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Volumn 65, Issue 2, 1997, Pages 514-518

Identification, characterization, and immunogenicity of the lactoferrin- binding protein from Helicobacter pylori

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN RECEPTOR;

EID: 1842370320     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/iai.65.2.514-518.1997     Document Type: Article
Times cited : (131)

References (34)
  • 1
    • 0026584326 scopus 로고
    • Siderophore production and membrane alterations by Bordetella pertussis in response to iron starvation
    • Agiato, L.-A., and D. W. Dyer. 1992. Siderophore production and membrane alterations by Bordetella pertussis in response to iron starvation. Infect. Immun. 60:117-123.
    • (1992) Infect. Immun. , vol.60 , pp. 117-123
    • Agiato, L.-A.1    Dyer, D.W.2
  • 2
    • 0029990115 scopus 로고    scopus 로고
    • Transferrin receptors of Neisseria meningitidis: Promising candidates for a broadly cross-protective vaccine
    • Ala'Aldeen, D. A. A. 1996. Transferrin receptors of Neisseria meningitidis: promising candidates for a broadly cross-protective vaccine. J. Med. Microbiol. 44:237-243.
    • (1996) J. Med. Microbiol. , vol.44 , pp. 237-243
    • Ala'Aldeen, D.A.A.1
  • 3
    • 0002536197 scopus 로고
    • Virulence factors of Helicobacter pylori - Ultrastructural features
    • P. Malfertheiner and H. Ditschuneit (ed.), Springer-Verlag Publishers, Berlin
    • Bode, G., P. Malfertheiner, G. Lehnhardt, and H. Ditschuneit. 1990. Virulence factors of Helicobacter pylori - ultrastructural features, p. 63-73. In P. Malfertheiner and H. Ditschuneit (ed.), Helicobacter pylori, gastritis and peptic ulcer. Springer-Verlag Publishers, Berlin.
    • (1990) Helicobacter Pylori, Gastritis and Peptic Ulcer , pp. 63-73
    • Bode, G.1    Malfertheiner, P.2    Lehnhardt, G.3    Ditschuneit, H.4
  • 4
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein
    • Bonnah, R. A., R. H. Yu, and A. B. Schryvers. 1995. Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein. Microb. Pathog. 19:285-297.
    • (1995) Microb. Pathog. , vol.19 , pp. 285-297
    • Bonnah, R.A.1    Yu, R.H.2    Schryvers, A.B.3
  • 6
    • 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
  • 8
    • 0025823864 scopus 로고
    • Essential role of urease in the pathogenesis of gastritis induced by Helicobacter pylori in gnotobiotic piglets
    • Eaton, K. A., C. L. Brooks, D. R. Morgan, and S. Krakowa. 1991. Essential role of urease in the pathogenesis of gastritis induced by Helicobacter pylori in gnotobiotic piglets. Infect. Immun. 59:2470-2475.
    • (1991) Infect. Immun. , vol.59 , pp. 2470-2475
    • Eaton, K.A.1    Brooks, C.L.2    Morgan, D.R.3    Krakowa, S.4
  • 9
    • 0026680505 scopus 로고
    • Motility as a factor in the colonisation of gnotobiotic piglets by Helicobacter pylori
    • Eaton, K. A., D. R. Morgan, and S. Krakowa. 1992. Motility as a factor in the colonisation of gnotobiotic piglets by Helicobacter pylori. J. Med. Microbiol. 37:123-127.
    • (1992) J. Med. Microbiol. , vol.37 , pp. 123-127
    • Eaton, K.A.1    Morgan, D.R.2    Krakowa, S.3
  • 10
    • 0006533202 scopus 로고
    • Association of Helicobacter pylori with epithelial cells
    • P. Malfertheiner and H. Ditschuneit (ed.), Springer-Verlag Publishers, Berlin
    • Fauchere, J. L., and M. J. Blaser. 1990. Association of Helicobacter pylori with epithelial cells, p. 110-117. In P. Malfertheiner and H. Ditschuneit (ed.), Helicobacter pylori, gastritis and peptic ulcer. Springer-Verlag Publishers, Berlin.
    • (1990) Helicobacter Pylori, Gastritis and Peptic Ulcer , pp. 110-117
    • Fauchere, J.L.1    Blaser, M.J.2
  • 12
    • 0026563174 scopus 로고
    • Cloning and expression of a transferrin-binding protein from Actinobacillus pleuropneumoniae
    • Gerlach, G. F., C. Anderson, A. A. Potter, S. Klashinsky, and P. J. Wilson. 1992. Cloning and expression of a transferrin-binding protein from Actinobacillus pleuropneumoniae. Infect. Immun. 60:892-898.
    • (1992) Infect. Immun. , vol.60 , pp. 892-898
    • Gerlach, G.F.1    Anderson, C.2    Potter, A.A.3    Klashinsky, S.4    Wilson, P.J.5
  • 13
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen, S. D., and A. B. Schryvers. 1996. Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 4:185-191.
    • (1996) Trends Microbiol. , vol.4 , pp. 185-191
    • Gray-Owen, S.D.1    Schryvers, A.B.2
  • 14
    • 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
  • 15
    • 0027653072 scopus 로고
    • Siderophore production and iron regulated envelope protein of Helicobacter pylori
    • Illingworth, D. A., K. S. Walter, P. L. Griffiths, and R. Barclay. 1993. Siderophore production and iron regulated envelope protein of Helicobacter pylori. Zentralbl. Bakteriol. 280:113-119.
    • (1993) Zentralbl. Bakteriol. , vol.280 , pp. 113-119
    • Illingworth, D.A.1    Walter, K.S.2    Griffiths, P.L.3    Barclay, R.4
