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Volumn 27, Issue 3, 1998, Pages 599-610

Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN RECEPTOR;

EID: 0031984119     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1998.00707.x     Document Type: Article
Times cited : (65)

References (53)
  • 1
    • 0023601678 scopus 로고
    • Whole-cell ELISA for typing of Neisseria meningitidis with monoclonal antibodies
    • Abdillahi, H., and Poolman, J.T. (1987) Whole-cell ELISA for typing of Neisseria meningitidis with monoclonal antibodies. FEMS Microbiol Lett 48: 367-371.
    • (1987) FEMS Microbiol Lett , vol.48 , pp. 367-371
    • Abdillahi, H.1    Poolman, J.T.2
  • 2
    • 0029936842 scopus 로고    scopus 로고
    • The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron
    • Adhikari, P., Berish, S.A., Nowalk, A.J., Veraldi, K.L., Morde, S.A., and Mietzner, T.A. (1996) The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron. J Bacteriol 178: 2145-2149.
    • (1996) J Bacteriol , vol.178 , pp. 2145-2149
    • Adhikari, P.1    Berish, S.A.2    Nowalk, A.J.3    Veraldi, K.L.4    Morde, S.A.5    Mietzner, T.A.6
  • 3
    • 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 Borriello, S.P. (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
  • 4
    • 0028332807 scopus 로고
    • Immune responses in humans and animals to meningococcal transferrin-binding proteins: Implications for vaccine design
    • Ala'Aldeen, D.A., Stevenson, P., Griffiths, E., Gorringe, A.R., Irons, L.I., Robinson, A., et al. (1994) Immune responses in humans and animals to meningococcal transferrin-binding proteins: implications for vaccine design. Infect Immun 62: 2984-2990.
    • (1994) Infect Immun , vol.62 , pp. 2984-2990
    • Ala'Aldeen, D.A.1    Stevenson, P.2    Griffiths, E.3    Gorringe, A.R.4    Irons, L.I.5    Robinson, A.6
  • 5
    • 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 Bacteriol 176: 3162-3170.
    • (1994) J Bacteriol , vol.176 , pp. 3162-3170
    • Anderson, J.E.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 7
    • 0023664923 scopus 로고
    • Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
    • Bagg, A., and Neilands, J.B. (1987) Ferric uptake regulation protein acts as a repressor, employing iron (II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli. Biochemistry 26: 5471-5477.
    • (1987) Biochemistry , vol.26 , pp. 5471-5477
    • Bagg, A.1    Neilands, J.B.2
  • 8
    • 0027440781 scopus 로고
    • Identification and cloning of a furhomolog from Neisseria gonorrhoeae
    • Berish, S.A., Subbarao, S., Chen, C.-Y., Trees, D.L., and Morse, S.A. (1993) Identification and cloning of a furhomolog from Neisseria gonorrhoeae. Infect Immun 61: 4599-4606.
    • (1993) Infect Immun , vol.61 , pp. 4599-4606
    • Berish, S.A.1    Subbarao, S.2    Chen, C.-Y.3    Trees, D.L.4    Morse, S.A.5
  • 9
    • 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
  • 10
    • 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
  • 11
    • 0029587287 scopus 로고
    • Biochemical analysis of lactoferrin receptors in the Neisseriaceae: Identification of a second bacterial lactoferrin receptor protein
    • Bonnah, R.A., Yu, R.-H., and Schryvers, A.B. (1995) Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein. Microb Pathogen 19: 285-297.
    • (1995) Microb Pathogen , vol.19 , pp. 285-297
    • Bonnah, R.A.1    Yu, R.-H.2    Schryvers, A.B.3
  • 12
    • 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 Mietzner, 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    Mietzner, T.A.4
  • 13
    • 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
  • 14
    • 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
  • 15
    • 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
  • 16
    • 0029885361 scopus 로고    scopus 로고
    • In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane
    • de Cock, H., van Blokland, S., and Tommassen, J. (1996) In vitro insertion and assembly of outer membrane protein PhoE of Escherichia coli K-12 into the outer membrane. J Biol Chem 271: 12885-12890.
