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Volumn 79, Issue 1, 2011, Pages 267-278

The fbpABC operon is required for ton-independent utilization of xenosiderophores by neisseria gonorrhoeae strain FA19

Author keywords

[No Author keywords available]

Indexed keywords

ABC TRANSPORTER; ENTEROCHELIN; FERRIC ION; LACTOFERRIN; PROTEIN FBPABC; SALMOCHELIN; SIDEROPHORE; TRANSFERRIN; UNCLASSIFIED DRUG; XENOSIDEROPHORE;

EID: 78650892287     PISSN: 00199567     EISSN: 10985522     Source Type: Journal    
DOI: 10.1128/IAI.00807-10     Document Type: Article
Times cited : (37)

References (70)
  • 1
    • 0029936842 scopus 로고    scopus 로고
    • The fbpABC locus of Neisseria gonorrhoeae functions in the periplasm-to-cytosol transport of iron
    • Adhikari, P., S. A. Berish, A. J. Nowalk, K. L. Veraldi, S. A. Morse, and T. A. Mietzner. 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    Morse, S.A.5    Mietzner, T.A.6
  • 2
    • 0017885589 scopus 로고
    • Stoichiometric and site characteristics of the binding of iron to human transferrin
    • Aisen, P., A. Leibman, and J. Zweier. 1978. Stoichiometric and site characteristics of the binding of iron to human transferrin. J. Biol. Chem. 253:1930-1937.
    • (1978) J. Biol. Chem. , vol.253 , pp. 1930-1937
    • Aisen, P.1    Leibman, A.2    Zweier, J.3
  • 3
    • 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
  • 5
    • 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
  • 7
    • 0030893908 scopus 로고    scopus 로고
    • Cloning and functional characterization of Neisseria gonorrhoeae tonB, exbB and exbD genes
    • Biswas, G. D., J. E. Anderson, and P. F. Sparling. 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
  • 8
    • 0029163535 scopus 로고
    • Characterization of lbpA, the structural gene for a lactoferrin receptor in Neisseria gonorrhoeae
    • Biswas, G. D., and P. F. Sparling. 1995. Characterization of lbpA, 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
  • 9
    • 0029155042 scopus 로고
    • Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins
    • Braun, V. 1995. Energy-coupled transport and signal transduction through the Gram-negative outer membrane via TonB-ExbB-ExbD-dependent receptor proteins. FEMS Microbiol. Rev. 16:295-307.
    • (1995) FEMS Microbiol. Rev. , vol.16 , pp. 295-307
    • Braun, V.1
  • 10
    • 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
  • 12
    • 77949898564 scopus 로고    scopus 로고
    • Centers for Disease Control and Prevention Centers for Disease Control and Prevention, Atlanta, GA
    • Centers for Disease Control and Prevention. 2009. Sexually transmitted disease surveillance, 2008. Centers for Disease Control and Prevention, Atlanta, GA.
    • (2009) Sexually Transmitted Disease Surveillance 2008
  • 13
    • 0029850699 scopus 로고    scopus 로고
    • Identification and purification of a hemoglobin-binding outer membrane protein from Neisseria gonorrhoeae
    • Chen, C. J., P. F. Sparling, L. A. Lewis, D. W. Dyer, and C. Elkins. 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
  • 14
    • 1642581491 scopus 로고    scopus 로고
    • A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds
    • Chen, C. J., D. M. Tobiason, C. E. Thomas, W. M. Shafer, H. S. Seifert, and P. F. Sparling. 2004. A mutant form of the Neisseria gonorrhoeae pilus secretin protein PilQ allows increased entry of heme and antimicrobial compounds. J. Bacteriol. 186:730-739.
    • (2004) J. Bacteriol. , vol.186 , pp. 730-739
    • Chen, C.J.1    Tobiason, D.M.2    Thomas, C.E.3    Shafer, W.M.4    Seifert, H.S.5    Sparling, P.F.6
  • 15
    • 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
  • 16
    • 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., G. D. Biswas, J. Tsai, D. K. Paruchuri, S. A. Thompson, and P. F. Sparling. 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
  • 17
    • 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
  • 18
    • 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
  • 19
    • 33644772217 scopus 로고    scopus 로고
    • The challenge of pelvic inflammatory disease
    • Crossman, S. H. 2006. The challenge of pelvic inflammatory disease. Am. Fam. Physician 73:859-864.