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head ot bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head ot bacteriophage T4. Nature (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 0024118398 scopus 로고
    • Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae
    • Lee, B. C., and A. B. Schryvers. 1988. Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae. Mol. Microbiol. 2:827-829.
    • (1988) Mol. Microbiol. , vol.2 , pp. 827-829
    • Lee, B.C.1    Schryvers, A.B.2
  • 18
    • 0027202149 scopus 로고
    • Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-proteins Tbp 1 and Thp 2
    • Legrain, M., V. Mazarin, S. W. Irwin, B. Bouchon, M. J. Quentin-Millet, E. Jacobs, and A. B. Schryvers. 1993. Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-proteins Tbp 1 and Thp 2. Gene 130:73-80.
    • (1993) Gene , vol.130 , pp. 73-80
    • Legrain, M.1    Mazarin, V.2    Irwin, S.W.3    Bouchon, B.4    Quentin-Millet, M.J.5    Jacobs, E.6    Schryvers, A.B.7
  • 21
    • 0027931293 scopus 로고
    • Helicobacter pylori
    • Marshall, B. 1994. Helicobacter pylori. Am. J. Gastroenterol. 89(Suppl.): S116-S128.
    • (1994) Am. J. Gastroenterol. , vol.89 , Issue.SUPPL.
    • Marshall, B.1
  • 22
    • 0026048122 scopus 로고
    • Identification and purification of transferrin- And lactoferrin-binding proteins of Bordetella pertussis and Bordetella bronchiseptica
    • Menozzi, F. D., C. Gantiez, and C. Locht. 1991. Identification and purification of transferrin-and lactoferrin-binding proteins of Bordetella pertussis and Bordetella bronchiseptica. Infect. Immun. 59:3982-3988.
    • (1991) Infect. Immun. , vol.59 , pp. 3982-3988
    • Menozzi, F.D.1    Gantiez, C.2    Locht, C.3
  • 23
    • 0020003691 scopus 로고
    • Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin
    • Mickelsen, P. A., E. Blackman, and P. F. Sparling. 1982. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin. Infect. Immun. 35:915-920.
    • (1982) Infect. Immun. , vol.35 , pp. 915-920
    • Mickelsen, P.A.1    Blackman, E.2    Sparling, P.F.3
  • 24
    • 0020346483 scopus 로고
    • Microbial envelope protein related to iron
    • Neilands, J. B. 1982. Microbial envelope protein related to iron. Annu. Rev. Microbiol. 36:285-309.
    • (1982) Annu. Rev. Microbiol. , vol.36 , pp. 285-309
    • Neilands, J.B.1
  • 25
    • 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
  • 26
    • 0026596453 scopus 로고
    • Transferrins and heme-compounds as iron sources for pathogenic bacteria
    • Otto, B. R., A. M. J. J. Verweij-Van Vugt, and D. M. MacLaren. 1992. Transferrins and heme-compounds as iron sources for pathogenic bacteria. Crit. Rev. Microbiol. 18(Suppl. 3):217-233.
    • (1992) Crit. Rev. Microbiol. , vol.18 , Issue.3 SUPPL. , pp. 217-233
    • Otto, B.R.1    Verweij-Van Vugt, A.M.J.J.2    MacLaren, D.M.3
  • 28
    • 0028607079 scopus 로고
    • Insertional inactivation of the gene for the meningococcal lactoferrin binding protein
    • Quinn, M. L., S. J. Weyer, L. A. Lewis, D. W. Dyer, and P. M. Wagner. 1994. Insertional inactivation of the gene for the meningococcal lactoferrin binding protein. Microb. Pathog. 17:227-237.
    • (1994) Microb. Pathog. , vol.17 , pp. 227-237
    • Quinn, M.L.1    Weyer, S.J.2    Lewis, L.A.3    Dyer, D.W.4    Wagner, P.M.5
  • 29
    • 0024475213 scopus 로고
    • Identification of the transferrin- And lactoferrin-binding proteins in Haemophilus influenzae
    • Schryvers, A. B. 1989. Identification of the transferrin-and lactoferrin-binding proteins in Haemophilus influenzae. J. Med. Microbiol. 29:121-130.
    • (1989) J. Med. Microbiol. , vol.29 , pp. 121-130
    • Schryvers, A.B.1
  • 30
    • 0025212523 scopus 로고
    • Receptors for transferrin in pathogenic bacteria are specific for the host's protein
    • Schryvers, A. B., and G. C. Gonzalez. 1990. Receptors for transferrin in pathogenic bacteria are specific for the host's protein. Can. J. Microbiol. 36(Suppl. 2):145-147.
    • (1990) Can. J. Microbiol. , vol.36 , Issue.2 SUPPL. , pp. 145-147
    • Schryvers, A.B.1    Gonzalez, G.C.2
  • 31
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A. B., and L. J. Morris. 1988. Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis. Infect. Immun. 56:1144-1149.
    • (1988) Infect. Immun. , vol.56 , pp. 1144-1149
    • Schryvers, A.B.1    Morris, L.J.2
  • 32
    • 0018149702 scopus 로고
    • Separation and characterisation of the outer membrane of Pseudomonas aeruginosa
    • Takeshi, M., and M. Kageyama. 1978. Separation and characterisation of the outer membrane of Pseudomonas aeruginosa. J. Biochem. 84:179-191.
    • (1978) J. Biochem. , vol.84 , pp. 179-191
    • Takeshi, M.1    Kageyama, M.2
  • 33
    • 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
  • 34
    • 0029128940 scopus 로고
    • Iron-repressible outer membrane proteins of Helicobacter pylori involved in heme uptake
    • Worst, D. J., B. R. Otto, and J. de Graff. 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 Graff, J.3


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