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Volumn 26, Issue 1, 1997, Pages 25-35

Energy-dependent changes in the gonococcal transferrin receptor

Author keywords

[No Author keywords available]

Indexed keywords

TRANSFERRIN RECEPTOR;

EID: 0030825114     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1997.5381914.x     Document Type: Article
Times cited : (46)

References (65)
  • 1
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: Structure, mechanism, and evolution
    • Ames, G.F.-L. (1986) Bacterial periplasmic transport systems: structure, mechanism, and evolution. Annu Rev Biochem 55: 397-425.
    • (1986) Annu Rev Biochem , vol.55 , pp. 397-425
    • Ames, G.F.-L.1
  • 2
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson, J.E., Sparling, P.F., and Cornelissen, C.N. (1994) Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization. J Bacterial 176: 3162-3170.
    • (1994) J Bacterial , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 3
    • 0018620068 scopus 로고
    • Removal of iron from human transferrin by Neisseria meningitidis
    • Archibald, F.S., and DeVoe, I.W. (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
  • 4
    • 0023576859 scopus 로고
    • Molecular mechanism of regulation of siderophore-mediated iron assimilation
    • Bagg, A., and Neilands, J.B. (1987) Molecular mechanism of regulation of siderophore-mediated iron assimilation. Microbiol Rev 51: 509-518.
    • (1987) Microbiol Rev , vol.51 , pp. 509-518
    • Bagg, A.1    Neilands, J.B.2
  • 5
    • 0025337694 scopus 로고
    • Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli
    • Bell, P.E., Nau, C.D., Brown, J.T., Konisky, J., and Kadner, R.J. (1990) Genetic suppression demonstrates interaction of TonB protein with outer membrane transport proteins in Escherichia coli. J Bacteriol 172: 3826-3829.
    • (1990) J Bacteriol , vol.172 , pp. 3826-3829
    • Bell, P.E.1    Nau, C.D.2    Brown, J.T.3    Konisky, J.4    Kadner, R.J.5
  • 6
    • 0029163535 scopus 로고
    • Characterization of IbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae
    • Biswas, G.D., and Sparling, P.F. (1995) Characterization of IbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae. Infect Immun 63: 2958-2967.
    • (1995) Infect Immun , vol.63 , pp. 2958-2967
    • Biswas, G.D.1    Sparling, P.F.2
  • 7
    • 0030893908 scopus 로고    scopus 로고
    • Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes
    • Biswas, G.D., Anderson, J.E., and Sparling, P.F. (1997) Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes. Mol Microbiol 24: 169-179.
    • (1997) Mol Microbiol , vol.24 , pp. 169-179
    • Biswas, G.D.1    Anderson, J.E.2    Sparling, P.F.3
  • 9
    • 0026002436 scopus 로고
    • Transport of iron across the outer membrane
    • Braun, V., Gunter, K., and Hantke, K. (1991) Transport of iron across the outer membrane. Biol Met 4: 14-22.
    • (1991) Biol Met , vol.4 , pp. 14-22
    • Braun, V.1    Gunter, K.2    Hantke, K.3
  • 10
    • 0028335766 scopus 로고
    • Energy-coupled transport through the outer membrane of Escherichia coli small deletions in the gating loop convert the FhuA transport protein into a diffusion channel
    • Braun, V., Killmann, H., and Benz, R. (1994) Energy-coupled transport through the outer membrane of Escherichia coli small deletions in the gating loop convert the FhuA transport protein into a diffusion channel. FEBS Lett 346: 59-64.
    • (1994) FEBS Lett , vol.346 , pp. 59-64
    • Braun, V.1    Killmann, H.2    Benz, R.3
  • 11
    • 0027076429 scopus 로고
    • Iron assimilation and storage in prokaryotes
    • Briat, J.-F. (1992) Iron assimilation and storage in prokaryotes. J Gen Microbiol 138: 2475-2483.
    • (1992) J Gen Microbiol , vol.138 , pp. 2475-2483
    • Briat, J.-F.1
  • 12
    • 0013579965 scopus 로고
    • Receptor binding methodology and analysis
    • O'Brian, R.A. (ed.). New York: Marcel Dekker
    • Burt, D.R. (1986) Receptor binding methodology and analysis. In Receptor Binding in Drug Research. O'Brian, R.A. (ed.). New York: Marcel Dekker, pp. 3-29.
