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Volumn 32, Issue 6, 1999, Pages 1117-1123

Iron acquisition systems in the pathogenic Neisseria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL VACCINE; HAPTOGLOBIN; HEME; HEMOGLOBIN; IRON; LACTOFERRIN; MEMBRANE RECEPTOR; RECEPTOR PROTEIN; SIDEROPHORE; TRANSFERRIN;

EID: 0033064808     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01411.x     Document Type: Review
Times cited : (210)

References (41)
  • 1
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson, J.A., 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.A.1    Sparling, P.F.2    Cornelissen, C.N.3
  • 2
    • 0013576948 scopus 로고    scopus 로고
    • A common deletion in Lf gonococci
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Anderson, J.E., Biswas, G.D., and Sparling, P.F. (1998) A common deletion in Lf gonococci. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 328
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 328
    • Anderson, J.E.1    Biswas, G.D.2    Sparling, P.F.3
  • 3
    • 0031747819 scopus 로고    scopus 로고
    • Preparation and characterization of Neisseria meningitidis mutants deficient in the production of the human lactoferrin binding proteins LbpA and LbpB
    • Bonnah, R.A., and Schryvers, A.B. (1998) Preparation and characterization of Neisseria meningitidis mutants deficient in the 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
  • 4
    • 0002200877 scopus 로고
    • Disorders of iron metabolism
    • Handlin, R.I., Lux, S.E., and Stossel, T.P. (eds). Phildalephia: J.B. Lippincott
    • Bridges, K.R., and Seligman, P.A. (1995) Disorders of iron metabolism. In Blood, Principles and Practice of Hematology. Handlin, R.I., Lux, S.E., and Stossel, T.P. (eds). Phildalephia: J.B. Lippincott, p. 1433
    • (1995) Blood, Principles and Practice of Hematology , pp. 1433
    • Bridges, K.R.1    Seligman, P.A.2
  • 7
    • 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
  • 8
    • 0031911354 scopus 로고    scopus 로고
    • Phase variation of hemoglobin utilization in Neisseria gonorrhoeae
    • Chen, C.J., Elkins, C., and Sparling, P.F. (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
  • 9
    • 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
  • 10
    • 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., Kelley, M., Hobbs, M.M., Anderson, J.E., Cannon, J.G., Cohen, M.S., et al. (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
  • 11
    • 0002323543 scopus 로고    scopus 로고
    • Safety and immunogenicity of a Neisseria meningitidis group B transferrin binding protein vaccine in adults
    • Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Danve, B., Lissolo, L., Guinet, F., Boutry, E., Speck, D., Cadoz, M., et al. (1998) Safety and immunogenicity of a Neisseria meningitidis group B transferrin binding protein vaccine in adults. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 53.
    • (1998) Abstract 11th Int. Path. , pp. 53
    • Danve, B.1    Lissolo, L.2    Guinet, F.3    Boutry, E.4    Speck, D.5    Cadoz, M.6
  • 12
    • 0028822737 scopus 로고
    • Binding and accumulation of hemin in Neisseria gonorrhoeae
    • Desai, P.J., Nzeribe, R., and Genco, C.A. (1995) Binding and accumulation of hemin in Neisseria gonorrhoeae. Infect Immun 63: 4634-4641
    • (1995) Infect Immun , vol.63 , pp. 4634-4641
    • Desai, P.J.1    Nzeribe, R.2    Genco, C.A.3
  • 13
    • 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
  • 14
    • 0032545324 scopus 로고    scopus 로고
    • Siderophore-Mediated iron transport: Crystal structure of FhuA with bound lipopolysaccharide
    • Ferguson, A.D., Hofmann, E., Coulton, J.W., Diederichs, K., and Welte, W. (1998) Siderophore-mediated iron transport: crystal structure of FhuA with bound lipopolysaccharide. Science 282: 2215-2220
    • (1998) Science , vol.282 , pp. 2215-2220
    • Ferguson, A.D.1    Hofmann, E.2    Coulton, J.W.3    Diederichs, K.4    Welte, W.5
  • 15
    • 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)
    • Gómez, J.A., Criado, M.T., and Ferreirós, C.M. (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
    • Gómez, J.A.1    Criado, M.T.2    Ferreirós, C.M.3
  • 16
    • 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
  • 17
    • 0027252119 scopus 로고
    • Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbp1 and tbp2, from Neisseria meningitidis
