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Volumn 180, Issue 6, 1998, Pages 1473-1479

Helicobacter pylori ribBA-mediated riboflavin production is involved in iron acquisition

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; DNA FRAGMENT; FERRIC ION; GUANOSINE TRIPHOSPHATE CYCLOHYDROLASE I; IRON; IRON BINDING PROTEIN; RIBOFLAVIN;

EID: 0031916447     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/jb.180.6.1473-1479.1998     Document Type: Article
Times cited : (89)

References (42)
  • 1
    • 0001449413 scopus 로고
    • Biosynthesis of flavins
    • F. Muller (ed.), Chemical Rubber Co., Boca Raton, Fla.
    • Bacher, A. 1991. Biosynthesis of flavins, p. 215-259. In F. Muller (ed.), Chemistry and biochemistry of flavoenzymes, vol. 1. Chemical Rubber Co., Boca Raton, Fla.
    • (1991) Chemistry and Biochemistry of Flavoenzymes , vol.1 , pp. 215-259
    • Bacher, A.1
  • 2
    • 0040796607 scopus 로고
    • Three linkage groups of genes involved in riboflavin biosynthesis in Escherichia coli
    • Bandrin, S. V., P. M. Rabinovich, and A. I. Stepanov. 1983. Three linkage groups of genes involved in riboflavin biosynthesis in Escherichia coli. Sov. Genet. 19:1103-1109.
    • (1983) Sov. Genet. , vol.19 , pp. 1103-1109
    • Bandrin, S.V.1    Rabinovich, P.M.2    Stepanov, A.I.3
  • 3
    • 0029766824 scopus 로고    scopus 로고
    • Extracellular iron reductase activity produced by Listeria monocytogenes
    • Barchini, E., and R. E. Cowart. 1996. Extracellular iron reductase activity produced by Listeria monocytogenes. Arch. Microbiol. 166:51-57.
    • (1996) Arch. Microbiol. , vol.166 , pp. 51-57
    • Barchini, E.1    Cowart, R.E.2
  • 4
    • 14444277191 scopus 로고    scopus 로고
    • Characterization of the Helicobacter pylori ribA gene that confers haemolytic activity to Escherichia coli
    • Bereswill, S., F. Fassbinder, A. Covacci, C. Völzing, H. Ries, A. Bacher, and M. Kist. 1997. Characterization of the Helicobacter pylori ribA gene that confers haemolytic activity to Escherichia coli. Ir. J. Med. Sci. 166:30.
    • (1997) Ir. J. Med. Sci. , vol.166 , pp. 30
    • Bereswill, S.1    Fassbinder, F.2    Covacci, A.3    Völzing, C.4    Ries, H.5    Bacher, A.6    Kist, M.7
  • 6
    • 0025349492 scopus 로고
    • Helicobacter pylori and the pathogenesis of gastroduodenal inflammation
    • Blaser, M. J. 1990. Helicobacter pylori and the pathogenesis of gastroduodenal inflammation. J. Infect. Dis. 161:626-633.
    • (1990) J. Infect. Dis. , vol.161 , pp. 626-633
    • Blaser, M.J.1
  • 7
    • 0028242210 scopus 로고
    • Ordered cosmid library and high-resolution physical-genetic map of Helicobacter pylori strain NCTC 11638
    • Bukanov, N. O., and D. E. Berg. 1994. Ordered cosmid library and high-resolution physical-genetic map of Helicobacter pylori strain NCTC 11638. Mol. Microbiol. 11:509-523.
    • (1994) Mol. Microbiol. , vol.11 , pp. 509-523
    • Bukanov, N.O.1    Berg, D.E.2
  • 8
    • 0027469590 scopus 로고
    • Reduction and mobilization of iron by a NAD(P)H:flavin oxidoreductase from Escherichia coli
    • Covès, J., and M. Fontecave. 1993. Reduction and mobilization of iron by a NAD(P)H:flavin oxidoreductase from Escherichia coli. Eur. J. Biochem. 211: 635-641.