    • (1986) Receptor Binding in Drug Research , pp. 3-29
    • Burt, D.R.1
  • 13
    • 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., and Meitzner, T.A. (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    Meitzner, T.A.4
  • 14
    • 0029850699 scopus 로고    scopus 로고
    • Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae
    • Chen, C.-J., Sparling, P.F., Lewis, L.A., Dyer, D.W., and Elkins, C. (1996) Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae. Infect Immun 64: 5008-5014.
    • (1996) Infect Immun , vol.64 , pp. 5008-5014
    • Chen, C.-J.1    Sparling, P.F.2    Lewis, L.A.3    Dyer, D.W.4    Elkins, C.5
  • 15
    • 0028073695 scopus 로고
    • Iron piracy: Acquisition of transferrin-bound iron by bacterial pathogens
    • Cornelissen, C.N., and Sparling, P.F. (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
  • 16
    • 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 Sparling, P.F. (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
  • 17
    • 0026768392 scopus 로고
    • Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors
    • Cornelissen, C.N., Biswas, G.D., Tsai, J., Paruchuri, D.K., Thompson, S.A., and Sparling, P.F. (1992) Gonococcal transferrin-binding protein 1 is required for transferrin utilization and is homologous to TonB-dependent outer membrane receptors. J Bacteriol 174: 5788-5797.
    • (1992) J Bacteriol , vol.174 , pp. 5788-5797
    • Cornelissen, C.N.1    Biswas, G.D.2    Tsai, J.3    Paruchuri, D.K.4    Thompson, S.A.5    Sparling, P.F.6
  • 18
    • 0031035323 scopus 로고    scopus 로고
    • Characterization of the diversity and the transferrin-binding domain of gonococcal transferrin-binding protein 2
    • Cornelissen, C.N., Anderson, J.E., and Sparling, P.F. (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
  • 19
    • 0023193093 scopus 로고
    • Effects of serum carrier proteins on the growth of pathogenic Neisseriae with heme-bound iron
    • Dyer, D.W., West, E.P., and Sparling, P.F. (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
  • 21
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen, S.D., and Schryvers, A.B. (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
  • 23
    • 0015633255 scopus 로고
    • Excretion of enterochelin by exbA and exbB mutants of Escherichia coli
    • Guterman, S.K., and Dann, L. (1973) Excretion of enterochelin by exbA and exbB mutants of Escherichia coli. J Bacteriol 114: 1225-1230.
    • (1973) J Bacteriol , vol.114 , pp. 1225-1230
    • Guterman, S.K.1    Dann, L.2
  • 24
    • 0017258036 scopus 로고
    • Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and φ80 to Escherichia coli
    • Hancock, R.E.W., and Braun, V. (1976) Nature of the energy requirement for the irreversible adsorption of bacteriophages T1 and φ80 to Escherichia coli. J Bacteriol 125: 409-415.
    • (1976) J Bacteriol , vol.125 , pp. 409-415
    • Hancock, R.E.W.1    Braun, V.2
  • 25
    • 0017846753 scopus 로고
    • Functional interaction of the tonA/tonB receptor system in Escherichia coli
    • Hantke, K., and Braun, V. (1978) Functional interaction of the tonA/tonB receptor system in Escherichia coli. J Bacteriol 135: 190-197.
    • (1978) J Bacteriol , vol.135 , pp. 190-197
    • Hantke, K.1    Braun, V.2
  • 26
    • 0023886391 scopus 로고
    • Suppression of the but/B451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli
    • Heller, K.J., Kadner, R.J., and Gunther, K. (1988) Suppression of the but/B451 mutation by mutations in the tonB gene suggests a direct interaction between TonB and TonB-dependent receptor proteins in the outer membrane of Escherichia coli. Gene 64: 147-153.
    • (1988) Gene , vol.64 , pp. 147-153
    • Heller, K.J.1    Kadner, R.J.2    Gunther, K.3
  • 27
    • 0021916461 scopus 로고
    • Haemophilus influenzae can use human transferrin as a sole source for required iron
    • Herrington, D.A., and Sparling, P.F. (1985) Haemophilus influenzae can use human transferrin as a sole source for required iron. Infect Immun 48: 284-251.
