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Volumn 198, Issue 4, 1999, Pages 497-505

A dynamic model of the meningococcal transferrin receptor

Author keywords

[No Author keywords available]

Indexed keywords

IRON; TRANSFERRIN; TRANSFERRIN RECEPTOR;

EID: 0033591605     PISSN: 00225193     EISSN: None     Source Type: Journal    
DOI: 10.1006/jtbi.1999.0928     Document Type: Article
Times cited : (22)

References (50)
  • 1
    • 0029936842 scopus 로고    scopus 로고
    • The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron
    • ADHIKARI S. A., BERISH S. A., NOWALK A. J., VERALDI K. L., MORSE S. A., MEITZNER T. A. The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron. J. Bacteriol. 178:1996;2145-2149.
    • (1996) J. Bacteriol. , vol.178 , pp. 2145-2149
    • Adhikari, S.A.1    Berish, S.A.2    Nowalk, A.J.3    Veraldi, K.L.4    Morse, S.A.5    Meitzner, T.A.6
  • 2
    • 0017885589 scopus 로고
    • Stoichiometric and site characteristics of the binding of iron to human transferrin
    • AISEN P., LEIBMAN A., ZWEIER J. Stoichiometric and site characteristics of the binding of iron to human transferrin. J. Biol. Chem. 253:1978;1930-1937.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 3
    • 0029976088 scopus 로고    scopus 로고
    • Transferrin binding protein 2 interacts with both the N-lobe and C-lobe of ovotransferrin
    • ALCANTARA J., SCHRYVERS A. B. Transferrin binding protein 2 interacts with both the N-lobe and C-lobe of ovotransferrin. Microb. Pathogen. 20:1996;73-85.
    • (1996) Microb. Pathogen. , vol.20 , pp. 73-85
    • Alcantara, J.1    Schryvers, A.B.2
  • 4
    • 0027314252 scopus 로고
    • The region of human transferrin involved in binding to the bacterial transferrin receptors is localised in the C-lobe
    • ALCANTARA J., YU R. H., SCHRYVERS A. B. The region of human transferrin involved in binding to the bacterial transferrin receptors is localised in the C-lobe. Mol. Microbiol. 8:1993;1135-1143.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1135-1143
    • Alcantara, J.1    Yu, R.H.2    Schryvers, A.B.3
  • 5
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilisation
    • ANDERSON J. E., SPARLING P. F., CORNELISSEN C. N. Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilisation. J. Bacteriol. 176:1994;3162-3170.
    • (1994) J. Bacteriol. , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 7
    • 0026646617 scopus 로고
    • New perspectives on the structure and function of transferrins
    • BAKER E. N., LINDLEY P. F. New perspectives on the structure and function of transferrins. J. Inorg. Biochem. 47:1992;147-160.
    • (1992) J. Inorg. Biochem. , vol.47 , pp. 147-160
    • Baker, E.N.1    Lindley, P.F.2
  • 8
    • 0001447664 scopus 로고
    • Transferrins: Insights into structure and function from studies on lactoferrin
    • BAKER E. N., RUMBALL S. V., ANDERSON B. F. Transferrins: insights into structure and function from studies on lactoferrin. TIBS. 12:1987;351-353.
    • (1987) TIBS , vol.12 , pp. 351-353
    • Baker, E.N.1    Rumball, S.V.2    Anderson, B.F.3
  • 9
    • 0032528861 scopus 로고    scopus 로고
    • Transferrin-binding protein B isolated from Neisseria meningitidis discriminates between apo and diferric human transferrin
    • BOULTON I. C., GORRINGE A. R., ALLISON N., ROBINSON A., GORINSKY B., EVANS R. W. Transferrin-binding protein B isolated from Neisseria meningitidis discriminates between apo and diferric human transferrin. Biochem J. 334:1998;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    Evans, R.W.6
  • 10
    • 0031559912 scopus 로고    scopus 로고
    • Characterization of the meningococcal transferrin binding protein complex by photon correlation spectroscopy
    • BOULTON I. C., GORRINGE A. R., CARR R. J. G., GORINSKY B., EVANS R. W. Characterization of the meningococcal transferrin binding protein complex by photon correlation spectroscopy. FEBS Lett. 414:1997;409-413.
