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Volumn 68, Issue 1, 2004, Pages 154-171

Iron Transport Systems in Neisseria meningitidis

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; EXBD PROTEIN; FERRIC ION; FUR PROTEIN; HAPTOGLOBIN; HEMOGLOBIN; HEMOGLOBIN RECEPTOR; HMBR PROTEIN; HPUAB PROTEIN; IRON; IRON COMPLEX; LACTOFERRIN; TONB PROTEIN; TRANSFERRIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG; VACCINE;

EID: 1542719913     PISSN: 10922172     EISSN: None     Source Type: Journal    
DOI: 10.1128/MMBR.68.1.154-171.2004     Document Type: Review
Times cited : (132)

References (180)
  • 1
    • 0029990115 scopus 로고    scopus 로고
    • Transferrin receptors of Neisseria meningitidis: Promising candidates for a broadly cross-protective vaccine
    • Ala'Aldeen, D. 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.1
  • 2
    • 0029671313 scopus 로고    scopus 로고
    • The meningococcal transferrin-binding proteins 1 and 2 are both surface exposed and generate bactericidal antibodies capable of killing homologous and heterologous strains
    • Ala'Aldeen, D. A., and S. P. Borriello. 1996. The meningococcal transferrin-binding proteins 1 and 2 are both surface exposed and generate bactericidal antibodies capable of killing homologous and heterologous strains. Vaccine 14:49-53.
    • (1996) Vaccine , vol.14 , pp. 49-53
    • Ala'Aldeen, D.A.1    Borriello, S.P.2
  • 3
    • 0027509306 scopus 로고
    • Localization of the meningococcal receptors for human transferrin
    • Ala'Aldeen, D. A., N. B. Powell, R. A. Wall, and S. P. Borriello. 1993. Localization of the meningococcal receptors for human transferrin. Infect Immun. 61:751-759.
    • (1993) Infect. Immun. , vol.61 , pp. 751-759
    • Ala'Aldeen, D.A.1    Powell, N.B.2    Wall, R.A.3    Borriello, S.P.4
  • 5
    • 0027314252 scopus 로고
    • The region of human transferrin involved in binding to bacterial transferrin receptors is localized in the C-lobe
    • Alcantara, J., R. H. Yu, and A. B. Schryvers. 1993. The region of human transferrin involved in binding to bacterial transferrin receptors is localized in the C-lobe. Mol. Microbiol. 8:1135-1143.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1135-1143
    • Alcantara, J.1    Yu, R.H.2    Schryvers, A.B.3
  • 6
    • 0034074236 scopus 로고    scopus 로고
    • An isogenic hemoglobin receptor-deficient mutant of Haemophilus ducreyi is attenuated in the human model of experimental infection
    • Al-Tawfiq, J. A., K. R. Fortney, B. P. Katz, A. F. Hood, C. Elkins, and S. M. Spinola. 2000. An isogenic hemoglobin receptor-deficient mutant of Haemophilus ducreyi is attenuated in the human model of experimental infection. J. Infect. Dis. 181:1049-1054.
    • (2000) J. Infect. Dis. , vol.181 , pp. 1049-1054
    • Al-Tawfiq, J.A.1    Fortney, K.R.2    Katz, B.P.3    Hood, A.F.4    Elkins, C.5    Spinola, S.M.6
  • 7
    • 0028661062 scopus 로고
    • A comparison of the three-dimensional structures of human lactoferrin in its iron free and iron saturated forms
    • Anderson, B. F., G. E. Norris, S. V. Rumball, D. H. Thomas, and E. N. Baker. 1994. A comparison of the three-dimensional structures of human lactoferrin in its iron free and iron saturated forms. Adv. Exp. Med. Biol. 357:227-230.
    • (1994) Adv. Exp. Med. Biol. , vol.357 , pp. 227-230
    • Anderson, B.F.1    Norris, G.E.2    Rumball, S.V.3    Thomas, D.H.4    Baker, E.N.5
  • 8
    • 0037783267 scopus 로고    scopus 로고
    • Opposing selective forces for expression of the gonococcal lactoferrin receptor
    • Anderson, J. E., M. M. Hobbs, G. D. Biswas, and P. F. Sparling. 2003. Opposing selective forces for expression of the gonococcal lactoferrin receptor. Mol. Microbiol. 48:1325-1337.
    • (2003) Mol. Microbiol. , vol.48 , pp. 1325-1337
    • Anderson, J.E.1    Hobbs, M.M.2    Biswas, G.D.3    Sparling, P.F.4
  • 9
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson, J. E., P. F. Sparling, and C. N. Cornelissen. 1994. Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization. J. Bacteriol. 176:3162-3170.
    • (1994) J. Bacteriol. , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 10
    • 0007996405 scopus 로고    scopus 로고
    • Meningococcal diseases
    • R. D. Feigin and J. D. Cherry (ed.). W. B. Saunders Co., Philadelphia, Pa
    • Anderson, M. S., M. P. Glode, and A. L. Smith. 1998. Meningococcal diseases, p. 1143-1156. In R. D. Feigin and J. D. Cherry (ed.), Textbook of pediatric infectious diseases. W. B. Saunders Co., Philadelphia, Pa.
    • (1998) Textbook of Pediatric Infectious Diseases , pp. 1143-1156
    • Anderson, M.S.1    Glode, M.P.2    Smith, A.L.3
  • 11
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • Andrews, S. C. 1998. Iron storage in bacteria. Adv. Microb. Physiol. 40:281-351.
    • (1998) Adv. Microb. Physiol. , vol.40 , pp. 281-351
    • Andrews, S.C.1
  • 12
    • 0025069914 scopus 로고
    • Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism
    • Angerer, A., S. Gaisser, and V. Braun. 1990. Nucleotide sequences of the sfuA, sfuB, and sfuC genes of Serratia marcescens suggest a periplasmic-binding-protein-dependent iron transport mechanism. J. Bacteriol. 172:572-578.
    • (1990) J. Bacteriol. , vol.172 , pp. 572-578
    • Angerer, A.1    Gaisser, S.2    Braun, V.3
  • 13
    • 0018837239 scopus 로고
    • Iron acquisition by Neisseria meningitidis in vitro
    • Archibald, F. S., and I. W. DeVoe. 1980. Iron acquisition by Neisseria meningitidis in vitro. Infect. Immun. 27:322-334.
    • (1980) Infect. Immun. , vol.27 , pp. 322-334
    • Archibald, F.S.1    DeVoe, I.W.2
  • 14
    • 0018143704 scopus 로고
    • Iron in Neisseria meningitidis: Minimum requirements, effects of limitation, and characteristics of uptake
    • Archibald, F. S., and I. W. DeVoe. 1978. Iron in Neisseria meningitidis: minimum requirements, effects of limitation, and characteristics of uptake. J. Bacteriol. 136:35-48.
    • (1978) J. Bacteriol. , vol.136 , pp. 35-48
    • Archibald, F.S.1    DeVoe, I.W.2
  • 15
    • 0018620068 scopus 로고
    • Removal of iron from human transferrin by Neisseria meningitidis
    • Archibald, F. S., and I. W. Devoe. 1979. Removal of iron from human transferrin by Neisseria meningitidis. FEMS Microbiol. Lett. 6:159-162.
    • (1979) FEMS Microbiol. Lett. , vol.6 , pp. 159-162
    • Archibald, F.S.1    Devoe, I.W.2
  • 17
    • 0036188896 scopus 로고    scopus 로고
    • Lactoferrin and transferrin: Functional variations on a common structural framework
    • Baker, E. N., H. M. Baker, and R. D. Kidd. 2002. Lactoferrin and transferrin: functional variations on a common structural framework. Biochem. Cell Biol. 80:27-34.
    • (2002) Biochem. Cell Biol. , vol.80 , pp. 27-34
    • Baker, E.N.1    Baker, H.M.2    Kidd, R.D.3
  • 18
    • 0025111596 scopus 로고
    • Expression of Neisseria meningitidis iron-regulated outer membrane proteins, including a 70-kilodalton transferrin receptor, and their potential for use as vaccines
    • Banerjee-Bhatnagar, N., and C. E. Frasch. 1990. Expression of Neisseria meningitidis iron-regulated outer membrane proteins, including a 70-kilodalton transferrin receptor, and their potential for use as vaccines. Infect. Immun. 58:2875-2881.
    • (1990) Infect. Immun. , vol.58 , pp. 2875-2881
    • Banerjee-Bhatnagar, N.1    Frasch, C.E.2
  • 19
    • 0026739111 scopus 로고
    • Expression of a functional neisserial fbp gene in Escherichia coli
    • Berish, S. A., C. Y. Chen, T. A. Mietzner, and S. A. Morse. 1992. Expression of a functional neisserial fbp gene in Escherichia coli. Mol. Microbiol. 6:2607-2615.
    • (1992) Mol. Microbiol. , vol.6 , pp. 2607-2615
    • Berish, S.A.1    Chen, C.Y.2    Mietzner, T.A.3    Morse, S.A.4
  • 20
    • 0025325414 scopus 로고
    • Molecular cloning and characterization of the structural gene for the major iron-regulated protein expressed by Neisseria gonorrhoeae
    • Berish, S. A., T. A. Mietzner, L. W. Mayer, C. A. Genco, B. P. Holloway, and S. A. Morse. 1990. Molecular cloning and characterization of the structural gene for the major iron-regulated protein expressed by Neisseria gonorrhoeae. J. Exp. Med. 171:1535-1546.