    • (2006) Am. Fam. Physician , vol.73 , pp. 859-864
    • Crossman, S.H.1
  • 20
    • 0024601398 scopus 로고
    • Interaction of complement with Neisseria meningitidis and Neisseria gonorrhoeae
    • Densen, P. 1989. Interaction of complement with Neisseria meningitidis and Neisseria gonorrhoeae. Clin. Microbiol. Rev. 2(Suppl):S11-S17.
    • (1989) Clin. Microbiol. Rev. , vol.2 , Issue.SUPPL.
    • Densen, P.1
  • 22
    • 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. Bac-teriol. 178:5020-5023.
    • (1996) J. Bac-teriol. , vol.178 , pp. 5020-5023
    • Desai, P.J.1    Angerer, A.2    Genco, C.A.3
  • 23
    • 0029560821 scopus 로고
    • The product of the pilQ gene is essential for the biogenesis of type IV pili in Neisseria gonorrhoeae
    • Drake, S. L., and M. Koomey. 1995. The product of the pilQ gene is essential for the biogenesis of type IV pili in Neisseria gonorrhoeae. Mol. Microbiol. 18:975-986.
    • (1995) Mol. Microbiol. , vol.18 , pp. 975-986
    • Drake, S.L.1    Koomey, M.2
  • 24
    • 0025773014 scopus 로고
    • Species-specific uptake of DNA by gonococci is mediated by a 10-base-pair sequence
    • Elkins, C., C. E. Thomas, H. S. Seifert, and P. F. Sparling. 1991. Species-specific uptake of DNA by gonococci is mediated by a 10-base-pair sequence. J. Bacteriol. 173:3911-3913.
    • (1991) J. Bacteriol. , vol.173 , pp. 3911-3913
    • Elkins, C.1    Thomas, C.E.2    Seifert, H.S.3    Sparling, P.F.4
  • 25
    • 0037064287 scopus 로고    scopus 로고
    • TonB-dependent receptors\structural perspectives
    • Ferguson, A. D., and J. Deisenhofer. 2002. TonB-dependent receptors\structural perspectives. Biochim. Biophys. Acta 1565:318-332.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 318-332
    • Ferguson, A.D.1    Deisenhofer, J.2
  • 26
    • 14144253168 scopus 로고    scopus 로고
    • In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase
    • Fischbach, M. A., H. Lin, D. R. Liu, and C. T. Walsh. 2005. In vitro characterization of IroB, a pathogen-associated C-glycosyltransferase. Proc. Natl. Acad. Sci. U.S.A. 102:571-576.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 571-576
    • Fischbach, M.A.1    Lin, H.2    Liu, D.R.3    Walsh, C.T.4
  • 27
  • 28
    • 0035055258 scopus 로고    scopus 로고
    • Characterization of the Yersinia pestis Yfu ABC inorganic iron transport system
    • Gong, S., S. W. Bearden, V. A. Geoffroy, J. D. Fetherston, and R. D. Perry. 2001. Characterization of the Yersinia pestis Yfu ABC inorganic iron transport system. Infect. Immun. 69:2829-2837.
    • (2001) Infect. Immun. , vol.69 , pp. 2829-2837
    • Gong, S.1    Bearden, S.W.2    Geoffroy, V.A.3    Fetherston, J.D.4    Perry, R.D.5
  • 31
    • 33750446693 scopus 로고    scopus 로고
    • Neisseria gonorrhoeae requires expression of TonB and the putative transporter TdfF to replicate within cervical epithelial cells
    • Hagen, T. A., and C. N. Cornelissen. 2006. Neisseria gonorrhoeae requires expression of TonB and the putative transporter TdfF to replicate within cervical epithelial cells. Mol. Microbiol. 62:1144-1157.