    • (1997) FEBS Lett. , vol.414 , pp. 409-413
    • Boulton, I.C.1    Gorringe, A.R.2    Carr, R.J.G.3    Gorinsky, B.4    Evans, R.W.5
  • 11
    • 0033119697 scopus 로고    scopus 로고
    • Purified meningococcal TbpB interacts with a secondary, strain specific, binding site in the N-lobe of human serum transferrin
    • BOULTON I. C., GORRINGE A. R., SCHRYVERS A. B., RETZER M. D., GORINSKY B., EVANS R. W. Purified meningococcal TbpB interacts with a secondary, strain specific, binding site in the N-lobe of human serum transferrin. Biochem. J. 339:1999;143-149.
    • (1999) Biochem. J. , vol.339 , pp. 143-149
    • Boulton, I.C.1    Gorringe, A.R.2    Schryvers, A.B.3    Retzer, M.D.4    Gorinsky, B.5    Evans, R.W.6
  • 14
    • 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., BERISH S. A., MORSE S. A., MEITZNER T. A. The ferric iron-binding protein of pathogenic Neisseria spp. functions as a periplasmic transport protein in iron acquisition from human transferrin. Mol. Microbiol. 10:1993;311-318.
    • (1993) Mol. Microbiol. , vol.10 , pp. 311-318
    • Chen, C.Y.1    Berish, S.A.2    Morse, S.A.3    Meitzner, T.A.4
  • 15
    • 0030825114 scopus 로고    scopus 로고
    • Energy dependent changes in the gonococcal transferrin receptor
    • CORNELISSEN, ANDERSON J. E., SPARLING P. F. Energy dependent changes in the gonococcal transferrin receptor. Mol. Microbiol. 26:1997a;25-35.
    • (1997) Mol. Microbiol. , vol.26 , pp. 25-35
    • Cornelissen1    Anderson, J.E.2    Sparling, P.F.3
  • 16
    • 0031035323 scopus 로고    scopus 로고
    • Characterisation of the diversity and the transferrin-binding domain of gonococcal transferrin-binding protein 2
    • CORNELISSEN C. N., ANDERSON J. E., SPARLING P. F. Characterisation of the diversity and the transferrin-binding domain of gonococcal transferrin-binding protein 2. Infect. Immun. 65:1997b;822-828.
    • (1997) Infect. Immun. , vol.65 , pp. 822-828
    • Cornelissen, C.N.1    Anderson, J.E.2    Sparling, P.F.3
  • 17
    • 0026768392 scopus 로고
    • Gonococcal transferrin-binding protein 1 is required for transferrin utilisation and is homologous to TonB-dependent outer membrane proteins
    • CORNELLISEN C. N., BISWAS G. D., TSAI J., PURCHURI D. K., THOMSON S. A., SPARLING P. F. Gonococcal transferrin-binding protein 1 is required for transferrin utilisation and is homologous to TonB-dependent outer membrane proteins. J. Bacteriol. 174:1992;5788-5797.
    • (1992) J. Bacteriol. , vol.174 , pp. 5788-5797
    • Cornellisen, C.N.1    Biswas, G.D.2    Tsai, J.3    Purchuri, D.K.4    Thomson, S.A.5    Sparling, P.F.6
  • 18
    • 0031974549 scopus 로고    scopus 로고
    • The transferrin receptor expressed by gonococcal FA1090 is required for the experimental infection of human male volunteers
    • CORNELISSEN C. N., KELLEY M., HOBBS M. M., ANDERSON J. E., CANNON J. G., COHEN M. S., SPARLING P. F. The transferrin receptor expressed by gonococcal FA1090 is required for the experimental infection of human male volunteers. Mol. Microbiol. 27:1998;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
  • 19
    • 0028073695 scopus 로고
    • Iron piracy: Acquisition of transferrin bound iron by bacterial pathogens
    • CORNELISSEN C. N., SPARLING P. F. Iron piracy: acquisition of transferrin bound iron by bacterial pathogens. Mol. Microbiol. 14:1994;843-850.