    • (1990) J. Exp. Med. , vol.171 , pp. 1535-1546
    • Berish, S.A.1    Mietzner, T.A.2    Mayer, L.W.3    Genco, C.A.4    Holloway, B.P.5    Morse, S.A.6
  • 21
    • 0028957513 scopus 로고
    • Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae
    • Beucher, M., and P. F. Sparling. 1995. Cloning, sequencing, and characterization of the gene encoding FrpB, a major iron-regulated, outer membrane protein of Neisseria gonorrhoeae. J. Bacteriol. 177:2041-2049.
    • (1995) J. Bacteriol. , vol.177 , pp. 2041-2049
    • Beucher, M.1    Sparling, P.F.2
  • 22
    • 0023032272 scopus 로고
    • Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis
    • Black, J. R., D. W. Dyer, M. K. Thompson, and P. F. Sparling. 1986. Human immune response to iron-repressible outer membrane proteins of Neisseria meningitidis. Infect. Immun. 54:710-713.
    • (1986) Infect. Immun. , vol.54 , pp. 710-713
    • Black, J.R.1    Dyer, D.W.2    Thompson, M.K.3    Sparling, P.F.4
  • 23
    • 0031747819 scopus 로고    scopus 로고
    • Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB
    • Bonnah, R. A., and A. B. Schryvers. 1998. Preparation and characterization of Neisseria meningitidis mutants deficient in production of the human lactoferrin-binding proteins LbpA and LbpB. J. Bacteriol. 180:3080-3090.
    • (1998) J. Bacteriol. , vol.180 , pp. 3080-3090
    • Bonnah, R.A.1    Schryvers, A.B.2
  • 24
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein
    • Bonnah, R. A., R. 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.2    Schryvers, A.B.3
  • 25
    • 0031933035 scopus 로고    scopus 로고
    • Biochemical and immunological properties of lactoferrin binding proteins from Moraxella (Branhamella) catarrhalis
    • Bonnah, R. A., R. H. Yu, H. Wong, and A. B. Schryvers. 1998. Biochemical and immunological properties of lactoferrin binding proteins from Moraxella (Branhamella) catarrhalis. Microb. Pathog. 24:89-100.
    • (1998) Microb. Pathog. , vol.24 , pp. 89-100
    • Bonnah, R.A.1    Yu, R.H.2    Wong, H.3    Schryvers, A.B.4
  • 26
    • 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
  • 27
    • 0031559912 scopus 로고    scopus 로고
    • Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy
    • Boulton, I. C., A. R. Gorringe, R. J. Carr, B. Gorinsky, C. L. Joannou, and R. W. Evans. 1997. Characterisation of the meningococcal transferrin binding protein complex by photon correlation spectroscopy. FEBS Lett. 414:409-413.
    • (1997) FEBS Lett. , vol.414 , pp. 409-413
    • Boulton, I.C.1    Gorringe, A.R.2    Carr, R.J.3    Gorinsky, B.4    Joannou, C.L.5    Evans, R.W.6
  • 29
    • 0034442794 scopus 로고    scopus 로고
    • Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions
    • Boulton, I. C., M. K. Yost, J. E. Anderson, and C. N. Cornelissen. 2000. Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions. Infect. Immun. 68:6988-6996.
    • (2000) Infect. Immun. , vol.68 , pp. 6988-6996
    • Boulton, I.C.1    Yost, M.K.2    Anderson, J.E.3    Cornelissen, C.N.4
  • 30
    • 0033496153 scopus 로고    scopus 로고
    • Active transport of siderophore-mimicking antibacterials across the outer membrane
    • Braun, V. 1999. Active transport of siderophore-mimicking antibacterials across the outer membrane. Drug Resist. Update 2:363-369.
    • (1999) Drug Resist. Update , vol.2 , pp. 363-369
    • Braun, V.1
  • 31
    • 0034975764 scopus 로고    scopus 로고
    • Iron uptake mechanisms and their regulation in pathogenic bacteria
    • Braun, V. 2001. Iron uptake mechanisms and their regulation in pathogenic bacteria. Int. J. Med. Microbiol. 291:67-79.
    • (2001) Int. J. Med. Microbiol. , vol.291 , pp. 67-79
    • Braun, V.1
  • 32
    • 0037010152 scopus 로고    scopus 로고
    • Iron transport and signaling in Escherichia coli
    • Braun, V., and M. Braun. 2002. Iron transport and signaling in Escherichia coli. FEBS Lett. 529:78-85.
    • (2002) FEBS Lett. , vol.529 , pp. 78-85
    • Braun, V.1    Braun, M.2
  • 33
    • 0032946645 scopus 로고    scopus 로고
    • Bacterial solutions to the iron-supply problem
    • Braun, V., and H. Killmann. 1999. Bacterial solutions to the iron-supply problem. Trends Biochem. Sci. 24:104-109.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 104-109
    • Braun, V.1    Killmann, H.2
  • 34
    • 0019423427 scopus 로고
    • Increased virulence of Neisseria meningitidis after in vitro iron-limited growth at low pH
    • Brener, D., I. W. DeVoe, and B. E. Holbein. 1981. Increased virulence of Neisseria meningitidis after in vitro iron-limited growth at low pH. Infect. Immun 33:59-66.
    • (1981) Infect. Immun. , vol.33 , pp. 59-66
    • Brener, D.1    DeVoe, I.W.2    Holbein, B.E.3
  • 36
    • 0033178531 scopus 로고    scopus 로고
    • Beta-barrel proteins from bacterial outer membranes: Structure, function and refolding
    • Buchanan, S. K. 1999. Beta-barrel proteins from bacterial outer membranes: structure, function and refolding. Curr. Opin. Struct. Biol. 9:455-461.
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 455-461
    • Buchanan, S.K.1
  • 37
    • 0036219963 scopus 로고    scopus 로고
    • Cytoglobin: A novel globin type ubiquitously expressed in vertebrate tissues
    • Burmester, T., B. Ebner, B. Weich, and T. Hankeln. 2002. Cytoglobin: a novel globin type ubiquitously expressed in vertebrate tissues. Mol. Biol. Evol. 19:416-421.
    • (2002) Mol. Biol. Evol. , vol.19 , pp. 416-421
    • Burmester, T.1    Ebner, B.2    Weich, B.3    Hankeln, T.4
  • 38
    • 0345551954 scopus 로고    scopus 로고
    • Ferric enterobactin binding and utilization by Neisseria gonorrhoeae
    • Carson, S. D., P. E. Klebba, S. M. Newton, and P. F. Sparling. 1999. Ferric enterobactin binding and utilization by Neisseria gonorrhoeae. J. Bacteriol. 181:2895-2901.
    • (1999) J. Bacteriol. , vol.181 , pp. 2895-2901
    • Carson, S.D.1    Klebba, P.E.2    Newton, S.M.3    Sparling, P.F.4
  • 39
    • 0031911354 scopus 로고    scopus 로고
    • Phase variation of hemoglobin utilization in Neisseria gonorrhoeae
    • Chen, C. J., C. Elkins, and P. F. Sparling. 1998. Phase variation of hemoglobin utilization in Neisseria gonorrhoeae. Infect. Immun. 66:987-993.
    • (1998) Infect. Immun. , vol.66 , pp. 987-993
    • Chen, C.J.1    Elkins, C.2    Sparling, P.F.3
  • 40
    • 0027491241 scopus 로고
    • The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin
    • Chen, C. Y., S. A. Berish, S. A. Morse, and T. A. Mietzner. 1993. The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol. Microbiol. 10:311-318.
    • (1993) Mol. Microbiol. , vol.10 , pp. 311-318
    • Chen, C.Y.1    Berish, S.A.2    Morse, S.A.3    Mietzner, T.A.4
  • 41
    • 0032849337 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae bacterioferritin: Structural heterogeneity, involvement in iron storage and protection against oxidative stress
    • Chen, C. Y., and S. A. Morse. 1999. Neisseria gonorrhoeae bacterioferritin: structural heterogeneity, involvement in iron storage and protection against oxidative stress. Microbiology 145:2967-2975.
    • (1999) Microbiology , vol.145 , pp. 2967-2975
    • Chen, C.Y.1    Morse, S.A.2
  • 42
    • 0035352440 scopus 로고    scopus 로고
    • Structural biology of bacterial iron uptake systems
    • Clarke, T. E., L. W. Tari, and H. J. Vogel. 2001. Structural biology of bacterial iron uptake systems. Curr. Top. Med. Chem. 1:7-30.
    • (2001) Curr. Top. Med. Chem. , vol.1 , pp. 7-30
    • Clarke, T.E.1    Tari, L.W.2    Vogel, H.J.3
  • 44
    • 0345492937 scopus 로고    scopus 로고
    • Transferrin-iron uptake by Gram-negative bacteria
    • Cornelissen, C. N. 2003. Transferrin-iron uptake by Gram-negative bacteria. Front. Biosci. 8:d836-d847.
    • (2003) Front. Biosci. , vol.8
    • Cornelissen, C.N.1
  • 45
    • 0031035323 scopus 로고    scopus 로고
    • Characterization of the diversity and the transferrin-binding domain of gonococcal transferrin-binding protein 2
    • Cornelissen, C. N., J. E. Anderson, and P. F. Sparling. 1997. Characterization of the diversity and the transferrin-binding domain of gonococcal transferrin-binding protein 2. Infect. Immun. 65:822-828.
