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Volumn 149, Issue 7, 2003, Pages 1729-1737

Bacterial lactoferrin-binding protein A binds to both domains of the human lactoferrin C-lobe

Author keywords

[No Author keywords available]

Indexed keywords

CELL SURFACE RECEPTOR; HYBRID PROTEIN; IRON; IRON BINDING PROTEIN; LACTOFERRIN; TRANSFERRIN;

EID: 0037810925     PISSN: 13500872     EISSN: None     Source Type: Journal    
DOI: 10.1099/mic.0.26281-0     Document Type: Article
Times cited : (21)

References (46)
  • 1
    • 0027051023 scopus 로고
    • The N-linked oligosaccharides of human lactoferrin are not required for binding to bacterial lactoferrin receptors
    • Alcantara, J., Padda, J. S. & Schryvers, A. B. (1992). The N-linked oligosaccharides of human lactoferrin are not required for binding to bacterial lactoferrin receptors. Can J Microbiol 38, 1202-1205.
    • (1992) Can. J. Microbiol. , vol.38 , pp. 1202-1205
    • Alcantara, J.1    Padda, J.S.2    Schryvers, A.B.3
  • 2
    • 0027314252 scopus 로고
    • The region of human transferrin involved in binding to bacterial transferrin receptors is localized in the C-lobe
    • Alcantara, J., Yu, R.-H. & Schryvers, A. B. (1993). The region of human transferrin involved in binding to bacterial transferrin receptors is localized in the C-lobe. Mol Microbiol 8, 1135-1143.
    • (1993) Mol. Microbiol. , vol.8 , pp. 1135-1143
    • Alcantara, J.1    Yu, R.-H.2    Schryvers, A.B.3
  • 3
    • 0029851856 scopus 로고    scopus 로고
    • High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization
    • Ali, S. A., Joao, H. C., Csonga, R., Hammerschmid, F. & Steinkasserer, A. (1996). High-yield production of functionally active human serum transferrin using a baculovirus expression system, and its structural characterization. Biochem J 319, 191-195.
    • (1996) Biochem. J. , vol.319 , pp. 191-195
    • Ali, S.A.1    Joao, H.C.2    Csonga, R.3    Hammerschmid, F.4    Steinkasserer, A.5
  • 4
    • 0024389662 scopus 로고
    • Structure of human lactoferrin: Crystallographic structure analysis and refinement at 2.8 Å resolution
    • Anderson, B. F., Baker, H. M., Norris, G. E., Rice, D. W. & Baker, E. N. (1989). Structure of human lactoferrin: crystallographic structure analysis and refinement at 2.8 Å resolution. J Mol Biol 209, 711-734.
    • (1989) J. Mol. Biol. , vol.209 , pp. 711-734
    • Anderson, B.F.1    Baker, H.M.2    Norris, G.E.3    Rice, D.W.4    Baker, E.N.5
  • 5
    • 0028308286 scopus 로고
    • Gonococcal transferrin-binding protein 2 facilitates but is not essential for transferrin utilization
    • Anderson, J. A., Sparling, P. F. & 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
  • 6
    • 0001447664 scopus 로고
    • Transferrins: Insights into structure and function from studies on lactoferrin
    • Baker, E. N., Rumball, S. V. & Anderson, B. F. (1987). Transferrins: insights into structure and function from studies on lactoferrin. Trends Biochem Sci 12, 350-355.
    • (1987) Trends. Biochem. Sci. , vol.12 , pp. 350-355
    • Baker, E.N.1    Rumball, S.V.2    Anderson, B.F.3
  • 7
    • 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. & 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 Bacterial 180, 3080-3090.
    • (1998) J. Bacterial. , vol.180 , pp. 3080-3090
    • Bonnah, R.A.1    Schryvers, A.B.2
  • 8
    • 0031933035 scopus 로고    scopus 로고
    • Biochemical and immunological properties of lactoferrin binding proteins from Moraxella (Branhamella) catarrhalis
    • Bonnah, R. A., Yu, R.-H., Wong, H. & Schryvers, A. B. (1998). Biochemical and immunological properties of lactoferrin binding proteins from Moraxella (Branhamella) catarrhalis. Microb Pathog 24, 89-100.
    • (1998) Microb. Pathog. , vol.24 , pp. 89-100
    • Bonnah, R.A.1    Yu, R.-H.2    Wong, H.3    Schryvers, A.B.4
  • 9
    • 0033015203 scopus 로고    scopus 로고
    • Characterization of Moraxella (Branhamella) catarrhalis lbpB, lbpA and lactoferrin receptor orf3 isogenic mutants
    • Bonnah, R. A., Wong, H., Loosmore, S. M. & Schryvers, A. B. (1999). Characterization of Moraxella (Branhamella) catarrhalis lbpB, lbpA and lactoferrin receptor orf3 isogenic mutants. Infect Immun 67, 1517-1520.
    • (1999) Infect. Immun. , vol.67 , pp. 1517-1520