    • (1985) Infect Immun , vol.48 , pp. 284-1251
    • Herrington, D.A.1    Sparling, P.F.2
  • 28
    • 0022500907 scopus 로고
    • Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: Isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane
    • Hoffmann, H., Fischer, E., Schwartz, H., and Braun, V. (1986) Overproduction of the proFhuA outer membrane receptor protein of Escherichia coli K-12: isolation, properties, and immunocytochemical localization at the inner side of the cytoplasmic membrane. Arch Microbiol 145: 334-341.
    • (1986) Arch Microbiol , vol.145 , pp. 334-341
    • Hoffmann, H.1    Fischer, E.2    Schwartz, H.3    Braun, V.4
  • 29
    • 0027252119 scopus 로고
    • Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbpA and tbpB, from Neisseria meningitidis
    • Irwin, S.W., Averil, N., Cheng, C.Y., and Schryvers, A.B. (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
  • 30
    • 0025572764 scopus 로고
    • 12 transport in Escherichia coli: Energy coupling between membranes
    • 12 transport in Escherichia coli: energy coupling between membranes. Mol Microbiol 4: 2027-2033.
    • (1990) Mol Microbiol , vol.4 , pp. 2027-2033
    • Kadner, R.J.1
  • 31
  • 32
    • 0027308190 scopus 로고
    • Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli
    • Killmann, H., Benz, R., and Braun, V. (1993) Conversion of the FhuA transport protein into a diffusion channel through the outer membrane of Escherichia coli. EMBO J 12: 3007-3016.
    • (1993) EMBO J , vol.12 , pp. 3007-3016
    • Killmann, H.1    Benz, R.2    Braun, V.3
  • 33
    • 0027729136 scopus 로고
    • Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope
    • Klebba, P.E., Rutz, J.M., Liu, J., and Murphy, C.K. (1993) Mechanisms of TonB-catalyzed iron transport through the enteric bacterial cell envelope. J Bioenerg Biomemb 25: 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
  • 34
    • 0024118398 scopus 로고
    • Specificity of the lactoferrin and transferrin receptors in Neisseria gonorrhoeae
    • Lee, B.C., and Schryvers. A.B. (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
  • 35
    • 0027202149 scopus 로고
    • Cloning and characterization of Neisseria meningitidis genes encoding the transferrin-binding proteins Tbp1 and Tbp2
    • Legrain, M., Mazarin, V., Irwin, S.W., Bouchon, B., Quentin-Millet, M.-J., Jacobs, E., and Schryvers, A.B. (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
  • 36
    • 0031025513 scopus 로고    scopus 로고
    • Molecular characterization of hpuAB, the haemoglobin-haptoglobin-utilization operon of Neisseria meningitidis
    • Lewis, L.A., Gray, E., Wang, Y.-P., Roe, B.A., and Dyer, D.W. (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
  • 37
    • 0027375517 scopus 로고
    • Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA
    • Liu, J., Rutz, J.M., Feix, J.B., and Klebba, P.E. (1993) Permeability properties of a large gated channel within the ferric enterobactin receptor, FepA. Proc Natl Acad Sci USA 90: 10653-10657.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 10653-10657
    • Liu, J.1    Rutz, J.M.2    Feix, J.B.3    Klebba, P.E.4
  • 38
    • 0010571592 scopus 로고
    • Computer analysis of binding data
    • O'Brian, R.A. (ed.). New York: Marcel Dekker
    • Lundeen, J.E., and Gordon, J.H. (1986) Computer analysis of binding data. In Receptor Binding in Drug Research. O'Brian, R.A. (ed.). New York: Marcel Dekker, pp. 31-49.
    • (1986) Receptor Binding in Drug Research , pp. 31-49
    • Lundeen, J.E.1    Gordon, J.H.2
  • 39
    • 0023883113 scopus 로고
    • Iron uptake from lactoferrin and transferrin by Neisseria gonorrhoeae
    • McKenna, W.R., Mickelsen, P.A., Sparling, P.F., and Dyer, D.W. (1988) Iron uptake from lactoferrin and transferrin by Neisseria gonorrhoeae. Infect Immun 56: 785-791.