    • (1997) Infect. Immun. , vol.65 , pp. 822-828
    • Cornelissen, C.N.1    Anderson, J.E.2    Sparling, P.F.3
  • 46
    • 0030825114 scopus 로고    scopus 로고
    • Energy-dependent changes in the gonococcal transferrin receptor
    • Cornelissen, C. N., J. E. Anderson, and P. F. Sparling. 1997. Energy-dependent changes in the gonococcal transferrin receptor. Mol. Microbiol. 26:25-35.
    • (1997) Mol. Microbiol. , vol.26 , pp. 25-35
    • Cornelissen, C.N.1    Anderson, J.E.2    Sparling, P.F.3
  • 47
    • 0031974549 scopus 로고    scopus 로고
    • The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers
    • Cornelissen, C. N., M. Kelley, M. M. Hobbs, J. E. Anderson, J. G. Cannon, M. S. Cohen, and P. F. Sparling. 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    Cohen, M.S.6    Sparling, P.F.7
  • 48
    • 0029913326 scopus 로고    scopus 로고
    • Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins
    • Cornelissen, C. N., and P. F. Sparling. 1996. Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins. J. Bacteriol. 178:1437-1444.
    • (1996) J. Bacteriol. , vol.178 , pp. 1437-1444
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 49
    • 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
  • 50
    • 0027378504 scopus 로고
    • Transferrin-binding proteins isolated from Neisseria meningitidis elicit protective and bactericidal antibodies in laboratory animals
    • Danve, B., L. Lissolo, M. Mignon, P. Dumas, S. Colombani, A. B. Schryvers, and M. J. Quentin-Millet. 1993. Transferrin-binding proteins isolated from Neisseria meningitidis elicit protective and bactericidal antibodies in laboratory animals. Vaccine 11:1214-1220.
    • (1993) Vaccine , vol.11 , pp. 1214-1220
    • Danve, B.1    Lissolo, L.2    Mignon, M.3    Dumas, P.4    Colombani, S.5    Schryvers, A.B.6    Quentin-Millet, M.J.7
  • 51
    • 0029783958 scopus 로고    scopus 로고
    • Analysis of Fur binding to operator sequences within the Neisseria gonorrhoeae fbpA promoter
    • Desai, P. J., A. Angerer, and C. A. Genco. 1996. Analysis of Fur binding to operator sequences within the Neisseria gonorrhoeae fbpA promoter. J. Bacteriol. 178:5020-5023.
    • (1996) J. Bacteriol. , vol.178 , pp. 5020-5023
    • Desai, P.J.1    Angerer, A.2    Genco, C.A.3
  • 52
    • 0033802232 scopus 로고    scopus 로고
    • Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus
    • Desai, P. J., E. Garges, and C. A. Genco. 2000. Pathogenic neisseriae can use hemoglobin, transferrin, and lactoferrin independently of the tonB locus. J. Bacteriol. 182:5586-5591.
    • (2000) J. Bacteriol. , vol.182 , pp. 5586-5591
    • Desai, P.J.1    Garges, E.2    Genco, C.A.3
  • 54
    • 0023881254 scopus 로고
    • A pleiotropic iron-uptake mutant of Neisseria meningitidis lacks a 70-kilodalton iron-regulated protein
    • Dyer, D. W., E. P. West, W. McKenna, S. A. Thompson, and P. F. Sparling. 1988. A pleiotropic iron-uptake mutant of Neisseria meningitidis lacks a 70-kilodalton iron-regulated protein. Infect. Immun. 56:977-983.
    • (1988) Infect. Immun. , vol.56 , pp. 977-983
    • Dyer, D.W.1    West, E.P.2    McKenna, W.3    Thompson, S.A.4    Sparling, P.F.5
  • 55
    • 0023193093 scopus 로고
    • Effects of serum carrier proteins on the growth of pathogenic neisseriae with heme-bound iron
    • Dyer, D. W., E. P. West, and P. F. Sparling. 1987. Effects of serum carrier proteins on the growth of pathogenic neisseriae with heme-bound iron. Infect. Immun. 55:2171-2175.
    • (1987) Infect. Immun. , vol.55 , pp. 2171-2175
    • Dyer, D.W.1    West, E.P.2    Sparling, P.F.3
  • 56
    • 0036231348 scopus 로고    scopus 로고
    • Identification of fur and fldA homologs and a Pasteurella multocida tbpA homolog in Histophilus ovis and effects of iron availability on their transcription
    • Ekins, A., and D. F. Niven. 2002. Identification of fur and fldA homologs and a Pasteurella multocida tbpA homolog in Histophilus ovis and effects of iron availability on their transcription. J. Bacteriol. 184:2539-2542.
    • (2002) J. Bacteriol. , vol.184 , pp. 2539-2542
    • Ekins, A.1    Niven, D.F.2
  • 58
    • 0026425756 scopus 로고
    • Analysis of the molecular mass heterogeneity of the transferrin receptor in Neisseria meningitidis and commensal Neisseria
    • Ferreiros, C. M., M. T. Criado, M. Pintor, and L. Ferron. 1991. Analysis of the molecular mass heterogeneity of the transferrin receptor in Neisseria meningitidis and commensal Neisseria. FEMS Microbiol. Lett. 67:123-136.
    • (1991) FEMS Microbiol. Lett. , vol.67 , pp. 123-136
    • Ferreiros, C.M.1    Criado, M.T.2    Pintor, M.3    Ferron, L.4
  • 59
    • 0031908640 scopus 로고    scopus 로고
    • Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein B
    • Fuller, C. A., R. Yu, S. W. Irwin, and A. B. Schryvers. 1998. Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein B. Microb. Pathog. 24:75-87.
    • (1998) Microb. Pathog. , vol.24 , pp. 75-87
    • Fuller, C.A.1    Yu, R.2    Irwin, S.W.3    Schryvers, A.B.4
  • 60
    • 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
  • 61
    • 0032102705 scopus 로고    scopus 로고
    • Cooperation between the components of the meningococcal transferrin receptor, TbpA and TbpB, in the uptake of transferrin iron by the 37-kDa ferric-binding protein (FbpA)
    • Gomez, J. A., M. T. Criado, and C. M. Ferreiros. 1998. Cooperation between the components of the meningococcal transferrin receptor, TbpA and TbpB, in the uptake of transferrin iron by the 37-kDa ferric-binding protein (FbpA). Res. Microbiol. 149:381-387.
    • (1998) Res. Microbiol. , vol.149 , pp. 381-387
    • Gomez, J.A.1    Criado, M.T.2    Ferreiros, C.M.3
  • 62
    • 0028846507 scopus 로고
    • Human antibody response to meningococcal transferrin binding proteins: Evidence for vaccine potential
    • Gorringe, A. R., R. Borrow, A. J. Fox, and A. Robinson. 1995. Human antibody response to meningococcal transferrin binding proteins: evidence for vaccine potential. Vaccine 13:1207-1212.
    • (1995) Vaccine , vol.13 , pp. 1207-1212
    • Gorringe, A.R.1    Borrow, R.2    Fox, A.J.3    Robinson, A.4
  • 63
    • 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
  • 65
    • 0001854259 scopus 로고    scopus 로고
    • Iron in biological systems
    • J. J. Bullen and E. Griffiths (ed.). John Wiley & Sons, Ltd., West Sussex, United Kingdom
    • Griffiths, E. 1999. Iron in biological systems, p. 1-26. In J. J. Bullen and E. Griffiths (ed.), Iron and infection: molecular, physiological and clinical aspects, 2nd ed., vol. 1. John Wiley & Sons, Ltd., West Sussex, United Kingdom.
    • (1999) Iron and Infection: Molecular, Physiological and Clinical Aspects, 2nd Ed. , vol.1 , pp. 1-26
    • Griffiths, E.1
  • 66
    • 0025319222 scopus 로고
    • Antigenic and molecular heterogeneity of the transferrin-binding protein of Neisseria meningitidis
    • Griffiths, E., P. Stevenson, and A. Ray. 1990. Antigenic and molecular heterogeneity of the transferrin-binding protein of Neisseria meningitidis. FEMS Microbiol Lett. 57:31-36.
    • (1990) FEMS Microbiol Lett. , vol.57 , pp. 31-36
    • Griffiths, E.1    Stevenson, P.2    Ray, A.3
  • 67
    • 0001790974 scopus 로고    scopus 로고
    • The iron-uptake systems of pathogenic bacteria, fungi and protozoa
    • J. J. Bullen and E. Griffiths (ed.). John Wiley & Sons, West Sussex, United Kingdom
    • Griffiths, E., and P. Williams. 1999. The iron-uptake systems of pathogenic bacteria, fungi and protozoa, p. 87-212. In J. J. Bullen and E. Griffiths (ed.), Iron and infection: molecular, physiological, and clinical aspects, vol. 1. John Wiley & Sons, West Sussex, United Kingdom.
    • (1999) Iron and Infection: Molecular, Physiological, and Clinical Aspects , vol.1 , pp. 87-212
    • Griffiths, E.1    Williams, P.2
  • 68
    • 0035069457 scopus 로고    scopus 로고
    • Iron and metal regulation in bacteria
    • Hantke, K. 2001. Iron and metal regulation in bacteria. Curr. Opin. Microbiol. 4:172-177.
    • (2001) Curr. Opin. Microbiol. , vol.4 , pp. 172-177
    • Hantke, K.1
  • 69
    • 0019360750 scopus 로고
    • Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin
    • Holbein, B. E. 1981. Enhancement of Neisseria meningitidis infection in mice by addition of iron bound to transferrin. Infect. Immun. 34:120-125.