    • (1996) J Biol Chem , vol.271 , pp. 12885-12890
    • De Cock, H.1    Van Blokland, S.2    Tommassen, J.3
  • 17
    • 0029783958 scopus 로고    scopus 로고
    • Analysis of fur binding to operator sequences within the Neisseria gonorrhoeae fbpA promoter
    • Desai, P.K., Angerer, A., and Genco, C.A. (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.K.1    Angerer, A.2    Genco, C.A.3
  • 19
    • 0025856968 scopus 로고
    • Isolation and characterization of a mutant of Neisseria gonorrhoeae that is defective in the uptake of iron from transferrin and hemoglobin and is avirulent in mouse subcutaneous chambers
    • Genco, C.A., Chen, C.Y., Arko, R.J., Kapczynski, D.R., and Morse, S.A. (1991) Isolation and characterization of a mutant of Neisseria gonorrhoeae that is defective in the uptake of iron from transferrin and hemoglobin and is avirulent in mouse subcutaneous chambers. J Gen Microbiol 137: 1313-1321.
    • (1991) J Gen Microbiol , vol.137 , pp. 1313-1321
    • Genco, C.A.1    Chen, C.Y.2    Arko, R.J.3    Kapczynski, D.R.4    Morse, S.A.5
  • 20
    • 0014531759 scopus 로고
    • Human immunity to the meningococcus. I. The role of antibodies
    • Goldschneider, I., Gotschlich, E.C., and Artenstein, M.S. (1969) Human immunity to the meningococcus. I. The role of antibodies. J Exp Med 129: 1307-1326.
    • (1969) J Exp Med , vol.129 , pp. 1307-1326
    • Goldschneider, I.1    Gotschlich, E.C.2    Artenstein, M.S.3
  • 21
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen, S.S., 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.S.1    Schryvers, A.B.2
  • 22
    • 14444277568 scopus 로고    scopus 로고
    • Lactoferrin and its receptor(s): Modulators of inflammation?
    • Laboratoire de Chimie Biologique. Lille: Université des Sciences et Technologies de Lille, Centre National de la Recherche Scientifique
    • Gschwentner, C., Lassman, H., and Huettinger, M. (1997) Lactoferrin and its receptor(s): modulators of inflammation? Abstracts of the Third International Conference on Lactoferrin. Laboratoire de Chimie Biologique. Lille: Université des Sciences et Technologies de Lille, Centre National de la Recherche Scientifique, p. 68.
    • (1997) Abstracts of the Third International Conference on Lactoferrin , pp. 68
    • Gschwentner, C.1    Lassman, H.2    Huettinger, M.3
  • 23
    • 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.A., Chen, 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.A.2    Chen, C.Y.3    Schryvers, A.B.4
  • 24
    • 0027376664 scopus 로고
    • Cloning and molecular analysis of the galE gene of Neisseria meningitidis and its role in lipopolysaccharide biosynthesis
    • Jennings, M.P., van der Ley, P., Wilks, K.E., Maskell, D.J., Poolman, J.T., and Moxon, E.R. (1993) Cloning and molecular analysis of the galE gene of Neisseria meningitidis and its role in lipopolysaccharide biosynthesis. Mol Microbiol 10: 361-369.
    • (1993) Mol Microbiol , vol.10 , pp. 361-369
    • Jennings, M.P.1    Van Der Ley, P.2    Wilks, K.E.3    Maskell, D.J.4    Poolman, J.T.5    Moxon, E.R.6
  • 25
    • 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., et al. (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
  • 26
    • 0029379719 scopus 로고
    • Production of lipidated meningococcal transferrin binding protein 2 in Escherichia coli
    • Legrain, M., Speck, D., and Jacobs, E. (1995) Production of lipidated meningococcal transferrin binding protein 2 in Escherichia coli. Protein Expression Purif 6: 570-578.
    • (1995) Protein Expression Purif , vol.6 , pp. 570-578
    • Legrain, M.1    Speck, D.2    Jacobs, E.3
  • 27
    • 0031025513 scopus 로고    scopus 로고
    • Molecular characterization of hpuAB, the hemoglobin-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 hemoglobin-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
  • 28
    • 0016841078 scopus 로고
    • Electrophoretic resolution of the 'major outer membrane protein' of Eschericha coli K12 into four bands
    • Lugtenberg, B., Meyers, J., Peters, R., van der Hoek, P., and van Alphen, L. (1975) Electrophoretic resolution of the 'major outer membrane protein' of Eschericha coli K12 into four bands. FEBS Lett 58: 254-258.
