tolerability of a 7-day quadruple therapy after failure of a first attempt to cure Helicobacter pylori infection. Med. Sci. Monit. 13:CR187-CR190. (Pubitemid 46557753)
    • (2007) Medical Science Monitor , vol.13 , Issue.4
    • Tursi, A.1    Elisei, W.2    Brandimarte, G.3    Giorgetti, G.M.4    Modeo, M.E.5    Aiello, F.6
  • 35
    • 0033913686 scopus 로고    scopus 로고
    • Iron acquisition and virulence in Helicobacter pylori: A major role for FeoB, a high-affinity ferrous iron transporter
    • Velayudhan, J., N. J. Hughes, A. A. McColm, J. Bagshaw, C. L. Clayton, S. C. Andrews, and D. J. Kelly. 2000. Iron acquisition and virulence in Helicobacter pylori: a major role for FeoB, a high-affinity ferrous iron transporter. Mol. Microbiol. 37:274-286.
    • (2000) Mol. Microbiol. , vol.37 , pp. 274-286
    • Velayudhan, J.1    Hughes, N.J.2    McColm, A.A.3    Bagshaw, J.4    Clayton, C.L.5    Andrews, S.C.6    Kelly, D.J.7
  • 36
    • 39649116032 scopus 로고    scopus 로고
    • Adherence of Helicobacter pylori to abiotic surfaces is influenced by serum
    • Williams, J. C., K. A. McInnis, and T. L. Testerman. 2008. Adherence of Helicobacter pylori to abiotic surfaces is influenced by serum. Appl. Environ. Microbiol. 74:1255-1258.
    • (2008) Appl. Environ. Microbiol. , vol.74 , pp. 1255-1258
    • Williams, J.C.1    McInnis, K.A.2    Testerman, T.L.3
  • 37
    • 0031916447 scopus 로고    scopus 로고
    • Helicobacter pylori ribBA-mediated riboflavin production is involved in iron acquisition
    • Worst, D. J., M. M. Gerrits, C. M. Vandenbroucke-Grauls, and J. G. Kusters. 1998. Helicobacter pylori ribBA-mediated riboflavin production is involved in iron acquisition. J. Bacteriol. 180:1473-1479.
    • (1998) J. Bacteriol. , vol.180 , pp. 1473-1479
    • Worst, D.J.1    Gerrits, M.M.2    Vandenbroucke-Grauls, C.M.3    Kusters, J.G.4
  • 38
    • 0029128940 scopus 로고
    • Iron-repressible outer membrane proteins of Helicobacter pylori involved in heme uptake
    • Worst, D. J., B. R. Otto, and J. de Graaff. 1995. Iron-repressible outer membrane proteins of Helicobacter pylori involved in heme uptake. Infect. Immun. 63:4161-4165.
    • (1995) Infect. Immun. , vol.63 , pp. 4161-4165
    • Worst, D.J.1    Otto, B.R.2    De Graaff, J.3
  • 39
    • 38849110869 scopus 로고    scopus 로고
    • Enhanced Fe ion-uptake activity in Helicobacter pylori strains isolated from patients with iron-deficiency anemia
    • Yokota, S. I., M. Konno, E. Mino, K. Sato, M. Takahashi, and N. Fujii. 2008. Enhanced Fe ion-uptake activity in Helicobacter pylori strains isolated from patients with iron-deficiency anemia. Clin. Infect. Dis. 46:e31-33.
    • (2008) Clin. Infect. Dis. , vol.46
    • Yokota, S.I.1    Konno, M.2    Mino, E.3    Sato, K.4    Takahashi, M.5    Fujii, N.6


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