    • (1981) Infect. Immun. , vol.34 , pp. 120-125
    • Holbein, B.E.1
  • 70
    • 0018926512 scopus 로고
    • Iron-controlled infection with Neisseria meningitidis in mice
    • Holbein, B. E. 1980. Iron-controlled infection with Neisseria meningitidis in mice. Infect. Immun. 29:886-891.
    • (1980) Infect. Immun. , vol.29 , pp. 886-891
    • Holbein, B.E.1
  • 71
    • 0018360061 scopus 로고
    • Neisseria meningitidis infection in mice: Influence of iron, variations in virulence among strains, and pathology
    • Holbein, B. E., K. W. Jericho, and G. C. Likes. 1979. Neisseria meningitidis infection in mice: influence of iron, variations in virulence among strains, and pathology. Infect. Immun. 24:545-551.
    • (1979) Infect. Immun. , vol.24 , pp. 545-551
    • Holbein, B.E.1    Jericho, K.W.2    Likes, G.C.3
  • 72
    • 0027490784 scopus 로고
    • Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex
    • Hor, L. I., and H. A. Shuman. 1993. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. J. Mol. Biol. 233:659-670.
    • (1993) J. Mol. Biol. , vol.233 , pp. 659-670
    • Hor, L.I.1    Shuman, H.A.2
  • 74
    • 0027252119 scopus 로고
    • Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis
    • Irwin, S. W., N. Averil, C. Y. Cheng, and A. B. Schryvers. 1993. Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis. Mol. Microbiol. 8:1125-1133.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1125-1133
    • Irwin, S.W.1    Averil, N.2    Cheng, C.Y.3    Schryvers, A.B.4
  • 76
    • 0028180667 scopus 로고
    • Cloning and sequence analysis of the fur gene encoding an iron-regulatory protein of Neisseria meningitidis
    • Karkhoff-Schweizer, R. R., A. B. Schryvers, and H. P. Schweizer. 1994. Cloning and sequence analysis of the fur gene encoding an iron-regulatory protein of Neisseria meningitidis. Gene 141:139-140.
    • (1994) Gene , vol.141 , pp. 139-140
    • Karkhoff-Schweizer, R.R.1    Schryvers, A.B.2    Schweizer, H.P.3
  • 77
    • 0036842863 scopus 로고    scopus 로고
    • Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB
    • Kenney, C. D., and C. N. Cornelissen. 2002. Demonstration and characterization of a specific interaction between gonococcal transferrin binding protein A and TonB. J. Bacteriol. 184:6138-6145.
    • (2002) J. Bacteriol. , vol.184 , pp. 6138-6145
    • Kenney, C.D.1    Cornelissen, C.N.2
  • 78
    • 0034441291 scopus 로고    scopus 로고
    • fbpABC gene cluster in Neisseria meningitidis is transcribed as an operon
    • Khun, H. H., V. Deved, H. Wong, and B. C. Lee. 2000. fbpABC gene cluster in Neisseria meningitidis is transcribed as an operon. Infect. Immun. 68:7166-7171.
    • (2000) Infect. Immun. , vol.68 , pp. 7166-7171
    • Khun, H.H.1    Deved, V.2    Wong, H.3    Lee, B.C.4
  • 79
    • 0031948656 scopus 로고    scopus 로고
    • A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth
    • Khun, H. H., S. D. Kirby, and B. C. Lee. 1998. A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth. Infect. Immun. 66:2330-2336.
    • (1998) Infect. Immun. , vol.66 , pp. 2330-2336
    • Khun, H.H.1    Kirby, S.D.2    Lee, B.C.3
  • 80
    • 0033942874 scopus 로고    scopus 로고
    • Structure and function of bacterial outer membrane proteins: Barrels in a nutshell
    • Koebnik, R., K. P. Locher, and P. Van Gelder. 2000. Structure and function of bacterial outer membrane proteins: barrels in a nutshell. Mol. Microbiol. 37:239-253.
    • (2000) Mol. Microbiol. , vol.37 , pp. 239-253
    • Koebnik, R.1    Locher, K.P.2    Van Gelder, P.3
  • 81
    • 0343395846 scopus 로고    scopus 로고
    • ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12
    • Koster, W. 2001. ABC transporter-mediated uptake of iron, siderophores, heme and vitamin B12. Res. Microbiol. 152:291-301.
    • (2001) Res. Microbiol. , vol.152 , pp. 291-301
    • Koster, W.1
  • 82
    • 0036176260 scopus 로고    scopus 로고
    • Replication of Neisseria meningitidis within epithelial cells requires TonB-dependent acquisition of host cell iron
    • Larson, J. A., D. L. Higashi, I. Stojiljkovic, and M. So. 2002. Replication of Neisseria meningitidis within epithelial cells requires TonB-dependent acquisition of host cell iron. Infect. Immun. 70:1461-1467.
    • (2002) Infect. Immun. , vol.70 , pp. 1461-1467
    • Larson, J.A.1    Higashi, D.L.2    Stojiljkovic, I.3    So, M.4
  • 83
    • 0028308217 scopus 로고
    • Isolation and characterization of the haemin-binding proteins from Neisseria meningitidis
    • Lee, B. C. 1994. Isolation and characterization of the haemin-binding proteins from Neisseria meningitidis. Microbiology 140:1473-1480.
    • (1994) Microbiology , vol.140 , pp. 1473-1480
    • Lee, B.C.1
  • 84
    • 0029560596 scopus 로고
    • Quelling the red menace: Haem capture by bacteria
    • Lee, B. C. 1995. Quelling the red menace: haem capture by bacteria. Mol. Microbiol. 18:383-390.
    • (1995) Mol. Microbiol. , vol.18 , pp. 383-390
    • Lee, B.C.1
  • 85
    • 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
  • 86
    • 0027202149 scopus 로고
    • Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2
    • 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-binding proteins Tbp1 and Tbp2. 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
  • 87
    • 0028937627 scopus 로고
    • Identification of an iron-regulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin
    • Lewis, L. A., and D. W. Dyer. 1995. Identification of an iron-regulated outer membrane protein of Neisseria meningitidis involved in the utilization of hemoglobin complexed to haptoglobin. J. Bacteriol. 177:1299-1306.
    • (1995) J. Bacteriol. , vol.177 , pp. 1299-1306
    • Lewis, L.A.1    Dyer, D.W.2
  • 88
    • 0033054886 scopus 로고    scopus 로고
    • Phase variation of HpuAB and HmbR, two distinct haemoglobin receptors of Neisseria meningitidis DNM2
    • Lewis, L. A., M. Gipson, K. Hartman, T. Ownbey, J. Vaughn, and D. W. Dyer. 1999. Phase variation of HpuAB and HmbR, two distinct haemoglobin receptors of Neisseria meningitidis DNM2. Mol. Microbiol. 32:977-989.
    • (1999) Mol. Microbiol. , vol.32 , pp. 977-989
    • Lewis, L.A.1    Gipson, M.2    Hartman, K.3    Ownbey, T.4    Vaughn, J.5    Dyer, D.W.6
  • 89
    • 0031025513 scopus 로고    scopus 로고
    • Molecular characterization of hpuAB, the haemoglobin-haptoglobin-utilization operon of Neisseria meningitidis
    • Lewis, L. A., E. Gray, Y. P. Wang, B. A. Roe, and D. W. Dyer. 1997. Molecular characterization of hpuAB, the haemoglobin-haptoglobin-utilization operon of Neisseria meningitidis. Mol. Microbiol. 23:737-749.
    • (1997) Mol. Microbiol. , vol.23 , pp. 737-749
    • Lewis, L.A.1    Gray, E.2    Wang, Y.P.3    Roe, B.A.4    Dyer, D.W.5
  • 90
    • 0031866123 scopus 로고    scopus 로고
    • Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor
    • Lewis, L. A., K. Rohde, M. Gipson, B. Behrens, E. Gray, S. I. Toth, B. A. Roe, and D. W. Dyer. 1998. Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor. Infect. Immun. 66:3017-3023.
    • (1998) Infect. Immun. , vol.66 , pp. 3017-3023
    • Lewis, L.A.1    Rohde, K.2    Gipson, M.3    Behrens, B.4    Gray, E.5    Toth, S.I.6    Roe, B.A.7    Dyer, D.W.8
  • 91
    • 0002023516 scopus 로고
    • Preliminary biochemical characterization of transferrin binding proteins from Neisseria meningitidis
    • C. Conde-Glez, S. Morse, P. Rice, F. Sparling, and E. Calderon (ed.). Instituto Nacional de Salud Publica, Cuernavaca, Mexico
    • Lissolo, L., P. Dumas, G. Maitre, and M. Quentin-Millet. 1994. Preliminary biochemical characterization of transferrin binding proteins from Neisseria meningitidis, p. 399-405. In C. Conde-Glez, S. Morse, P. Rice, F. Sparling, and E. Calderon (ed.), Pathobiology and immunobiology of Neisseriaceae. Instituto Nacional de Salud Publica, Cuernavaca, Mexico.