    • (1993) Eur. J. Biochem. , vol.211 , pp. 635-641
    • Covès, J.1    Fontecave, M.2
  • 9
    • 0025354925 scopus 로고
    • Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae
    • Dancis, A., R. D. Klausner, A. G. Hinnebusch, and J. G. Barriocanal. 1990. Genetic evidence that ferric reductase is required for iron uptake in Saccharomyces cerevisiae. Mol. Cell. Biol. 10:2294-2301.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 2294-2301
    • Dancis, A.1    Klausner, R.D.2    Hinnebusch, A.G.3    Barriocanal, J.G.4
  • 10
    • 0015458831 scopus 로고
    • Oversynthesis of riboflavin
    • Demain, A. L. 1972. Oversynthesis of riboflavin. Annu. Rev. Microbiol. 26: 369-388.
    • (1972) Annu. Rev. Microbiol. , vol.26 , pp. 369-388
    • Demain, A.L.1
  • 11
    • 0029115569 scopus 로고
    • Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp.
    • Deneer, H. G., V. Healey, and I. Boychuk. 1995. Reduction of exogenous ferric iron by a surface-associated ferric reductase of Listeria spp. Microbiology 141:1985-1992.
    • (1995) Microbiology , vol.141 , pp. 1985-1992
    • Deneer, H.G.1    Healey, V.2    Boychuk, I.3
  • 12
    • 1842370320 scopus 로고    scopus 로고
    • Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori
    • Dhaenens, L., F. Szczebara, and M. O. Husson. 1997. Identification, characterization, and immunogenicity of the lactoferrin-binding protein from Helicobacter pylori. Infect. Immun. 65:514-518.
    • (1997) Infect. Immun. , vol.65 , pp. 514-518
    • Dhaenens, L.1    Szczebara, F.2    Husson, M.O.3
  • 14
    • 0018881256 scopus 로고
    • The involvement of cytochromes in the uptake of ferrichrome by Escherichia coli K-12
    • Eberspächer, B., and V. Braun. 1980. The involvement of cytochromes in the uptake of ferrichrome by Escherichia coli K-12. FEMS Microbiol. Lett. 7: 61-64.
    • (1980) FEMS Microbiol. Lett. , vol.7 , pp. 61-64
    • Eberspächer, B.1    Braun, V.2
  • 15
    • 0024360313 scopus 로고
    • Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers
    • Fontecave, M., R. Eliasson, and P. Reichard. 1989. Enzymatic regulation of the radical content of the small subunit of Escherichia coli ribonucleotide reductase involving reduction of its redox centers. J. Biol. Chem. 264:9164-9170.
    • (1989) J. Biol. Chem. , vol.264 , pp. 9164-9170
    • Fontecave, M.1    Eliasson, R.2    Reichard, P.3
  • 16
    • 0028069230 scopus 로고
    • Ferric reductases or flavin reductases
    • Fontecave, M., J. Covès, and J. L. Pierre. 1994. Ferric reductases or flavin reductases. Biometals 7:3-8.
    • (1994) Biometals , vol.7 , pp. 3-8
    • Fontecave, M.1    Covès, J.2    Pierre, J.L.3
  • 17
    • 0028884997 scopus 로고
    • Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes
    • Fuller, T. E., and M. H. Mulks. 1995. Characterization of Actinobacillus pleuropneumoniae riboflavin biosynthesis genes. J. Bacteriol. 177:7265-7270.
    • (1995) J. Bacteriol. , vol.177 , pp. 7265-7270
    • Fuller, T.E.1    Mulks, M.H.2
  • 18
    • 0028239772 scopus 로고
    • The NAD(P)H: Flavin oxidoreductase from Escherichia coli as a source of Superoxide radicals
    • Gaudu, P., D. Touati, V. Nivière, and M. Fontecave. 1994. The NAD(P)H: flavin oxidoreductase from Escherichia coli as a source of Superoxide radicals. J. Biol. Chem. 269:8182-8188.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8182-8188
    • Gaudu, P.1    Touati, D.2    Nivière, V.3    Fontecave, M.4
  • 19
    • 0001720053 scopus 로고
    • The iron-uptake systems of pathogenic bacteria
    • J. J. Bullen and E. Griffiths (ed.), John Wiley & Sons, Chichester, United Kingdom
    • Griffiths, E. 1987. The iron-uptake systems of pathogenic bacteria, p. 69-138. In J. J. Bullen and E. Griffiths (ed.), Iron and infection: molecular, physiological and clinical aspects. John Wiley & Sons, Chichester, United Kingdom.