    • (1994) Mol. Microbiol. , vol.14 , pp. 843-850
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 20
    • 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., SPARLING P. F. Binding and surface exposure characteristics of the gonococcal transferrin receptor are dependent on both transferrin-binding proteins. J. Bacteriol. 178:1996;1437-1444.
    • (1996) J. Bacteriol. , vol.178 , pp. 1437-1444
    • Cornelissen, C.N.1    Sparling, P.F.2
  • 21
    • 0026779245 scopus 로고
    • Crystal Structures explain functional properties of two e.coli porins
    • COWAN S. W., SCHIRMER T., RUMMEL G. Crystal Structures explain functional properties of two e.coli porins. Nature. 358:1992;727-723.
    • (1992) Nature , vol.358 , pp. 727-723
    • Cowan, S.W.1    Schirmer, T.2    Rummel, G.3
  • 23
    • 0001781299 scopus 로고
    • Surface plasmon resonance: The technique and its applications to biomaterial processes
    • DAVIES J. Surface plasmon resonance: the technique and its applications to biomaterial processes. Nanobiology. 3:1994;5-16.
    • (1994) Nanobiology , vol.3 , pp. 5-16
    • Davies, J.1
  • 25
    • 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., YU R., IRWIN S. W., SCHRYVERS A. B. Biochemical evidence for a conserved interaction between bacterial transferrin binding protein A and transferrin binding protein B. Mircob. Pathogen. 24:1998;75-87.
    • (1998) Mircob. Pathogen. , vol.24 , pp. 75-87
    • Fuller, C.A.1    Yu, R.2    Irwin, S.W.3    Schryvers, A.B.4
  • 26
    • 0030266168 scopus 로고    scopus 로고
    • Antigenicity, cross-reactivity and surface exposre of the Neisseria meningitidis 37 kDa protein Fbp
    • GOMEZ J. A., AGRA C., FERRON L., POWELL N., PINTOR M., CRIADO M. T., FERREIROS C. M. Antigenicity, cross-reactivity and surface exposre of the Neisseria meningitidis 37 kDa protein Fbp. Vaccine. 14:1996;1340-1346.
    • (1996) Vaccine , vol.14 , pp. 1340-1346
    • Gomez, J.A.1    Agra, C.2    Ferron, L.3    Powell, N.4    Pintor, M.5    Criado, M.T.6    Ferreiros, C.M.7
  • 27
    • 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., CRIADO M. T., FERREIROS C. M. 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. 149:1998;381-387.
    • (1998) Res. Microbiol. , vol.149 , pp. 381-387
    • Gomez, J.A.1    Criado, M.T.2    Ferreiros, C.M.3
  • 28
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • GRAY-OWEN S. D., SCHRYVERS A. B. Bacterial transferrin and lactoferrin receptors. Trends Microbiol. 4:1996;185-191.
    • (1996) Trends Microbiol. , vol.4 , pp. 185-191
    • Gray-Owen, S.D.1    Schryvers, A.B.2
  • 29
    • 85030353437 scopus 로고
    • Structure and thermal stability of isolated N- And C-lobes of human serum transferrin
    • p. 107
    • HADDEN J. M., EVANS R. W., SRAI K. S. Structure and thermal stability of isolated N- and C-lobes of human serum transferrin. Proc. Int. Conf. Bioiron. 1995;. p. 107.