    • (1994) Pathobiology and Immunobiology of Neisseriaceae , pp. 399-405
    • Lissolo, L.1    Dumas, P.2    Maitre, G.3    Quentin-Millet, M.4
  • 92
    • 0028935214 scopus 로고
    • Evaluation of transferrin-binding protein 2 within the transferrin-binding protein complex as a potential antigen for future meningococcal vaccines
    • Lissolo, L., G. Maitre-Wilmotte, P. Dumas, M. Mignon, B. Danve, and M. J. Quentin-Millet. 1995. Evaluation of transferrin-binding protein 2 within the transferrin-binding protein complex as a potential antigen for future meningococcal vaccines. Infect. Immun. 63:884-890.
    • (1995) Infect. Immun. , vol.63 , pp. 884-890
    • Lissolo, L.1    Maitre-Wilmotte, G.2    Dumas, P.3    Mignon, M.4    Danve, B.5    Quentin-Millet, M.J.6
  • 93
    • 0036153922 scopus 로고    scopus 로고
    • Specific ligand binding attributable to individual epitopes of gonococcal transferrin binding protein A
    • Masri, H. P., and C. N. Cornelissen. 2002. Specific ligand binding attributable to individual epitopes of gonococcal transferrin binding protein A. Infect. Immun. 70:732-740.
    • (2002) Infect. Immun. , vol.70 , pp. 732-740
    • Masri, H.P.1    Cornelissen, C.N.2
  • 94
    • 0029032190 scopus 로고
    • Diversity of the transferrin-binding protein Tbp2 of Neisseria meningitidis
    • Mazarin, V., B. Rokbi, and M. J. Quentin-Millet. 1995. Diversity of the transferrin-binding protein Tbp2 of Neisseria meningitidis. Gene 158:145-146.
    • (1995) Gene , vol.158 , pp. 145-146
    • Mazarin, V.1    Rokbi, B.2    Quentin-Millet, M.J.3
  • 95
    • 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
  • 96
    • 0019450043 scopus 로고
    • Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds
    • Mickelsen, P. A., and P. F. Sparling. 1981. Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from transferrin and iron compounds. Infect. Immun. 33:555-564.
    • (1981) Infect. Immun. , vol.33 , pp. 555-564
    • Mickelsen, P.A.1    Sparling, P.F.2
  • 97
    • 0023223872 scopus 로고
    • Purification and characterization of the major iron-regulated protein expressed by pathogenic Neisseriae
    • Mietzner, T. A., G. Bolan, G. K. Schoolnik, and S. A. Morse. 1987. Purification and characterization of the major iron-regulated protein expressed by pathogenic Neisseriae. J. Exp Med. 165:1041-1057.
    • (1987) J. Exp Med. , vol.165 , pp. 1041-1057
    • Mietzner, T.A.1    Bolan, G.2    Schoolnik, G.K.3    Morse, S.A.4
  • 98
    • 0021240437 scopus 로고
    • Identification of an iron-regulated 37,000-dalton protein in the cell envelope of Neisseria gonorrhoeae
    • Mietzner, T. A., G. H. Luginbuhl, E. Sandstrom, and S. A. Morse. 1984. Identification of an iron-regulated 37,000-dalton protein in the cell envelope of Neisseria gonorrhoeae. Infect. Immun. 45:410-416.
    • (1984) Infect. Immun. , vol.45 , pp. 410-416
    • Mietzner, T.A.1    Luginbuhl, G.H.2    Sandstrom, E.3    Morse, S.A.4
  • 99
    • 0028070009 scopus 로고
    • The role of iron-binding proteins in the survival of pathogenic bacteria
    • Mietzner, T. A., and S. A. Morse. 1994. The role of iron-binding proteins in the survival of pathogenic bacteria. Annu. Rev. Nutr. 14:471-493.
    • (1994) Annu. Rev. Nutr. , vol.14 , pp. 471-493
    • Mietzner, T.A.1    Morse, S.A.2
  • 100
    • 0026570878 scopus 로고
    • Meningococcal meningitis in sub-Saharan Africa: A model for the epidemic process
    • Moore, P. S. 1992. Meningococcal meningitis in sub-Saharan Africa: a model for the epidemic process. Clin. Infect. Dis. 14:515-525.
    • (1992) Clin. Infect. Dis. , vol.14 , pp. 515-525
    • Moore, P.S.1
  • 101
    • 0024042264 scopus 로고
    • A potential role for the major iron-regulated protein expressed by pathogenic Neisseria species
    • Morse, S. A., C. Y. Chen, A. LeFaou, and T. A. Mietzner. 1988. A potential role for the major iron-regulated protein expressed by pathogenic Neisseria species. Rev. Infect. Dis. 10(Suppl. 2):S306-S310.
    • (1988) Rev. Infect. Dis. , vol.10 , Issue.SUPPL. 2
    • Morse, S.A.1    Chen, C.Y.2    LeFaou, A.3    Mietzner, T.A.4
  • 102
    • 0032323640 scopus 로고    scopus 로고
    • Overview of bacterial ABC transporters
    • Nikaido, H., and J. A. Hall. 1998. Overview of bacterial ABC transporters. Methods Enzymol. 292:3-20.
    • (1998) Methods Enzymol. , vol.292 , pp. 3-20
    • Nikaido, H.1    Hall, J.A.2
  • 103
    • 0028073139 scopus 로고
    • Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins
    • Nowalk, A. J., S. B. Tencza, and T. A. Mietzner. 1994. Coordination of iron by the ferric iron-binding protein of pathogenic Neisseria is homologous to the transferrins. Biochemistry 33:12769-12775.
    • (1994) Biochemistry , vol.33 , pp. 12769-12775
    • Nowalk, A.J.1    Tencza, S.B.2    Mietzner, T.A.3
  • 104
    • 0037097029 scopus 로고    scopus 로고
    • Expression and purification of functional recombinant meningococcal transferrin-binding protein A
    • Oakhill, J. S., C. L. Joannou, S. K. Buchanan, A. R. Gorringe, and R. W. Evans. 2002. Expression and purification of functional recombinant meningococcal transferrin-binding protein A. Biochem. J. 364:613-616.
    • (2002) Biochem. J. , vol.364 , pp. 613-616
    • Oakhill, J.S.1    Joannou, C.L.2    Buchanan, S.K.3    Gorringe, A.R.4    Evans, R.W.5
  • 105
    • 0031689477 scopus 로고    scopus 로고
    • Vibrio cholerae iron transport: Haem transport genes are linked to one of two sets of tonB, exbB, exbD genes
    • Occhino, D. A., E. E. Wyckoff, D. P. Henderson, T. J. Wrona, and S. M. Payne. 1998. Vibrio cholerae iron transport: haem transport genes are linked to one of two sets of tonB, exbB, exbD genes. Mol. Microbiol. 29:1493-1507.
    • (1998) Mol. Microbiol. , vol.29 , pp. 1493-1507
    • Occhino, D.A.1    Wyckoff, E.E.2    Henderson, D.P.3    Wrona, T.J.4    Payne, S.M.5
  • 106
    • 0035148818 scopus 로고    scopus 로고
    • Characterization of a novel transferrin receptor in bovine strains of Pasteurella multocida
    • Ogunnariwo, J. A., and A. B. Schryvers. 2001. Characterization of a novel transferrin receptor in bovine strains of Pasteurella multocida. J. Bacteriol. 183:890-896.
    • (2001) J. Bacteriol. , vol.183 , pp. 890-896
    • Ogunnariwo, J.A.1    Schryvers, A.B.2
  • 107
    • 0034874744 scopus 로고    scopus 로고
    • Neisseria meningitidis RTX protein FrpC induces high levels of serum antibodies during invasive disease: Polymorphism of frpC alleles and purification of recombinant FrpC
    • Osicka, R., J. Kalmusova, P. Krizova, and P. Sebo. 2001. Neisseria meningitidis RTX protein FrpC induces high levels of serum antibodies during invasive disease: polymorphism of frpC alleles and purification of recombinant FrpC. Infect. Immun. 69:5509-5519.
    • (2001) Infect. Immun. , vol.69 , pp. 5509-5519
    • Osicka, R.1    Kalmusova, J.2    Krizova, P.3    Sebo, P.4
  • 108
    • 0025040130 scopus 로고
    • N-linked oligosaccharides of human transferrin are not required for binding to bacterial transferrin receptors
    • Padda, J. S., and A. B. Schryvers. 1990. N-linked oligosaccharides of human transferrin are not required for binding to bacterial transferrin receptors. Infect. Immun. 58:2972-2976.
    • (1990) Infect. Immun. , vol.58 , pp. 2972-2976
    • Padda, J.S.1    Schryvers, A.B.2
  • 109
    • 0035174049 scopus 로고    scopus 로고
    • Characterization of HasB, a Serratia marcescens TonB-like protein specifically involved in the haemophore-dependent haem acquisition system
    • Paquelin, A., J. M. Ghigo, S. Bertin, and C. Wandersman. 2001. Characterization of HasB, a Serratia marcescens TonB-like protein specifically involved in the haemophore-dependent haem acquisition system. Mol. Microbiol. 42:995-1005.
    • (2001) Mol. Microbiol. , vol.42 , pp. 995-1005
    • Paquelin, A.1    Ghigo, J.M.2    Bertin, S.3    Wandersman, C.4
  • 110
    • 0017660608 scopus 로고
    • Detection and differentiation of iron-responsive avirulent mutants on Congo red agar
    • Payne, S. M., and R. A. Finkelstein. 1977. Detection and differentiation of iron-responsive avirulent mutants on Congo red agar. Infect. Immun. 18:94-98.