    • (1987) Iron and Infection: Molecular, Physiological and Clinical Aspects , pp. 69-138
    • Griffiths, E.1
  • 21
    • 0027276444 scopus 로고
    • Iron acquisition by Helicobacter pylori: Importance of human lactoferrin
    • Husson, M. A., 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.A.1    Legrand, D.2    Spik, G.3    Leclerc, H.4
  • 22
    • 0026599222 scopus 로고
    • Excretion of anthranilate and 3-hydroxyanthranilate by Saccharomyces cerevisiae: Relationship to iron metabolism
    • Lesuisse, E., M. Simon, R. Klein, and P. Labbe. 1992. Excretion of anthranilate and 3-hydroxyanthranilate by Saccharomyces cerevisiae: relationship to iron metabolism. J. Gen. Microbiol. 138:85-89.
    • (1992) J. Gen. Microbiol. , vol.138 , pp. 85-89
    • Lesuisse, E.1    Simon, M.2    Klein, R.3    Labbe, P.4
  • 23
    • 0030959086 scopus 로고    scopus 로고
    • Regulation of intestinal non-haem iron absorption
    • Lombard, M., E. Chua, and P. O'Toole. 1997. Regulation of intestinal non-haem iron absorption. Gut 40:435-439.
    • (1997) Gut , vol.40 , pp. 435-439
    • Lombard, M.1    Chua, E.2    O'Toole, P.3
  • 25
    • 0031018258 scopus 로고    scopus 로고
    • Ferric iron reduction by Ciyptococcus neoformans
    • Nyhus, K. J., A. T. Wilborn, and E. S. Jacobson. 1997. Ferric iron reduction by Ciyptococcus neoformans. Infect. Immun. 65:434-438.
    • (1997) Infect. Immun. , vol.65 , pp. 434-438
    • Nyhus, K.J.1    Wilborn, A.T.2    Jacobson, E.S.3
  • 26
    • 0024243440 scopus 로고
    • Iron and virulence in the family Enterobacteriaceae
    • Payne, S. M. 1988. Iron and virulence in the family Enterobacteriaceae. Crit. Rev. Microbiol. 16:81-111.
    • (1988) Crit. Rev. Microbiol. , vol.16 , pp. 81-111
    • Payne, S.M.1
  • 28
    • 0027236679 scopus 로고
    • Biosynthesis of riboflavin: Cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II in Escherichia coli
    • Richter, G., H. Ritz, G. Katzenmeier, R. Volk, A. Kohnle, F. Lottspeich, D. Allendorf, and A. Bacher. 1993. Biosynthesis of riboflavin: cloning, sequencing, mapping, and expression of the gene coding for GTP cyclohydrolase II in Escherichia coli. J. Bacteriol. 175:4045-4051.
    • (1993) J. Bacteriol. , vol.175 , pp. 4045-4051
    • Richter, G.1    Ritz, H.2    Katzenmeier, G.3    Volk, R.4    Kohnle, A.5    Lottspeich, F.6    Allendorf, D.7    Bacher, A.8
  • 29
    • 0026642218 scopus 로고
    • Biosynthesis of riboflavin: Cloning, sequencing, and expression of the gene coding for 3,4-dihydroxy-2-butanone 4-phosphate synthase of Escherichia coli
    • Richter, G., R. Volk, C. Krieger, H.-W. Lahm, U. Röthlisberger, and A. Bacher. 1992. Biosynthesis of riboflavin: cloning, sequencing, and expression of the gene coding for 3,4-dihydroxy-2-butanone 4-phosphate synthase of Escherichia coli. J. Bacteriol. 174:4050-4056.
    • (1992) J. Bacteriol. , vol.174 , pp. 4050-4056
    • Richter, G.1    Volk, R.2    Krieger, C.3    Lahm, H.-W.4    Röthlisberger, U.5    Bacher, A.6
  • 31
    • 0000773956 scopus 로고
    • Polynuclear complexes of iron and their biological implications
    • Spiro, T. G., and P. Saltman. 1969. Polynuclear complexes of iron and their biological implications. Struct. Bonding 6:116-120.
    • (1969) Struct. Bonding , vol.6 , pp. 116-120
    • Spiro, T.G.1    Saltman, P.2
  • 32
    • 0026445951 scopus 로고
    • Hemin uptake system of Yersinia enterocolitica: Similarities with other TonB-dependent systems in gram-negative bacteria
    • Stojiljkovic, I., and K. Hantke. 1992. Hemin uptake system of Yersinia enterocolitica: similarities with other TonB-dependent systems in gram-negative bacteria. EMBO J. 11:4359-4367.