    • Bonnah, R.A.1    Wong, H.2    Loosmore, S.M.3    Schryvers, A.B.4
  • 10
    • 0024500555 scopus 로고
    • The role of the carboxy-terminal membrane-spanning fragment in the biogenesis of Escherichia coli K12 outer membrane protein PhoE
    • Bosch, D., Scholten, M., Verhagen, C. & Tornmassen, J. (1989). The role of the carboxy-terminal membrane-spanning fragment in the biogenesis of Escherichia coli K12 outer membrane protein PhoE, Mol Gen Genet 216, 144-148.
    • (1989) Mol. Gen. Genet. , vol.216 , pp. 144-148
    • Bosch, D.1    Scholten, M.2    Verhagen, C.3    Tornmassen, J.4
  • 11
    • 0034442794 scopus 로고    scopus 로고
    • Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions
    • Boulton, I. C., Yost, M. K., Anderson, J. E. & Cornelissen, C. N. (2000). Identification of discrete domains within gonococcal transferrin-binding protein A that are necessary for ligand binding and iron uptake functions. Infect Immun 68, 6988-6996.
    • (2000) Infect. Immun. , vol.68 , pp. 6988-6996
    • Boulton, I.C.1    Yost, M.K.2    Anderson, J.E.3    Cornelissen, C.N.4
  • 13
    • 0345551954 scopus 로고    scopus 로고
    • Ferric enterobactin binding and utilization by Neisseria gonorrhoeae
    • Carson, S. D., Klebba, P. E., Newton, S. M. & Sparling, P. F. (1999). Ferric enterobactin binding and utilization by Neisseria gonorrhoeae. J Bacterial 181, 2895-2901.
    • (1999) J. Bacterial. , vol.181 , pp. 2895-2901
    • Carson, S.D.1    Klebba, P.E.2    Newton, S.M.3    Sparling, P.F.4
  • 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. & 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. & 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
    • 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. & Sparling, P. F. (1998). The transferrin receptor expressed by gonococcal strain FA1090 is required for the experimental infection of human male volunteers. Mol Microbial 27, 611-616.
    • (1998) Mol. Microbial. , 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
  • 17
    • 0033819031 scopus 로고    scopus 로고
    • Biotinylation of proteins in vivo and in vitro using small peptide tags
    • Cull, M. G. & Schatz, P. J. (2000). Biotinylation of proteins in vivo and in vitro using small peptide tags. Methods Enzymol 326, 430-440.
    • (2000) Methods Enzymol. , vol.326 , pp. 430-440
    • Cull, M.G.1    Schatz, P.J.2
  • 19
    • 0025096790 scopus 로고
    • Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein
    • Funk, W. D., MacGillivray, R. T. A., Mason, A. B., Brown, S. A. & Woodworth, R. C. (1990). Expression of the amino-terminal half-molecule of human serum transferrin in cultured cells and characterization of the recombinant protein. Biochemistry 29, 1654-1660.
    • (1990) Biochemistry , vol.29 , pp. 1654-1660
    • Funk, W.D.1    MacGillivray, R.T.A.2    Mason, A.B.3    Brown, S.A.4    Woodworth, R.C.5
  • 20
    • 0028865548 scopus 로고
    • Sequence, genetic analysis, and expression of Actinobacillus pleuro-pneumoniae transferrin receptor genes
    • Gonzalez, G. C., Yu, R.-H., Rosteck, P. & Schryvers, A. B. (1995). Sequence, genetic analysis, and expression of Actinobacillus pleuro-pneumoniae transferrin receptor genes. Microbiology 141, 2405-2416.
    • (1995) Microbiology , vol.141 , pp. 2405-2416
    • Gonzalez, G.C.1    Yu, R.-H.2    Rosteck, P.3    Schryvers, A.B.4
  • 21
    • 0029894182 scopus 로고    scopus 로고
    • Bacterial transferrin and lactoferrin receptors
    • Gray-Owen, S. D. & 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
  • 22
    • 0028958297 scopus 로고
    • Identification and characterization of genes encoding the human transferrin binding proteins from Haemophilus influenzae
    • Gray-Owen, S. D., Loosmore, S. & Schryvers, A. B. (1995). Identification and characterization of genes encoding the human transferrin binding proteins from Haemophilus influenzae. Infect Immun 63, 1201-1210.
    • (1995) Infect. Immun. , vol.63 , pp. 1201-1210
    • Gray-Owen, S.D.1    Loosmore, S.2    Schryvers, A.B.3
  • 23
    • 0023659137 scopus 로고
    • New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues
    • Hochuli, E., Dobeli, H. & Schacher, A. (1987). New metal chelate adsorbent selective for proteins and peptides containing neighbouring histidine residues. J Chromatogr 411, 177-184.