    • (1977) Infect. Immun. , vol.18 , pp. 94-98
    • Payne, S.M.1    Finkelstein, R.A.2
  • 111
    • 0346252351 scopus 로고    scopus 로고
    • Identification of important functional regions of a hemoglobin receptor from Neisseria meningitidis
    • Perkins-Balding, D., M. Baer, and I. Stojiljkovic. 2003. Identification of important functional regions of a hemoglobin receptor from Neisseria meningitidis. Microbiology 149:3423-3435.
    • (2003) Microbiology , vol.149 , pp. 3423-3435
    • Perkins-Balding, D.1    Baer, M.2    Stojiljkovic, I.3
  • 112
    • 0028641362 scopus 로고
    • Molecular characterization of the structural gene for the lactoferrin receptor of the meningococcal strain H44/76
    • Pettersson, A., V. Klarenbeek, J. van Deurzen, J. T. Poolman, and J. Tommassen. 1994. Molecular characterization of the structural gene for the lactoferrin receptor of the meningococcal strain H44/76. Microb. Pathog. 17:395-408.
    • (1994) Microb. Pathog. , vol.17 , pp. 395-408
    • Pettersson, A.1    Klarenbeek, V.2    Van Deurzen, J.3    Poolman, J.T.4    Tommassen, J.5
  • 113
    • 0029080741 scopus 로고
    • Molecular characterization of FrpB, the 70-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis
    • Pettersson, A., A. Maas, D. van Wassenaar, P. van der Ley, and J. Tommassen. 1995. Molecular characterization of FrpB, the 70-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis. Infect. Immun. 63:4181-4184.
    • (1995) Infect. Immun. , vol.63 , pp. 4181-4184
    • Pettersson, A.1    Maas, A.2    Van Wassenaar, D.3    Van Der Ley, P.4    Tommassen, J.5
  • 115
    • 0031984119 scopus 로고    scopus 로고
    • Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis
    • Pettersson, A., T. Prinz, A. Umar, J. van der Biezen, and J. Tommassen. 1998. Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis. Mol. Microbiol. 27:599-610.
    • (1998) Mol. Microbiol. , vol.27 , pp. 599-610
    • Pettersson, A.1    Prinz, T.2    Umar, A.3    Van Der Biezen, J.4    Tommassen, J.5
  • 116
    • 0033614452 scopus 로고    scopus 로고
    • Sequence variability of the meningococcal lactoferrin-binding protein LbpB
    • Pettersson, A., J. van der Biezen, V. Joosten, J. Hendriksen, and J. Tommassen. 1999. Sequence variability of the meningococcal lactoferrin-binding protein LbpB. Gene 231:105-110.
    • (1999) Gene , vol.231 , pp. 105-110
    • Pettersson, A.1    Van Der Biezen, J.2    Joosten, V.3    Hendriksen, J.4    Tommassen, J.5
  • 117
    • 0027281653 scopus 로고
    • Characterization of the transferrin-iron uptake system in Neisseria meningitidis
    • Pintor, M., C. M. Ferreiros, and M. T. Criado. 1993. Characterization of the transferrin-iron uptake system in Neisseria meningitidis. FEMS Microbiol. Lett. 112:159-165.
    • (1993) FEMS Microbiol. Lett. , vol.112 , pp. 159-165
    • Pintor, M.1    Ferreiros, C.M.2    Criado, M.T.3
  • 118
    • 0029762329 scopus 로고    scopus 로고
    • Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2
    • Pintor, M., L. Ferron, J. A. Gomez, A. Gorringe, M. T. Criado, and C. M. Ferreiros. 1996. Blocking of iron uptake by monoclonal antibodies specific for the Neisseria meningitidis transferrin-binding protein 2. J. Med. Microbiol. 45:252-257.
    • (1996) J. Med. Microbiol. , vol.45 , pp. 252-257
    • Pintor, M.1    Ferron, L.2    Gomez, J.A.3    Gorringe, A.4    Criado, M.T.5    Ferreiros, C.M.6
  • 120
    • 0042065285 scopus 로고    scopus 로고
    • Touch and go: Tying TonB to transport
    • Postle, K., and R. J. Kadner. 2003. Touch and go: tying TonB to transport. Mol. Microbiol. 49:869-882.
    • (2003) Mol. Microbiol. , vol.49 , pp. 869-882
    • Postle, K.1    Kadner, R.J.2
  • 121
    • 0031937703 scopus 로고    scopus 로고
    • Differential binding of apo and holo human transferrin to meningococci and co-localisation of the transferrin-binding proteins (TbpA and TbpB)
    • Powell, N. B., K. Bishop, H. M. Palmer, D. A. Ala'Aldeen, A. R. Gorringe, and S. P. Borriello. 1998. Differential binding of apo and holo human transferrin to meningococci and co-localisation of the transferrin-binding proteins (TbpA and TbpB). J. Med. Microbiol. 47:257-264.
    • (1998) J. Med. Microbiol. , vol.47 , pp. 257-264
    • Powell, N.B.1    Bishop, K.2    Palmer, H.M.3    Ala'Aldeen, D.A.4    Gorringe, A.R.5    Borriello, S.P.6
  • 122
    • 0032798522 scopus 로고    scopus 로고
    • Structural characterization of the lactoferrin receptor from Neisseria meningitidis
    • Prinz, T., M. Meyer, A. Pettersson, and J. Tommassen. 1999. Structural characterization of the lactoferrin receptor from Neisseria meningitidis. J. Bacteriol. 181:4417-4419.
    • (1999) J. Bacteriol. , vol.181 , pp. 4417-4419
    • Prinz, T.1    Meyer, M.2    Pettersson, A.3    Tommassen, J.4
  • 123
    • 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
  • 124
    • 0035688874 scopus 로고    scopus 로고
    • Homologues of neisserial heme oxygenase in gram-negative bacteria: Degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa
    • Ratliff, M., W. Zhu, R. Deshmukh, A. Wilks, and I. Stojiljkovic. 2001. Homologues of neisserial heme oxygenase in gram-negative bacteria: degradation of heme by the product of the pigA gene of Pseudomonas aeruginosa. J. Bacteriol. 183:6394-6403.
    • (2001) J. Bacteriol. , vol.183 , pp. 6394-6403
    • Ratliff, M.1    Zhu, W.2    Deshmukh, R.3    Wilks, A.4    Stojiljkovic, I.5
  • 125
    • 0031763457 scopus 로고    scopus 로고
    • Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin
    • Renauld-Mongenie, G., M. Latour, D. Poncet, S. Naville, and M. J. Quentin-Millet. 1998. Both the full-length and the N-terminal domain of the meningococcal transferrin-binding protein B discriminate between human iron-loaded and apo-transferrin. FEMS Microbiol. Lett. 169:171-177.
    • (1998) FEMS Microbiol. Lett. , vol.169 , pp. 171-177
    • Renauld-Mongenie, G.1    Latour, M.2    Poncet, D.3    Naville, S.4    Quentin-Millet, M.J.5
  • 127
    • 0030023410 scopus 로고    scopus 로고
    • Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors
    • Retzer, M. D., A. Kabani, L. L. Button, R. H. Yu, and A. B. Schryvers. 1996. Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors. J. Biol. Chem. 271:1166-1173.
    • (1996) J. Biol. Chem. , vol.271 , pp. 1166-1173
    • Retzer, M.D.1    Kabani, A.2    Button, L.L.3    Yu, R.H.4    Schryvers, A.B.5
  • 128
    • 0031727167 scopus 로고    scopus 로고
    • Discrimination between apo and iron-loaded forms of transferrin 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 transferrin 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
  • 129
    • 0032954031 scopus 로고    scopus 로고
    • Identification of sequences in human transferrin that bind to the bacterial receptor protein, transferrin-binding protein B
    • Retzer, M. D., R. H. Yu, and A. B. Schryvers. 1999. Identification of sequences in human transferrin that bind to the bacterial receptor protein, transferrin-binding protein B. Mol. Microbiol. 32:111-121.
    • (1999) Mol. Microbiol. , vol.32 , pp. 111-121
    • Retzer, M.D.1    Yu, R.H.2    Schryvers, A.B.3
  • 130
    • 0032913075 scopus 로고    scopus 로고
    • HmbR, a hemoglobin-binding outer membrane protein of Neisseria meningitidis, undergoes phase variation
    • Richardson, A. R., and I. Stojiljkovic. 1999. HmbR, a hemoglobin-binding outer membrane protein of Neisseria meningitidis, undergoes phase variation. J. Bacteriol. 181:2067-2074.
    • (1999) J. Bacteriol. , vol.181 , pp. 2067-2074
    • Richardson, A.R.1    Stojiljkovic, I.2
  • 131
    • 0034997722 scopus 로고    scopus 로고
    • Mismatch repair and the regulation of phase variation in Neisseria meningitidis
    • Richardson, A. R., and I. Stojiljkovic. 2001. Mismatch repair and the regulation of phase variation in Neisseria meningitidis. Mol. Microbiol. 40:645-655.
    • (2001) Mol. Microbiol. , vol.40 , pp. 645-655
    • Richardson, A.R.1    Stojiljkovic, I.2
  • 132
  • 133
    • 3242658420 scopus 로고    scopus 로고
    • Mechanisms of iron acquisition by the human pathogens Neisseria meningitidis and Neisseria gonorrhoeae
    • Rohde, K. H., and D. W. Dyer. 2003. Mechanisms of iron acquisition by the human pathogens Neisseria meningitidis and Neisseria gonorrhoeae. Front. Biosci. 8:d1186-d1218.