    • (1992) EMBO J. , vol.11 , pp. 4359-4367
    • Stojiljkovic, I.1    Hantke, K.2
  • 33
    • 0027442863 scopus 로고
    • Riboflavin 3″- and 5′-sulfate, two novel flavins accumulating in the roots of iron-deficient sugar beet (Beta vulgaris)
    • Susin, S., J. Abian, F. Sanchez-Baeza, M. Luisa Peleato, A. Abadia, E. Gelpi, and J. Abadia. 1993. Riboflavin 3″-and 5′-sulfate, two novel flavins accumulating in the roots of iron-deficient sugar beet (Beta vulgaris). J. Biol. Chem. 268:20958-20965.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20958-20965
    • Susin, S.1    Abian, J.2    Sanchez-Baeza, F.3    Luisa Peleato, M.4    Abadia, A.5    Gelpi, E.6    Abadia, J.7
  • 34
    • 0020452003 scopus 로고
    • Riboflavin photosensitized nemolysis of rat erythrocytes in the presence of serum
    • Suzuki, Y., T. Miura, and T. Ogiso. 1982. Riboflavin photosensitized nemolysis of rat erythrocytes in the presence of serum. J. Pharmacobio-Dyn. 5: 568-575.
    • (1982) J. Pharmacobio-Dyn. , vol.5 , pp. 568-575
    • Suzuki, Y.1    Miura, T.2    Ogiso, T.3
  • 36
    • 0022427805 scopus 로고
    • In vivo transfer of genetic information between gram-positive and gram-negative bacteria
    • Trieu-Cuot, P., G. Gerbaud, T. Lambert, and P. Courvalin. 1985. In vivo transfer of genetic information between gram-positive and gram-negative bacteria. EMBO J. 4:3583-3587.
    • (1985) EMBO J. , vol.4 , pp. 3583-3587
    • Trieu-Cuot, P.1    Gerbaud, G.2    Lambert, T.3    Courvalin, P.4
  • 37
    • 0027439286 scopus 로고
    • Transformation of Helicobacter pylori by chromosomal metronidazole resistance and by a plasmid with a selectable chloramphenicol resistance marker
    • Wang, Y., K. P. Roos, and D. E. Taylor. 1993. Transformation of Helicobacter pylori by chromosomal metronidazole resistance and by a plasmid with a selectable chloramphenicol resistance marker. J. Gen. Microbiol. 139:2485-2493.
    • (1993) J. Gen. Microbiol. , vol.139 , pp. 2485-2493
    • Wang, Y.1    Roos, K.P.2    Taylor, D.E.3
  • 38
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E. D. 1978. Iron and infection. Microbiol. Rev. 42:45-66.
    • (1978) Microbiol. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 39
    • 0029128940 scopus 로고
    • Iron-repressible outer membrane proteins of Helicobacter pylori involved in home uptake
    • Worst, D. J., B. R. Otto, and J. De Graaff. 1995. Iron-repressible outer membrane proteins of Helicobacter pylori involved in home 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
  • 40
    • 0030588074 scopus 로고    scopus 로고
    • Human serum antibody response against iron-repressible outer membrane proteins of Helicobacter pylori
    • Worst, D. J., M. Sparrius, E. J. Kuipers, J. G. Kuslers, and J. De Graaff. 1996. Human serum antibody response against iron-repressible outer membrane proteins of Helicobacter pylori. FEMS Microbiol. Lett. 144:29-32.
    • (1996) FEMS Microbiol. Lett. , vol.144 , pp. 29-32
    • Worst, D.J.1    Sparrius, M.2    Kuipers, E.J.3    Kuslers, J.G.4    De Graaff, J.5
  • 42
    • 0017401042 scopus 로고
    • NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme
    • Yubisui, T., T. Maksuki, K. Tanishima, K. Takeshita, and M. Yoneyama. 1977. NADPH-flavin reductase in human erythrocytes and the reduction of methemoglobin through flavin by the enzyme. Biochem. Biophys. Res. Commun. 76:174-182.
    • (1977) Biochem. Biophys. Res. Commun. , vol.76 , pp. 174-182
    • Yubisui, T.1    Maksuki, T.2    Tanishima, K.3    Takeshita, K.4    Yoneyama, M.5


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