    • (1995) Proc. Int. Conf. Bioiron
    • Hadden, J.M.1    Evans, R.W.2    Srai, K.S.3
  • 31
    • 0027252119 scopus 로고
    • Preparation and analysis of isogenic mutants in the transferrin receptor protein genes. tbpA and tbpB, fromNeisseria meningitidis
    • IRWIN S. W., AVERIL N., CHENG C. Y., SCHRYVERS A. B. Preparation and analysis of isogenic mutants in the transferrin receptor protein genes. tbpA and tbpB, fromNeisseria meningitidis. Mol. Microbiol. 8:1993;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
  • 32
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalysed iron transport through the enteric bacterial cell envelope
    • KLEBBA P. E., RUTZ J. M., LIU J., MURPHY C. K. Mechanisms of TonB-catalysed iron transport through the enteric bacterial cell envelope. J. Bioenerg. Biomemb. 25:1993;603-611.
    • (1993) J. Bioenerg. Biomemb. , vol.25 , pp. 603-611
    • Klebba, P.E.1    Rutz, J.M.2    Liu, J.3    Murphy, C.K.4
  • 33
    • 0030943591 scopus 로고    scopus 로고
    • TonB protein appears to transduce energy by shuttleing between the cytoplasmic membrane and the outer membrane inEscherichia coli
    • LETAIN T. E., POSTLE K. TonB protein appears to transduce energy by shuttleing between the cytoplasmic membrane and the outer membrane inEscherichia coli. Mol. Microbiol. 24:1997;271-283.
    • (1997) Mol. Microbiol. , vol.24 , pp. 271-283
    • Letain, T.E.1    Postle, K.2
  • 34
    • 0027375517 scopus 로고
    • Permeability properties of a large gated channel within the ferric enterobactin receptor Fep A
    • 653-10 657
    • LIU J., RUTZ M., FEIX J. B., KLEBBA P. E. Permeability properties of a large gated channel within the ferric enterobactin receptor Fep A. Proc. Natl. Acad. Sci. USA. 90:1993;10 653-10 657.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 10
    • Liu, J.1    Rutz, M.2    Feix, J.B.3    Klebba, P.E.4
  • 35
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signalling across the ligand-gated FhuA receptor: Crystal structures of free and ferrichrome-bound states reveal allosteric changes
    • LOCHER K. P., REES B., KOEBNIK R., MITSCHLER A., MOULINIER L., ROSENBUSCH J. P., MORAS D. Transmembrane signalling across the ligand-gated FhuA receptor: crystal structures of free and ferrichrome-bound states reveal allosteric changes. Cell. 95:1998;771-778.
    • (1998) Cell , vol.95 , pp. 771-778
    • Locher, K.P.1    Rees, B.2    Koebnik, R.3    Mitschler, A.4    Moulinier, L.5    Rosenbusch, J.P.6    Moras, D.7
  • 36
    • 0028073139 scopus 로고    scopus 로고
    • Coordination of iron by the ferric iron binding protein of pathogenic Neisseria is homolgous to the transferrins
    • 769-12 775
    • NORWALK A. J., BURROUGHS-TENCZA S., MEITZNER T. A. Coordination of iron by the ferric iron binding protein of pathogenic Neisseria is homolgous to the transferrins. Biochemistry. 33:1997;12 769-12 775.
    • (1997) Biochemistry , vol.33 , pp. 12
    • Norwalk, A.J.1    Burroughs-Tencza, S.2    Meitzner, T.A.3
  • 37
    • 0030844499 scopus 로고    scopus 로고
    • Sequence analysis of the structural tbpA gene: Protein topology and variable regions within neisserial receptors for transferrin iron acquisition
    • PAJON R., CHINEA G., MARRERO E., GONZALEZ D., GUILLEN G. Sequence analysis of the structural tbpA gene: protein topology and variable regions within neisserial receptors for transferrin iron acquisition. Microb. Pathogen. 23:1997;71-84.
    • (1997) Microb. Pathogen. , vol.23 , pp. 71-84
    • Pajon, R.1    Chinea, G.2    Marrero, E.3    Gonzalez, D.4    Guillen, G.5
  • 38
    • 0022082599 scopus 로고
    • Folding patterns of porin and bacteriorhodopsin
    • PAUL C., ROSENBUSCH J. P. Folding patterns of porin and bacteriorhodopsin. EMBO J. 4:1985;1593-1597.