    • (2003) Front. Biosci. , vol.8
    • Rohde, K.H.1    Dyer, D.W.2
  • 134
    • 0036172781 scopus 로고    scopus 로고
    • Interactions of haemoglobin with the Neisseria meningitidis receptor HpuAB: The role of TonB and an intact proton motive force
    • Rohde, K. H., A. F. Gillaspy, M. D. Hatfield, L. A. Lewis, and D. W. Dyer. 2002. Interactions of haemoglobin with the Neisseria meningitidis receptor HpuAB: the role of TonB and an intact proton motive force. Mol. Microbiol. 43:335-354.
    • (2002) Mol. Microbiol. , vol.43 , pp. 335-354
    • Rohde, K.H.1    Gillaspy, A.F.2    Hatfield, M.D.3    Lewis, L.A.4    Dyer, D.W.5
  • 135
    • 0031032906 scopus 로고    scopus 로고
    • Evaluation of recombinant transferrin-binding protein B variants from Neisseria meningitidis for their ability to induce cross-reactive and bactericidal antibodies against a genetically diverse collection of serogroup B strains
    • Rokbi, B., M. Mignon, G. Maitre-Wilmotte, L. Lissolo, B. Danve, D. A. Caugant, and M. J. Quentin-Millet. 1997. Evaluation of recombinant transferrin-binding protein B variants from Neisseria meningitidis for their ability to induce cross-reactive and bactericidal antibodies against a genetically diverse collection of serogroup B strains. Infect. Immun. 65:55-63.
    • (1997) Infect. Immun. , vol.65 , pp. 55-63
    • Rokbi, B.1    Mignon, M.2    Maitre-Wilmotte, G.3    Lissolo, L.4    Danve, B.5    Caugant, D.A.6    Quentin-Millet, M.J.7
  • 136
    • 0026052699 scopus 로고
    • Evolution of the ferric enterobactin receptor in gram-negative bacteria
    • Rutz, J. M., T. Abdullah, S. P. Singh, V. I. Kalve, and P. E. Klebba. 1991. Evolution of the ferric enterobactin receptor in gram-negative bacteria. J. Bacteriol. 173:5964-5974.
    • (1991) J. Bacteriol. , vol.173 , pp. 5964-5974
    • Rutz, J.M.1    Abdullah, T.2    Singh, S.P.3    Kalve, V.I.4    Klebba, P.E.5
  • 137
    • 0027998545 scopus 로고
    • Identification of a locus involved in the utilization of iron by Haemophilus influenzae
    • Sanders, J. D., L. D. Cope, and E. J. Hansen. 1994. Identification of a locus involved in the utilization of iron by Haemophilus influenzae. Infect. Immun. 62:4515-4525.
    • (1994) Infect. Immun. , vol.62 , pp. 4515-4525
    • Sanders, J.D.1    Cope, L.D.2    Hansen, E.J.3
  • 138
    • 0031034090 scopus 로고    scopus 로고
    • Utilization of host iron sources by Corynebacterium diphtheriae: Identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin
    • Schmitt, M. P. 1997. Utilization of host iron sources by Corynebacterium diphtheriae: identification of a gene whose product is homologous to eukaryotic heme oxygenases and is required for acquisition of iron from heme and hemoglobin. J. Bacteriol. 179:838-845.
    • (1997) J. Bacteriol. , vol.179 , pp. 838-845
    • Schmitt, M.P.1
  • 140
    • 0024323936 scopus 로고
    • Comparison of the abilities of different protein sources of iron to enhance Neisseria meningitidis infection in mice
    • Schryvers, A. B., and G. C. Gonzalez. 1989. Comparison of the abilities of different protein sources of iron to enhance Neisseria meningitidis infection in mice. Infect. Immun. 57:2425-2429.
    • (1989) Infect. Immun. , vol.57 , pp. 2425-2429
    • Schryvers, A.B.1    Gonzalez, G.C.2
  • 141
    • 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. 36:145-147.
    • (1990) Can J. Microbiol. , vol.36 , pp. 145-147
    • Schryvers, A.B.1    Gonzalez, G.C.2
  • 142
    • 0024633541 scopus 로고
    • Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae
    • Schryvers, A. B., and B. C. Lee. 1989. Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae. Can J. Microbiol. 35:409-415.
    • (1989) Can J. Microbiol. , vol.35 , pp. 409-415
    • Schryvers, A.B.1    Lee, B.C.2
  • 143
    • 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
  • 144
    • 0023974498 scopus 로고
    • Identification and characterization of the transferrin receptor from Neisseria meningitidis
    • Schryvers, A. B., and L. J. Morris. 1988. Identification and characterization of the transferrin receptor from Neisseria meningitidis. Mol. Microbiol. 2:281-288.
    • (1988) Mol. Microbiol. , vol.2 , pp. 281-288
    • Schryvers, A.B.1    Morris, L.J.2
  • 145
    • 0033064808 scopus 로고    scopus 로고
    • Iron acquisition systems in the pathogenic Neisseria
    • Schryvers, A. B., and I. Stojiljkovic. 1999. Iron acquisition systems in the pathogenic Neisseria. Mol. Microbiol. 32:1117-1123.
    • (1999) Mol. Microbiol. , vol.32 , pp. 1117-1123
    • Schryvers, A.B.1    Stojiljkovic, I.2
  • 146
    • 0035949642 scopus 로고    scopus 로고
    • Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1
    • Schuller, D. J., W. Zhu, I. Stojiljkovic, A. Wilks, and T. L. Poulos. 2001. Crystal structure of heme oxygenase from the gram-negative pathogen Neisseria meningitidis and a comparison with mammalian heme oxygenase-1. Biochemistry 40:11552-11558.
    • (2001) Biochemistry , vol.40 , pp. 11552-11558
    • Schuller, D.J.1    Zhu, W.2    Stojiljkovic, I.3    Wilks, A.4    Poulos, T.L.5
  • 147
    • 0013475970 scopus 로고
    • Global epidemiology of meningococcal disease
    • Schwartz, B., P. S. Moore, and C. V. Broome. 1989. Global epidemiology of meningococcal disease. Clin. Microbiol. Rev. 2(Suppl.):S118-S124.
    • (1989) Clin. Microbiol. Rev. , vol.2 , Issue.SUPPL.
    • Schwartz, B.1    Moore, P.S.2    Broome, C.V.3
  • 148
    • 0036302724 scopus 로고    scopus 로고
    • The gonococcal fur regulon: Identification of additional genes involved in major catabolic, recombination, and secretory pathways
    • Sebastian, S., S. Agarwal, J. R. Murphy, and C. A. Genco. 2002. The gonococcal fur regulon: identification of additional genes involved in major catabolic, recombination, and secretory pathways. J. Bacteriol. 184:3965-3974.
    • (2002) J. Bacteriol. , vol.184 , pp. 3965-3974
    • Sebastian, S.1    Agarwal, S.2    Murphy, J.R.3    Genco, C.A.4
  • 149
    • 0020045384 scopus 로고
    • Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis
    • Simonson, C., D. Brener, and I. W. DeVoe. 1982. Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis. Infect. Immun. 36:107-113.
    • (1982) Infect. Immun. , vol.36 , pp. 107-113
    • Simonson, C.1    Brener, D.2    DeVoe, I.W.3
  • 151
    • 0034875104 scopus 로고    scopus 로고
    • Comparative whole-genome analyses reveal over 100 putative phase-variable genes in the pathogenic Neisseria spp
    • Snyder, L. A., S. A. Butcher, and N. J. Saunders. 2001. Comparative whole-genome analyses reveal over 100 putative phase-variable genes in the pathogenic Neisseria spp. Microbiology 147:2321-2332.
    • (2001) Microbiology , vol.147 , pp. 2321-2332
    • Snyder, L.A.1    Butcher, S.A.2    Saunders, N.J.3
  • 152
    • 0028086537 scopus 로고
    • Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica
    • Stojiljkovic, I., and K. Hantke. 1994. Transport of haemin across the cytoplasmic membrane through a haemin-specific periplasmic binding-protein-dependent transport system in Yersinia enterocolitica. Mol. Microbiol. 13:719-732.
    • (1994) Mol. Microbiol. , vol.13 , pp. 719-732
    • Stojiljkovic, I.1    Hantke, K.2
  • 154
    • 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
  • 155
    • 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., J. Larson, V. Hwa, S. Anic, and M. So. 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
  • 156
    • 0036263269 scopus 로고    scopus 로고
    • Processing of heme and heme-containing proteins by bacteria
    • Stojiljkovic, I., and D. Perkins-Balding. 2002. Processing of heme and heme-containing proteins by bacteria. DNA Cell Biol. 21:281-295.
    • (2002) DNA Cell Biol. , vol.21 , pp. 281-295
    • Stojiljkovic, I.1    Perkins-Balding, D.2
  • 157
    • 0031018882 scopus 로고    scopus 로고
    • Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in neisseriae
    • Stojiljkovic, I., and N. Srinivasan. 1997. Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in neisseriae. J. Bacteriol. 179:805-812.
    • (1997) J. Bacteriol. , vol.179 , pp. 805-812
    • Stojiljkovic, I.1    Srinivasan, N.2
  • 158
    • 0033678157 scopus 로고    scopus 로고
    • Functional genomics of Neisseria meningitidis pathogenesis
    • Sun, Y. H., S. Bakshi, R. Chalmers, and C. M. Tang. 2000. Functional genomics of Neisseria meningitidis pathogenesis. Nat. Med. 6:1269-1273.