    • (1988) Infect Immun , vol.56 , pp. 785-791
    • McKenna, W.R.1    Mickelsen, P.A.2    Sparling, P.F.3    Dyer, D.W.4
  • 41
    • 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 Sparling, P.F. (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
  • 42
    • 0020003691 scopus 로고
    • Ability of Neisseria gonorrhoeae, Neisseria meningitidis, and commensal Neisseria species to obtain iron from lactoferrin
    • Mickelsen, P.A., Blackman, E., and Sparling, P.F. (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
  • 43
    • 0029836552 scopus 로고    scopus 로고
    • Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12
    • Moeck, O.S., Tawa, P., Xiang, H., Ismail, A.A., Turnbull, J.L., and Coulton, J.W. (1996) Ligand-induced conformational change in the ferrichrome-iron receptor of Escherichia coli K-12. Mol Microbiol 22: 459-471.
    • (1996) Mol Microbiol , vol.22 , pp. 459-471
    • Moeck, O.S.1    Tawa, P.2    Xiang, H.3    Ismail, A.A.4    Turnbull, J.L.5    Coulton, J.W.6
  • 44
    • 0025345176 scopus 로고
    • Siderophore-independent acquisition of transferrin-bound iron by Haemophilus influenzae type b
    • Morton, D.J., and Williams, P. (1990) Siderophore-independent acquisition of transferrin-bound iron by Haemophilus influenzae type b. J Gen Microbiol 136: 927-933.
    • (1990) J Gen Microbiol , vol.136 , pp. 927-933
    • Morton, D.J.1    Williams, P.2
  • 45
    • 0026662843 scopus 로고
    • Mechanism and regulation of synthesis of aerobactin in Escherichia coli K12 (pColV-K30)
    • Neilands, J.B. (1992) Mechanism and regulation of synthesis of aerobactin in Escherichia coli K12 (pColV-K30). Can J Microbiol 38: 728-733.
    • (1992) Can J Microbiol , vol.38 , pp. 728-733
    • Neilands, J.B.1
  • 46
    • 0024713264 scopus 로고
    • Responses of Haemophilus pleuropneumoniae to iron restriction: Changes in the outer membrane protein profile and the removal of iron from porcine transferrin
    • Niven, D.F., Donga, J., and Archibald, F.S. (1989) Responses of Haemophilus pleuropneumoniae to iron restriction: changes in the outer membrane protein profile and the removal of iron from porcine transferrin. Mol Microbiol 3: 1083-1089.
    • (1989) Mol Microbiol , vol.3 , pp. 1083-1089
    • Niven, D.F.1    Donga, J.2    Archibald, F.S.3
  • 47
    • 0025666854 scopus 로고
    • TonB and the Gram-negative dilemma
    • Postle, K. (1990) TonB and the Gram-negative dilemma. Mol Microbiol 4: 2019-2025.
    • (1990) Mol Microbiol , vol.4 , pp. 2019-2025
    • Postle, K.1
  • 48
    • 0027752437 scopus 로고
    • TonB protein and energy transduction between membranes
    • Postle, K. (1993) TonB protein and energy transduction between membranes. J Bioenerg Biomemb 25: 591-601.
    • (1993) J Bioenerg Biomemb , vol.25 , pp. 591-601
    • Postle, K.1
  • 49
    • 0021592032 scopus 로고
    • In vitro insertional mutagenesis with a selectable DNA fragment
    • Prentki, P., and Krisch, H.M. (1984) In vitro insertional mutagenesis with a selectable DNA fragment. Gene 29: 303-313.
    • (1984) Gene , vol.29 , pp. 303-313
    • Prentki, P.1    Krisch, H.M.2
  • 50
  • 51
    • 0025271609 scopus 로고
    • Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants
    • Sauer, M., Hantke, K., and Braun, V. (1990) Sequence of the fhuE outer-membrane receptor gene of Escherichia coli K12 and properties of mutants. Mol Microbiol 4: 427-437.
    • (1990) Mol Microbiol , vol.4 , pp. 427-437
    • Sauer, M.1    Hantke, K.2    Braun, V.3
  • 52
    • 0024676062 scopus 로고
    • Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane
    • Schoffler, H., and Braun, V. (1989) Transport across the outer membrane of Escherichia coli K12 via the FhuA receptor is regulated by the TonB protein of the cytoplasmic membrane. Mol Gen Genet 217: 378-383.
    • (1989) Mol Gen Genet , vol.217 , pp. 378-383
    • Schoffler, H.1    Braun, V.2
  • 53
    • 0023218137 scopus 로고
    • Nucleotide sequence of the colicin B activity gene cba: Consensus peptapeptide among TonB-dependent colicins and receptors
    • Schramm, E., Mende, J., Braun, V., and Kamp, R.M. (1987) Nucleotide sequence of the colicin B activity gene cba: consensus peptapeptide among TonB-dependent colicins and receptors. J Bacteriol 169: 3350-3357.