    • (1985) EMBO J. , vol.4 , pp. 1593-1597
    • Paul, C.1    Rosenbusch, J.P.2
  • 42
    • 0030023410 scopus 로고    scopus 로고
    • Production and characterisation of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors
    • RETZER M. D., KABANI A., BUTTON L. L., YU R. H., SCRYVERS A. B. Production and characterisation of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors. J. Biol. Chem. 271:1996;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    Scryvers, A.B.5
  • 43
    • 85030355994 scopus 로고
    • Infections of the central nervous system
    • Edinburgh: Churchill Livingstone. p. 200-201
    • ROSS P. W., PEUTHERER J. F. Infections of the central nervous system. Clinical Microbiology. 1987;Churchill Livingstone, Edinburgh. p. 200-201.
    • (1987) Clinical Microbiology
    • Ross, P.W.1    Peutherer, J.F.2
  • 44
    • 0345263949 scopus 로고
    • Molecules and life
    • New York: W. H. Freeman & Co. p. 7
    • STRYER L. Molecules and life. Biochemistry. 1988;W. H. Freeman & Co, New York. p. 7.
    • (1988) Biochemistry
    • Stryer, L.1
  • 45
    • 0022497221 scopus 로고
    • The non-random distribution of transferrin iron in fresh human sera
    • VAN-EIJK H. G., VAN-NOORT W. L. The non-random distribution of transferrin iron in fresh human sera. Clin. Chim. Acta. 157:1986;299-303.
    • (1986) Clin. Chim. Acta. , vol.157 , pp. 299-303
    • Van-Eijk, H.G.1    Van-Noort, W.L.2
  • 46
    • 0027944473 scopus 로고
    • Characterisation of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin
    • VONDER HAAR R. A., LEGRAIN M., KOLBE H. V. J., JACOBS E. Characterisation of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin. J. Bacteriol. 176:1994;6207-6213.
    • (1994) J. Bacteriol. , vol.176 , pp. 6207-6213
    • Vonder Haar, R.A.1    Legrain, M.2    Kolbe, H.V.J.3    Jacobs, E.4
  • 47
    • 0018102319 scopus 로고
    • Iron and infection
    • WEINBERG E. D. Iron and infection. Microbiol. Rev. 42:1978;46-66.
    • (1978) Microbiol. Rev. , vol.42 , pp. 46-66
    • Weinberg, E.D.1
  • 48
    • 85030356219 scopus 로고
    • Transferrin structure and function
    • Boca Raton: CRC Press. p. 93-96
    • WELCH S. Transferrin structure and function. Transferrin: The Iron Carrier. 1992;CRC Press, Boca Raton. p. 93-96.
    • (1992) Transferrin: The Iron Carrier
    • Welch, S.1
  • 49
    • 0028132653 scopus 로고
    • Transferrin receptors on ruminant pathogens vary in their interaction with C-lobe and N-lobe of ruminant transferrin
    • YU R. H., SCHRYVERS A. B. Transferrin receptors on ruminant pathogens vary in their interaction with C-lobe and N-lobe of ruminant transferrin. Can. J. Microbiol. 40:1994;532-540.
    • (1994) Can. J. Microbiol , vol.40 , pp. 532-540
    • Yu, R.H.1    Schryvers, A.B.2
  • 50
    • 0021857721 scopus 로고
    • Preparation and properties of a single-sited fragment from the C-terminal domain of human transferrin
    • ZAK O., AISEN P. Preparation and properties of a single-sited fragment from the C-terminal domain of human transferrin. Biochem. Biophys. Acta. 829:1985;348-353.
    • (1985) Biochem. Biophys. Acta , vol.829 , pp. 348-353
    • Zak, O.1    Aisen, P.2


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