    • (2006) Mol. Microbiol. , vol.62 , pp. 1144-1157
    • Hagen, T.A.1    Cornelissen, C.N.2
  • 32
    • 0030788726 scopus 로고    scopus 로고
    • The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system
    • Hagman, K. E., C. E. Lucas, J. T. Balthazar, L. Snyder, M. Nilles, R. C. Judd, and W. M. Shafer. 1997. The MtrD protein of Neisseria gonorrhoeae is a member of the resistance/nodulation/division protein family constituting part of an efflux system. Microbiology 143:2117-2125.
    • (1997) Microbiology , vol.143 , pp. 2117-2125
    • Hagman, K.E.1    Lucas, C.E.2    Balthazar, J.T.3    Snyder, L.4    Nilles, M.5    Judd, R.C.6    Shafer, W.M.7
  • 33
    • 0028906903 scopus 로고
    • Resistance of Neisseria gonorrhoeae to antimicrobial hydropho-bic agents is modulated by the mtrRCDE efflux system
    • Hagman, K. E., W. Pan, B. G. Spratt, J. T. Balthazar, R. C. Judd, and W. M. Shafer. 1995. Resistance of Neisseria gonorrhoeae to antimicrobial hydropho-bic agents is modulated by the mtrRCDE efflux system. Microbiology 141: 611-622.
    • (1995) Microbiology , vol.141 , pp. 611-622
    • Hagman, K.E.1    Pan, W.2    Spratt, B.G.3    Balthazar, J.T.4    Judd, R.C.5    Shafer, W.M.6
  • 34
    • 0037388150 scopus 로고    scopus 로고
    • Salmo-chelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN
    • Hantke, K., G. Nicholson, W. Rabsch, and G. Winkelmann. 2003. Salmo-chelins, siderophores of Salmonella enterica and uropathogenic Escherichia coli strains, are recognized by the outer membrane receptor IroN. Proc. Natl. Acad. Sci. U.S.A. 100:3677-3682.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 3677-3682
    • Hantke, K.1    Nicholson, G.2    Rabsch, W.3    Winkelmann, G.4
  • 35
    • 77951981537 scopus 로고    scopus 로고
    • Chemistry and biology of siderophores
    • Hider, R. C., and X. Kong. 2010. Chemistry and biology of siderophores. Nat. Prod. Rep. 27:637-657.
    • (2010) Nat. Prod. Rep. , vol.27 , pp. 637-657
    • Hider, R.C.1    Kong, X.2
  • 36
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction
    • Horton, R. M., Z. L. Cai, S. N. Ho, and L. R. Pease. 1990. Gene splicing by overlap extension: tailor-made genes using the polymerase chain reaction. Biotechniques 8:528-535.
    • (1990) Biotechniques , vol.8 , pp. 528-535
    • Horton, R.M.1    Cai, Z.L.2    Ho, S.N.3    Pease, L.R.4
  • 39
    • 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
  • 40
    • 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
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 42
    • 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
  • 43
    • 0027244956 scopus 로고
    • Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells
    • Menard, R., P. J. Sansonetti, and C. Parsot. 1993. Nonpolar mutagenesis of the ipa genes defines IpaB, IpaC, and IpaD as effectors of Shigella flexneri entry into epithelial cells. J. Bacteriol. 175:5899-5906.
    • (1993) J. Bacteriol. , vol.175 , pp. 5899-5906
    • Menard, R.1    Sansonetti, P.J.2    Parsot, C.3
  • 44
    • 50249085014 scopus 로고    scopus 로고
    • Vibrio cholerae VciB promotes iron uptake via ferrous iron transporters
    • Mey, A. R., E. E. Wyckoff, L. A. Hoover, C. R. Fisher, and S. M. Payne. 2008. Vibrio cholerae VciB promotes iron uptake via ferrous iron transporters. J. Bacteriol. 190:5953-5962.
    • (2008) J. Bacteriol. , vol.190 , pp. 5953-5962
    • Mey, A.R.1    Wyckoff, E.E.2    Hoover, L.A.3    Fisher, C.R.4    Payne, S.M.5
  • 45
    • 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
  • 46
    • 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
  • 47
    • 0026019764 scopus 로고
    • A series of wide-host-range low-copy-number vectors that allow direct screening for recom-binants
    • Morales, V. M., A. Backman, and M. Bagdasarian. 1991. A series of wide-host-range low-copy-number vectors that allow direct screening for recom-binants. Gene 97:39-47.