    • Irwin, S.W., Averill, N., Cheng, C.Y., and Schryvers, A.B. (1993) Preparation and analysis of isogenic mutants in the transferrin receptor protein genes, tbp1 and tbp2, from Neisseria meningitidis. Mol Microbiol 8: 1125-1133
    • (1993) Mol Microbiol , vol.8 , pp. 1125-1133
    • Irwin, S.W.1    Averill, N.2    Cheng, C.Y.3    Schryvers, A.B.4
  • 18
    • 0031948656 scopus 로고    scopus 로고
    • A Neisseria meningitidis fbpABC mutant is incapable of using nonheme iron for growth
    • Khun, H.H., Kirby, S.D., and Lee, B.C. (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
  • 19
    • 0027202149 scopus 로고
    • Molecular cloning and characterization of Neisseria meningitidis genes encoding the transferrin binding proteins Tbp1 and Tbp2
    • Legrain, M., Jacobs, E., Irwin, S.W., Schryvers, A.B., and Quentin-Millet, M.J. (1993) Molecular 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    Jacobs, E.2    Irwin, S.W.3    Schryvers, A.B.4    Quentin-Millet, M.J.5
  • 20
    • 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
  • 21
    • 0013577108 scopus 로고    scopus 로고
    • Phase variation between HpuAB and HmbR, two meningococcal hemoglobin receptors
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Lewis, L.A., Gipson, M., Hartman, K., Ownbey, T., Vaughn, J., and Dyer, D.W. (1998) Phase variation between HpuAB and HmbR, two meningococcal hemoglobin receptors. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 336
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 336
    • Lewis, L.A.1    Gipson, M.2    Hartman, K.3    Ownbey, T.4    Vaughn, J.5    Dyer, D.W.6
  • 22
    • 0002023516 scopus 로고
    • Preliminary biochemical characterization of transferrin binding proteins from Neisseria meningitidis
    • Conde-Glez, C.J., Morse, S., Rice, P., Sparling, F., and Calderon, E. (eds). Mexico: Publications Office INSP
    • Lissolo, L., Dumas, P., Maitre, G., and Quentin-Millet, M.J. (1994) Preliminary biochemical characterization of transferrin binding proteins from Neisseria meningitidis. In Pathobiology and Immunobiology of Neisseriaceae. Conde-Glez, C.J., Morse, S., Rice, P., Sparling, F., and Calderon, E. (eds). Mexico: Publications Office INSP, pp. 399-405
    • (1994) Pathobiology and Immunobiology of Neisseriaceae , pp. 399-405
    • Lissolo, L.1    Dumas, P.2    Maitre, G.3    Quentin-Millet, M.J.4
  • 23
    • 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., Maitre-Wilmotte, G., Dumas, P., Mignon, M., Danve, B., and Quentin-Millet, M.-J. (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
  • 24
    • 0032414254 scopus 로고    scopus 로고
    • Transmembrane signaling across the ligand-gated FhuA receptor: Crystal structure of free and ferrichrome-bound states reveal allosteric changes
    • Locher, K.P., Rees, B., Koebnik, R., Mitschler, A., Moulinier, L., Rosenbusch, J.P., et al. (1998) Transmembrane signaling across the ligand-gated FhuA receptor: crystal structure of free and ferrichrome-bound states reveal allosteric changes. Cell 95: 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
  • 25
    • 0013606423 scopus 로고    scopus 로고
    • Selectivity of ferric enterobactin binding and transport in Gram-negative bacteria
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Newton, S.M.C., Thulasuraman, P., Carson, S.B., Sparling, P.F., and Klebba, P.E. (1998) Selectivity of ferric enterobactin binding and transport in Gram-negative bacteria. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 333
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 333
    • Newton, S.M.C.1    Thulasuraman, P.2    Carson, S.B.3    Sparling, P.F.4    Klebba, P.E.5
  • 26
    • 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. (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
  • 27
    • 0031984119 scopus 로고    scopus 로고
    • Molecular characterization of LbpB, the second lactoferrin-binding protein of Neisseria meningitidis
    • Pettersson, A., Prinz, T., Umar, A., vanderBlezen, J., and Tommassen, J. (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    Vanderblezen, J.4    Tommassen, J.5
  • 28
    • 0013612353 scopus 로고    scopus 로고
    • Structural characterization of the lactoferrin receptor from Neisseria meningitidis
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Prinz, T., Meyer, M., Pettersson, A., Van der Biezen, J., and Tommassen, J. (1998) Structural characterization of the lactoferrin receptor from Neisseria meningitidis. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 330