    • (2000) Nat. Med. , vol.6 , pp. 1269-1273
    • Sun, Y.H.1    Bakshi, S.2    Chalmers, R.3    Tang, C.M.4
  • 159
    • 0028308565 scopus 로고
    • Identification and cloning of a fur homologue from Neisseria meningitidis
    • Thomas, C. E., and P. F. Sparling. 1994. Identification and cloning of a fur homologue from Neisseria meningitidis. Mol. Microbiol. 11:725-737.
    • (1994) Mol. Microbiol. , vol.11 , pp. 725-737
    • Thomas, C.E.1    Sparling, P.F.2
  • 160
    • 8944231163 scopus 로고    scopus 로고
    • Isolation and analysis of a fur mutant of Neisseria gonorrhoeae
    • Thomas, C. E., and P. F. Sparling. 1996. Isolation and analysis of a fur mutant of Neisseria gonorrhoeae. J. Bacteriol. 178:4224-4232.
    • (1996) J. Bacteriol. , vol.178 , pp. 4224-4232
    • Thomas, C.E.1    Sparling, P.F.2
  • 162
    • 0027274752 scopus 로고
    • Cloning and nucleotide sequence of frpC, a second gene from Neisseria meningitidis encoding a protein similar to RTX cytotoxins
    • Thompson, S. A., L. L. Wang, and P. F. Sparling. 1993. Cloning and nucleotide sequence of frpC, a second gene from Neisseria meningitidis encoding a protein similar to RTX cytotoxins. Mol. Microbiol. 9:85-96.
    • (1993) Mol. Microbiol. , vol.9 , pp. 85-96
    • Thompson, S.A.1    Wang, L.L.2    Sparling, P.F.3
  • 163
    • 0027537129 scopus 로고
    • Neisseria meningitidis produces iron-regulated proteins related to the RTX family of exoproteins
    • Thompson, S. A., L. L. Wang, A. West, and P. F. Sparling. 1993. Neisseria meningitidis produces iron-regulated proteins related to the RTX family of exoproteins. J. Bacteriol. 175:811-818.
    • (1993) J. Bacteriol. , vol.175 , pp. 811-818
    • Thompson, S.A.1    Wang, L.L.2    West, A.3    Sparling, P.F.4
  • 164
    • 0034998677 scopus 로고    scopus 로고
    • Neisserial TonB-dependent outer-membrane proteins: Detection, regulation and distribution of three putative candidates identified from the genome sequences
    • Turner, P. C., C. E. Thomas, I. Stojiljkovic, C. Elkins, G. Kizel, D. A. Ala'Aldeen, and P. F. Sparling. 2001. Neisserial TonB-dependent outer-membrane proteins: detection, regulation and distribution of three putative candidates identified from the genome sequences. Microbiology 147:1277-1290.
    • (2001) Microbiology , vol.147 , pp. 1277-1290
    • Turner, P.C.1    Thomas, C.E.2    Stojiljkovic, I.3    Elkins, C.4    Kizel, G.5    Ala'Aldeen, D.A.6    Sparling, P.F.7
  • 165
    • 0029946485 scopus 로고    scopus 로고
    • Sequence variability of FrpB, a major iron-regulated outer-membrane protein in the pathogenic neisseriae
    • van der Ley, P., J. van der Biezen, R. Sutmuller, P. Hoogerhout, and J. T. Poolman. 1996. Sequence variability of FrpB, a major iron-regulated outer-membrane protein in the pathogenic neisseriae. Microbiology 142:3269-3274.
    • (1996) Microbiology , vol.142 , pp. 3269-3274
    • Van Der Ley, P.1    Van Der Biezen, J.2    Sutmuller, R.3    Hoogerhout, P.4    Poolman, J.T.5
  • 166
    • 0027944473 scopus 로고
    • Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin
    • Vonder Haar, R. A., M. Legrain, H. V. Kolbe, and E. Jacobs. 1994. Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin. J. Bacteriol. 176:6207-6213.
    • (1994) J. Bacteriol. , vol.176 , pp. 6207-6213
    • Vonder Haar, R.A.1    Legrain, M.2    Kolbe, H.V.3    Jacobs, E.4
  • 168
    • 0021356806 scopus 로고
    • Iron witholding: Defense against infection and neoplasia
    • Weinberg, E. 1984. Iron witholding: defense against infection and neoplasia. Physiol. Rev. 64:65-102.
    • (1984) Physiol. Rev. , vol.64 , pp. 65-102
    • Weinberg, E.1
  • 170
    • 0023252285 scopus 로고
    • Aerobactin utilization by Neisseria gonorrhoeae and cloning of a genomic DNA fragment that complements Escherichia coli fhuB mutations
    • West, S. E., and P. F. Sparling. 1987. Aerobactin utilization by Neisseria gonorrhoeae and cloning of a genomic DNA fragment that complements Escherichia coli fhuB mutations. J. Bacteriol. 169:3414-3421.
    • (1987) J. Bacteriol. , vol.169 , pp. 3414-3421
    • West, S.E.1    Sparling, P.F.2
  • 171
    • 0022005202 scopus 로고
    • Response of Neisseria gonorrhoeae to iron limitation: Alterations in expression of membrane proteins without apparent siderophore production
    • West, S. E., and P. F. Sparling. 1985. Response of Neisseria gonorrhoeae to iron limitation: alterations in expression of membrane proteins without apparent siderophore production. Infect. Immun. 47:388-394.
    • (1985) Infect. Immun. , vol.47 , pp. 388-394
    • West, S.E.1    Sparling, P.F.2
  • 172
    • 1842372027 scopus 로고    scopus 로고
    • Transcription of genes encoding iron and heme acquisition proteins of Haemophilus influenzae during acute otitis media
    • Whitby, P. W., K. E. Sim, D. J. Morton, J. A. Patel, and T. L. Stull. 1997. Transcription of genes encoding iron and heme acquisition proteins of Haemophilus influenzae during acute otitis media. Infect. Immun. 65:4696-4700.
    • (1997) Infect. Immun. , vol.65 , pp. 4696-4700
    • Whitby, P.W.1    Sim, K.E.2    Morton, D.J.3    Patel, J.A.4    Stull, T.L.5
  • 173
    • 0027055150 scopus 로고
    • Bacterial transferrin receptors-structure, function and contribution to virulence
    • Williams, P., and E. Griffiths. 1992. Bacterial transferrin receptors-structure, function and contribution to virulence. Med. Microbiol. Immunol. 181:301-322.
    • (1992) Med. Microbiol. Immunol. , vol.181 , pp. 301-322
    • Williams, P.1    Griffiths, E.2
  • 174
    • 0037810925 scopus 로고    scopus 로고
    • Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe
    • Wong, H., and A. B. Schryvers. 2003. Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe. Microbiology 149:1729-1737.
    • (2003) Microbiology , vol.149 , pp. 1729-1737
    • Wong, H.1    Schryvers, A.B.2
  • 175
    • 84871879182 scopus 로고    scopus 로고
    • Reference deleted
    • Reference deleted.
  • 176
    • 0027818306 scopus 로고
    • The interaction between human transferrin and transferrin binding protein 2 from Moraxella (Branhamella) catarrhalis differs from that of other human pathogens
    • Yu, R. H., and A. B. Schryvers. 1993. The interaction between human transferrin and transferrin binding protein 2 from Moraxella (Branhamella) catarrhalis differs from that of other human pathogens. Microb. Pathog. 15:433-445.
    • (1993) Microb. Pathog. , vol.15 , pp. 433-445
    • Yu, R.H.1    Schryvers, A.B.2
  • 177
    • 0022538777 scopus 로고
    • Nonrandom distribution of iron in circulating human transferrin
    • Zak, O., and P. Aisen. 1986. Nonrandom distribution of iron in circulating human transferrin. Blood 68:157-161.
    • (1986) Blood , vol.68 , pp. 157-161
    • Zak, O.1    Aisen, P.2
  • 178
    • 0033962643 scopus 로고    scopus 로고
    • A second tonB gene in Pseudomonas aeruginosa is linked to the exbB and exbD genes
    • Zhao, Q., and K. Poole. 2000. A second tonB gene in Pseudomonas aeruginosa is linked to the exbB and exbD genes. FEMS Microbiol. Lett. 184:127-132.
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 127-132
    • Zhao, Q.1    Poole, K.2
  • 179
    • 0033988059 scopus 로고    scopus 로고
    • Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene
    • Zhu, W., D. J. Hunt, A. R. Richardson, and I. Stojiljkovic. 2000. Use of heme compounds as iron sources by pathogenic neisseriae requires the product of the hemO gene. J. Bacteriol. 182:439-447.
    • (2000) J. Bacteriol. , vol.182 , pp. 439-447
    • Zhu, W.1    Hunt, D.J.2    Richardson, A.R.3    Stojiljkovic, I.4
  • 180
    • 0034461244 scopus 로고    scopus 로고
    • Degradation of heme in gram-negative bacteria: The product of the hemO gene of neisseriae is a heme oxygenase
    • Zhu, W., A. Wilks, and I. Stojiljkovic. 2000. Degradation of heme in gram-negative bacteria: the product of the hemO gene of neisseriae is a heme oxygenase. J. Bacteriol. 182:6783-6790.
    • (2000) J. Bacteriol. , vol.182 , pp. 6783-6790
    • Zhu, W.1    Wilks, A.2    Stojiljkovic, I.3


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