    • (1975) FEBS Lett , vol.58 , pp. 254-258
    • Lugtenberg, B.1    Meyers, J.2    Peters, R.3    Van Der Hoek, P.4    Van Alphen, L.5
  • 29
    • 0009665799 scopus 로고
    • An iron-binding protein common to many external secretions
    • Masson, P.L., Heremans, J.F., and Dive, C.H. (1966) An iron-binding protein common to many external secretions. Clin Chim Acta 14: 735-739.
    • (1966) Clin Chim Acta , vol.14 , pp. 735-739
    • Masson, P.L.1    Heremans, J.F.2    Dive, C.H.3
  • 30
    • 0029032190 scopus 로고
    • Diversity of the transferrin-binding protein Tbp2 of Neisseria meningitidis
    • Mazarin, V., Rokbi, B., and Quentin-Millet, M.-J. (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
  • 31
    • 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
  • 32
    • 0019348762 scopus 로고
    • Microbial iron compounds
    • Neilands, J.B. (1981) Microbial iron compounds. Annu Rev Biochem 50: 715-731.
    • (1981) Annu Rev Biochem , vol.50 , pp. 715-731
    • Neilands, J.B.1
  • 33
    • 0025145454 scopus 로고
    • Monoclonal antibodies against the 70-kilodalton iron-regulated protein of Neisseria meningitidis are bactericidal and strain specific
    • Pettersson, A., Kuipers, B., Pelzer, M., Verhagen, E., Tiesjema, R.H., Tommassen, J., et al. (1990) Monoclonal antibodies against the 70-kilodalton iron-regulated protein of Neisseria meningitidis are bactericidal and strain specific. Infect Immun 58: 3036-3041.
    • (1990) Infect Immun , vol.58 , pp. 3036-3041
    • Pettersson, A.1    Kuipers, B.2    Pelzer, M.3    Verhagen, E.4    Tiesjema, R.H.5    Tommassen, J.6
  • 34
    • 0027364814 scopus 로고
    • Molecular characterization of the 98-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis
    • Pettersson, A., van der Ley, P., Poolman, J.T., and Tommassen, J. (1993) Molecular characterization of the 98-kilodalton iron-regulated outer membrane protein of Neisseria meningitidis. Infect Immun 61: 4724-4733.
    • (1993) Infect Immun , vol.61 , pp. 4724-4733
    • Pettersson, A.1    Van Der Ley, P.2    Poolman, J.T.3    Tommassen, J.4
  • 35
    • 0028345373 scopus 로고
    • Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor
    • Pettersson, A., Maas, A., and Tommassen, J. (1994a) Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor. J Bacteriol 176: 1764-1766.
    • (1994) J Bacteriol , vol.176 , pp. 1764-1766
    • Pettersson, A.1    Maas, A.2    Tommassen, J.3
  • 36
    • 0028641362 scopus 로고
    • Molecular characterization of the structural gene for the lactoferrin receptor of the meningococcal strain H44/76
    • Pettersson, A., Klarenbeek, V., van Deurzen, J., Poolman, J.T., and Tommassen, J. (1994b) Molecular characterization of the structural gene for the lactoferrin receptor of the meningococcal strain H44/76. Microb Pathogen 17: 395-408.
    • (1994) Microb Pathogen , vol.17 , pp. 395-408
    • Pettersson, A.1    Klarenbeek, V.2    Van Deurzen, J.3    Poolman, J.T.4    Tommassen, J.5
  • 37
    • 0018081614 scopus 로고
    • Immunochemical characterization of outer membrane complexes from Neisseria meningitidis by the SDS-polyacrylamide-gel-electrophoresis-immunoperoxidase technique (SGIP)
    • Poolman, J.T., Hopman, C.T.P., and Zanen, H.C. (1978) Immunochemical characterization of outer membrane complexes from Neisseria meningitidis by the SDS-polyacrylamide-gel-electrophoresis-immunoperoxidase technique (SGIP). FEMS Microbiol Lett 4: 245-248.
    • (1978) FEMS Microbiol Lett , vol.4 , pp. 245-248
    • Poolman, J.T.1    Hopman, C.T.P.2    Zanen, H.C.3
  • 38
    • 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
  • 39
    • 0027233438 scopus 로고
    • Identification of two major families of transferrin receptors among Neisseria meningitidis strains based on antigenic and genomic features
    • Rokbi, B., Mazarin, V., Maitre-Wilmotte, G., and Quentin-Millet, M.-J. (1993) Identification of two major families of transferrin receptors among Neisseria meningitidis strains based on antigenic and genomic features. FEMS Microbiol Lett 110: 51-58.