    • (1987) J Bacteriol , vol.169 , pp. 3350-3357
    • Schramm, E.1    Mende, J.2    Braun, V.3    Kamp, R.M.4
  • 54
    • 0024633541 scopus 로고
    • Comparative analysis of the transferrin and lactoferrin binding proteins in the family Neisseriaceae
    • Schryvers, A.B., and Lee, B.C. (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
  • 55
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A.B., and Morris, L.J. (1988a) 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
  • 56
    • 0023974498 scopus 로고
    • Identification and characterization of the transferrin receptor from Neisseria meningitidis
    • Schryvers, A.B., and Morris, L.J. (1988b) 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
  • 57
    • 0001071291 scopus 로고
    • Shuttle mutagenesis: A method of introducing transposons into transformable organisms
    • Hollaender, A., and Setlow, J.K. (eds). New York: Plenum Press
    • Seifert, H.S., So, M., and Heffron, F. (1986) Shuttle mutagenesis: a method of introducing transposons into transformable organisms. In Genetic Engineering, Principles and Methods. Hollaender, A., and Setlow, J.K. (eds). New York: Plenum Press, pp. 123-134.
    • (1986) Genetic Engineering, Principles and Methods , pp. 123-134
    • Seifert, H.S.1    So, M.2    Heffron, F.3
  • 58
    • 0020045384 scopus 로고
    • Expression of a high-affinity mechanism for acquisition of transferrin iron by Neisseria meningitidis
    • Simonson, C., Brener, D., and DeVoe, I.W. (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
  • 59
    • 0027282061 scopus 로고
    • Energy transduction between membranes: TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA
    • Skare, J.T., Ahmer, B.M.M., Seachord, C.L., Darveau, R.P., and Postle, K. (1993) Energy transduction between membranes: TonB, a cytoplasmic membrane protein, can be chemically cross-linked in vivo to the outer membrane receptor FepA. J Biol Chem 268: 16302-16308.
    • (1993) J Biol Chem , vol.268 , pp. 16302-16308
    • Skare, J.T.1    Ahmer, B.M.M.2    Seachord, C.L.3    Darveau, R.P.4    Postle, K.5
  • 60
    • 0031018882 scopus 로고    scopus 로고
    • Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in Neisseriae
    • Stojilkovic, I., and Srinivasan, N. (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
    • Stojilkovic, I.1    Srinivasan, N.2
  • 61
    • 33847670407 scopus 로고
    • Ferrozine - A new spectrophotometric reagent for iron
    • Stookey, L. L. (1970) Ferrozine - a new spectrophotometric reagent for iron. Anal Chem 42: 779-781.
    • (1970) Anal Chem , vol.42 , pp. 779-781
    • Stookey, L.L.1
  • 62
    • 0023787101 scopus 로고
    • Loss of transferrin receptor activity in Neisseria meningitidis correlates with inability to use transferrin as an iron source
    • Tsai, J., Dyer, D.W., and Sparling, P.F. (1988) Loss of transferrin receptor activity in Neisseria meningitidis correlates with inability to use transferrin as an iron source. Infect Immun 56: 3132-3138.
    • (1988) Infect Immun , vol.56 , pp. 3132-3138
    • Tsai, J.1    Dyer, D.W.2    Sparling, P.F.3
  • 63
    • 0027944473 scopus 로고
    • Characterization of a highly structured domain in Tbp2 from Neisseria meningitidis involved in binding to human transferrin
    • Vender Haar, R.A., Legrain, M., Kolbe, H.V.J., and Jacobs, E. (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
    • Vender Haar, R.A.1    Legrain, M.2    Kolbe, H.V.J.3    Jacobs, E.4
  • 64
    • 0022005202 scopus 로고
    • Response of Neisseria gonorrhoeae to iron limitation: Alterations in expression of membrane proteins without apparent siderophore production
    • West, S.E.H., and Sparling, P.F. (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.H.1    Sparling, P.F.2
  • 65
    • 0023252285 scopus 로고
    • Aerobactin utilization by Neisseria gonorrhoeae and cloning of a genomic DNA fragment that complements Escherichia coli fhuB mutations
    • West, S.E.H., and Sparling, P.F. (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.H.1    Sparling, P.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.