    • (1991) Gene , vol.97 , pp. 39-47
    • Morales, V.M.1    Backman, A.2    Bagdasarian, M.3
  • 48
    • 0016123958 scopus 로고
    • Glucose metabolism in Neisseria gonorrhoeae
    • Morse, S. A., S. Stein, and J. Hines. 1974. Glucose metabolism in Neisseria gonorrhoeae. J. Bacteriol. 120:702-714.
    • (1974) J. Bacteriol. , vol.120 , pp. 702-714
    • Morse, S.A.1    Stein, S.2    Hines, J.3
  • 49
    • 67651242062 scopus 로고    scopus 로고
    • Salmochelin, the long-overlooked catecholate siderophore of Salmonella
    • Muller, S. I., M. Valdebenito, and K. Hantke. 2009. Salmochelin, the long-overlooked catecholate siderophore of Salmonella. Biometals 22:691-695.
    • (2009) Biometals , vol.22 , pp. 691-695
    • Muller, S.I.1    Valdebenito, M.2    Hantke, K.3
  • 51
    • 70350643410 scopus 로고    scopus 로고
    • The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis
    • Oves-Costales, D., N. Kadi, and G. L. Challis. 2009. The long-overlooked enzymology of a nonribosomal peptide synthetase-independent pathway for virulence-conferring siderophore biosynthesis. Chem. Commun. (Camb.) 43: 6530-6541.
    • (2009) Chem. Commun. (Camb.) , vol.43 , pp. 6530-6541
    • Oves-Costales, D.1    Kadi, N.2    Challis, G.L.3
  • 54
    • 34648843572 scopus 로고    scopus 로고
    • Gonococcal transferrin binding protein chimeras induce bactericidal and growth inhibitory antibodies in mice
    • Price, G. A., H. P. Masri, A. M. Hollander, M. W. Russell, and C. N. Cornelissen. 2007. Gonococcal transferrin binding protein chimeras induce bactericidal and growth inhibitory antibodies in mice. Vaccine 25:7247-7260.
    • (2007) Vaccine , vol.25 , pp. 7247-7260
    • Price, G.A.1    Masri, H.P.2    Hollander, A.M.3    Russell, M.W.4    Cornelissen, C.N.5
  • 56
    • 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. 8:1186-1218.
    • (2003) Front. Biosci. , vol.8 , pp. 1186-1218
    • Rohde, K.H.1    Dyer, D.W.2
  • 57
    • 0032767010 scopus 로고    scopus 로고
    • Induction of the mtrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein
    • Rouquette, C., J. B. Harmon, and W. M. Shafer. 1999. Induction of the mtrCDE-encoded efflux pump system of Neisseria gonorrhoeae requires MtrA, an AraC-like protein. Mol. Microbiol. 33:651-658.
    • (1999) Mol. Microbiol. , vol.33 , pp. 651-658
    • Rouquette, C.1    Harmon, J.B.2    Shafer, W.M.3
  • 58
    • 0036150304 scopus 로고    scopus 로고
    • Inducible, but not constitutive, resistance of gonococci to hydrophobic agents due to the MtrC-MtrD-MtrE efflux pump requires TonB-ExbB-ExbD proteins
    • Rouquette-Loughlin, C., I. Stojiljkovic, T. Hrobowski, J. T. Balthazar, and W. M. Shafer. 2002. Inducible, but not constitutive, resistance of gonococci to hydrophobic agents due to the MtrC-MtrD-MtrE efflux pump requires TonB-ExbB-ExbD proteins. Antimicrob. Agents Chemother. 46:561-565.
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 561-565
    • Rouquette-Loughlin, C.1    Stojiljkovic, I.2    Hrobowski, T.3    Balthazar, J.T.4    Shafer, W.M.5
  • 59
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II protein secretion systems
    • Russel, M. 1998. Macromolecular assembly and secretion across the bacterial cell envelope: type II protein secretion systems. J. Mol. Biol. 279:485-499.