    • (1993) FEMS Microbiol Lett , vol.110 , pp. 51-58
    • Rokbi, B.1    Mazarin, V.2    Maitre-Wilmotte, G.3    Quentin-Millet, M.-J.4
  • 40
    • 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., Mignon, M., Maitre-Wilmotte, G., Lissolo, L., Danve, B., Caugant, D.A., et al. (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
  • 42
    • 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
  • 43
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A.B., and Morris, L.J. (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
  • 44
    • 0031018882 scopus 로고    scopus 로고
    • Neisseria meningitidis tonB, exbB, and exbD genes: Ton-dependent utilization of protein-bound iron in Neisseriae
    • Stojiljkovic, 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
    • Stojiljkovic, I.1    Srinivasan, N.2
  • 45
    • 0028968322 scopus 로고
    • The Neisseria meningitidis haemoglobin receptor: Its role in iron utilization and virulence
    • Stojiljkovic, I., Hwa, V., de Saint Martin, L., O'Gaora, P., Nassif, X., and So, M. (1995) The Neisseria meningitidis haemoglobin receptor: its role in iron utilization and virulence. Mol Microbiol 15: 531-541.
    • (1995) Mol Microbiol , vol.15 , pp. 531-541
    • Stojiljkovic, I.1    Hwa, V.2    De Saint Martin, L.3    O'Gaora, P.4    Nassif, X.5    So, M.6
  • 46
    • 0028308565 scopus 로고
    • Identification and cloning of a fur homologue from Neisseria meningitidis
    • Thomas, C.E., and Sparling, P.F. (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
  • 47
    • 8944231163 scopus 로고    scopus 로고
    • Isolation of a fur mutant in Neisseria gonorrhoeae
    • Thomas, C.E., and Sparling, P.F. (1996) Isolation of a fur mutant in Neisseria gonorrhoeae. J Bacteriol 178: 4224-4232.
    • (1996) J Bacteriol , vol.178 , pp. 4224-4232
    • Thomas, C.E.1    Sparling, P.F.2
  • 48
    • 0028875343 scopus 로고
    • Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial polysaccharide, but differ in their susceptibilities towards tryptic proteolysis
    • van Berkel, P.H.C., Geerts, M.E.J., van Veen, H.A., Kooiman, P.M., Pieper, F.R., de Boer, H.A., et al. (1995) Glycosylated and unglycosylated human lactoferrins both bind iron and show identical affinities towards human lysozyme and bacterial polysaccharide, but differ in their susceptibilities towards tryptic proteolysis. Biochem J 312: 107-114.
    • (1995) Biochem J , vol.312 , pp. 107-114
    • Van Berkel, P.H.C.1    Geerts, M.E.J.2    Van Veen, H.A.3    Kooiman, P.M.4    Pieper, F.R.5    De Boer, H.A.6
  • 49
    • 0026717525 scopus 로고
    • Construction of a multivalent meningococcal strain based on the class 1 outer membrane protein
    • van der Ley, P., and Poolman, J.T. (1992) Construction of a multivalent meningococcal strain based on the class 1 outer membrane protein. Infect Immun 60: 3156-3161.
    • (1992) Infect Immun , vol.60 , pp. 3156-3161
    • Van Der Ley, P.1    Poolman, J.T.2
  • 51
    • 0027944473 scopus 로고
    • Characterization 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., 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
    • Vonder Haar, R.A.1    Legrain, M.2    Kolbe, H.V.J.3    Jacobs, E.4
  • 52
    • 0024393453 scopus 로고
    • The structure of signal peptides from bacterial lipoproteins
    • von Heijne, G. (1989) The structure of signal peptides from bacterial lipoproteins. Protein Eng 2: 531-534.
    • (1989) Protein Eng , vol.2 , pp. 531-534
    • Von Heijne, G.1
  • 53
    • 0021081961 scopus 로고
    • Yeast RNA polymerase Il genes: Isolation with antibody probes
    • Young, R.A., and Davis, R.W. (1983) Yeast RNA polymerase Il genes: isolation with antibody probes. Science 222: 778-782.
    • (1983) Science , vol.222 , pp. 778-782
    • Young, R.A.1    Davis, R.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.