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 330
    • Prinz, T.1    Meyer, M.2    Pettersson, A.3    Van der Biezen, J.4    Tommassen, J.5
  • 29
    • 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., Yu, R.-H., Zhang, Y., Gonzalez, G.C., and Schryvers, A.B. (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.-H.2    Zhang, Y.3    Gonzalez, G.C.4    Schryvers, A.B.5
  • 30
    • 0032954031 scopus 로고    scopus 로고
    • Identification of transferrin binding protein binding sequences in human transferrin
    • Retzer, M.D., Yu, R.-H., and Schryvers, A.B. (1999) Identification of transferrin binding protein binding sequences in human transferrin. Mol Microbiol 32: 111-122
    • (1999) Mol Microbiol , vol.32 , pp. 111-122
    • Retzer, M.D.1    Yu, R.-H.2    Schryvers, A.B.3
  • 31
    • 0031032906 scopus 로고    scopus 로고
    • Evaluation of recombinant transferrin binding protein B variants from Neisseria meningitidis for their ability of 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 of 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
  • 32
    • 0002253278 scopus 로고
    • Disorders of heme production and catabolism
    • Handlin, R.I., Lux, S.E., and Stossel, T.P. (eds). Philadelphia: J.B. Lippincott
    • Sassa, S., and Kappas, A. (1995) Disorders of heme production and catabolism. In Blood, Principles and Practice of Hematology. Handlin, R.I., Lux, S.E., and Stossel, T.P. (eds). Philadelphia: J.B. Lippincott, pp. 1473
    • (1995) Blood, Principles and Practice of Hematology , pp. 1473
    • Sassa, S.1    Kappas, A.2
  • 33
    • 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
  • 35
    • 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 Hantke, K. (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
  • 36
    • 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
  • 37
    • 0029765788 scopus 로고    scopus 로고
    • HmbR outer membrane proteins of pathogenic Neisseriae: Iron-regulated, hemoglobin binding proteins with high degree of primary structure conservation
    • Stojiljkovic, I., Larson, J., Hwa, V., Anic, S., and So, M. (1996) HmbR outer membrane proteins of pathogenic Neisseriae: iron-regulated, hemoglobin binding proteins with high degree of primary structure conservation. J Bacteriol 178: 3341-3352
    • (1996) J Bacteriol , vol.178 , pp. 3341-3352
    • Stojiljkovic, I.1    Larson, J.2    Hwa, V.3    Anic, S.4    So, M.5
  • 38
    • 0013603535 scopus 로고    scopus 로고
    • Hemoglobin utilization by Neisseria meningitidis
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Stojiljkovic, I., Baer, M.T., and Richardson, A.R. (1998) Hemoglobin utilization by Neisseria meningitidis. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 52
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 52
    • Stojiljkovic, I.1    Baer, M.T.2    Richardson, A.R.3
  • 39
    • 0013576950 scopus 로고    scopus 로고
    • Identification and analysis of three previously uncharacterized putative TonB-dependant outer membrane proteins in pathogenic Neisseriae
    • Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K.
    • Turner, P.C., Ala'Aldeen, D.A.A., Kizil, G., Thomas, C.E., Elkins, C., and Sparling, P.F. (1998a) Identification and analysis of three previously uncharacterized putative TonB-dependant outer membrane proteins in pathogenic Neisseriae. In Abstract 11th Int. Path. Neisseria Conference. Nassif, X., Quentin-Millet, M.-J., and Taha, M.K. (eds). Paris: Editions E.D.K., p. 341
    • (1998) Abstract 11th Int. Path. Neisseria Conference , pp. 341
    • Turner, P.C.1    Ala'Aldeen, D.A.A.2    Kizil, G.3    Thomas, C.E.4    Elkins, C.5    Sparling, P.F.6
  • 40
    • 0032435637 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as a heme source but fail to grow within epithelial cells
    • Turner, P.C., Thomas, C.E., Elkins, C., Clary, S., and Sparling, P.F. (1998b) Neisseria gonorrhoeae heme biosynthetic mutants utilize heme and hemoglobin as a heme source but fail to grow within epithelial cells. Infect Immun 66: 5215-5223
    • (1998) Infect Immun , vol.66 , pp. 5215-5223
    • Turner, P.C.1    Thomas, C.E.2    Elkins, C.3    Clary, S.4    Sparling, P.F.5
  • 41
    • 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


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