    • (1998) J. Mol. Biol. , vol.279 , pp. 485-499
    • Russel, M.1
  • 60
    • 0034007472 scopus 로고    scopus 로고
    • Molecular characterization of a novel siderophore-independent iron transport system in Yersinia
    • Saken, E., A. Rakin, and J. Heesemann. 2000. Molecular characterization of a novel siderophore-independent iron transport system in Yersinia. Int. J. Med. Microbiol. 290:51-60.
    • (2000) Int. J. Med. Microbiol. , vol.290 , pp. 51-60
    • Saken, E.1    Rakin, A.2    Heesemann, J.3
  • 61
    • 0030995983 scopus 로고    scopus 로고
    • Insertionally inactivated and inducible recA alleles for use in Neisseria
    • Seifert, H. S. 1997. Insertionally inactivated and inducible recA alleles for use in Neisseria. Gene 188:215-220.
    • (1997) Gene , vol.188 , pp. 215-220
    • Seifert, H.S.1
  • 62
    • 0035083379 scopus 로고    scopus 로고
    • Genetic organization and regulation of antimicrobial efflux systems possessed by Neisseria gonorrhoeae and Neisseria meningitidis
    • Shafer, W. M., W. L. Veal, E. H. Lee, L. Zarantonelli, J. T. Balthazar, and C. Rouquette. 2001. Genetic organization and regulation of antimicrobial efflux systems possessed by Neisseria gonorrhoeae and Neisseria meningitidis. J. Mol. Microbiol. Biotechnol. 3:219-224.
    • (2001) J. Mol. Microbiol. Biotechnol. , vol.3 , pp. 219-224
    • Shafer, W.M.1    Veal, W.L.2    Lee, E.H.3    Zarantonelli, L.4    Balthazar, J.T.5    Rouquette, C.6
  • 63
    • 0000517003 scopus 로고
    • Biology of Neisseria gonorrhoeae
    • K. K. Holmes, P.-A. Mardh, P. F. Sparling, and P. J. Weisner (ed.) McGraw-Hill, New York, NY
    • Sparling, P. F. 1990. Biology of Neisseria gonorrhoeae, p. 131-138. In K. K. Holmes, P.-A. Mardh, P. F. Sparling, and P. J. Weisner (ed.), Sexually transmitted diseases, 2nd ed. McGraw-Hill, New York, NY.
    • (1990) Sexually Transmitted Diseases, 2nd Ed. , pp. 131-138
    • Sparling, P.F.1
  • 64
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedures and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedures and some applications. Proc. Natl. Acad. Sci. U.S.A. 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 65
    • 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., C. E. Thomas, C. Elkins, S. Clary, and P. F. Sparling. 1998. 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
  • 66
    • 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. (Pubitemid 32454646)
    • (2001) Microbiology , vol.147 , Issue.5 , pp. 1277-1290
    • Turner, P.C.1    Thomas, C.E.2    Stojiljkovic, I.3    Elkins, C.4    Kizel, G.5    Ala'Aldeen, D.A.A.6    Sparling, P.F.7
  • 68
    • 0031883514 scopus 로고    scopus 로고
    • Loss-of-function mutations in the mtr efflux system of Neisseria gonorrhoeae
    • Veal, W. L., A. Yellen, J. T. Balthazar, W. Pan, B. G. Spratt, and W. M. Shafer. 1998. Loss-of-function mutations in the mtr efflux system of Neisseria gonorrhoeae. Microbiology 144(Pt. 3):621-627.
    • (1998) Microbiology , vol.144 , Issue.PART 3 , pp. 621-627
    • Veal, W.L.1    Yellen, A.2    Balthazar, J.T.3    Pan, W.4    Spratt, B.G.5    Shafer, W.M.6
  • 69
    • 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
  • 70
    • 33748766356 scopus 로고    scopus 로고
    • Characterization of ferric and ferrous iron transport systems in Vibrio chol-erae
    • Wyckoff, E. E., A. R. Mey, A. Leimbach, C. F. Fisher, and S. M. Payne. 2006. Characterization of ferric and ferrous iron transport systems in Vibrio chol-erae. J. Bacteriol. 188:6515-6523.
    • (2006) J. Bacteriol. , vol.188 , pp. 6515-6523
    • Wyckoff, E.E.1    Mey, A.R.2    Leimbach, A.3    Fisher, C.F.4    Payne, S.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.