    • (1987) J. Chromatogr. , vol.411 , pp. 177-184
    • Hochuli, E.1    Dobeli, H.2    Schacher, A.3
  • 24
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using the polymerase chain reaction
    • Horton, R. M., Cai, Z., Ho, S. N. & Pease, L. R. (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.2    Ho, S.N.3    Pease, L.R.4
  • 25
    • 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
  • 26
    • 0031866123 scopus 로고    scopus 로고
    • Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor
    • Lewis, L. A., Rohde, K., Gipson, M., Behrens, B., Gray, E., Toth, S. I., Roe, B. A. & Dyer, D. W. (1998). Identification and molecular analysis of lbpBA, which encodes the two-component meningococcal lactoferrin receptor. Infect Immun 66, 3017-3023.
    • (1998) Infect. Immun. , vol.66 , pp. 3017-3023
    • Lewis, L.A.1    Rohde, K.2    Gipson, M.3    Behrens, B.4    Gray, E.5    Toth, S.I.6    Roe, B.A.7    Dyer, D.W.8
  • 27
    • 0033534452 scopus 로고    scopus 로고
    • Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex
    • Liu, C. E., Lui, P.-Q., Wolf, A., Lin, E. & Ames, G. F.-L. (1999). Both lobes of the soluble receptor of the periplasmic histidine permease, an ABC transporter (traffic ATPase), interact with the membrane-bound complex. J Biol Chem 274, 739-747.
    • (1999) J. Biol. Chem. , vol.274 , pp. 739-747
    • Liu, C.E.1    Lui, P.-Q.2    Wolf, A.3    Lin, E.4    Ames, G.F.-L.5
  • 28
    • 0019306494 scopus 로고
    • Nature of the heterogeneity within genetic variants of bovine serum transferrin
    • Maeda, K., McKenzie, H. A. & Shaw, D. C. (1980). Nature of the heterogeneity within genetic variants of bovine serum transferrin. Anim Blood Groups Biochem Genet 11, 63-80.
    • (1980) Anim. Blood Groups Biochem. Genet. , vol.11 , pp. 63-80
    • Maeda, K.1    McKenzie, H.A.2    Shaw, D.C.3
  • 29
    • 0036153922 scopus 로고    scopus 로고
    • Specific ligand binding attributable to individual epitopes of gonococcal transferrin binding protein A
    • Masri, H. P. & Cornelissen, C. N. (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
  • 31
    • 0031304915 scopus 로고    scopus 로고
    • Periplasmic secretion of functional ovotransferrin N-lobe in Escherichia coli
    • Miyauchi, T., Takahashi, N. & Hirose, M. (1997). Periplasmic secretion of functional ovotransferrin N-lobe in Escherichia coli. Biosci Biotechnol Biochem 61, 2125-2126.
    • (1997) Biosci. Biotechnol. Biochem. , vol.61 , pp. 2125-2126
    • Miyauchi, T.1    Takahashi, N.2    Hirose, M.3
  • 32
    • 0024400694 scopus 로고
    • Expression of gonococcal protein II in Escherichia coli by translational fusion
    • Palmer, L., Brooks, G. F. & Falkow, S. (1989). Expression of gonococcal protein II in Escherichia coli by translational fusion. Mol Microbial 3, 663-671.
    • (1989) Mol. Microbial. , vol.3 , pp. 663-671
    • Palmer, L.1    Brooks, G.F.2    Falkow, S.3
  • 33
    • 0028345373 scopus 로고
    • Identification of the iroA gene product of Neisseria meningitidis as a lactoferrin receptor
    • Pettersson, A., Maas, A. & Tommassen, J. (1994). 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
  • 34
    • 0030023410 scopus 로고    scopus 로고
    • Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors
    • Retzer, M. D., Kabani, A., Button, L., Yu, R.-H. & Schryvers, A. B. (1996). Production and characterization of chimeric transferrins for the determination of the binding domains for bacterial transferrin receptors. J Biol Chem 271, 1166-1173,
    • (1996) J. Biol. Chem. , vol.271 , pp. 1166-1173
    • Retzer, M.D.1    Kabani, A.2    Button, L.3    Yu, R.-H.4    Schryvers, A.B.5
  • 36
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: A 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz, P. J. (1993). Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology 11, 1138-1143.
    • (1993) Biotechnology , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 37
    • 0025212523 scopus 로고
    • Receptors for transferrin in pathogenic bacteria are specific for the host's protein
    • Schryvers, A. B. & Gonzalez, G. C. (1990). Receptors for transferrin in pathogenic bacteria are specific for the host's protein. Can J Microbiol 36, 145-147.
    • (1990) Can. J. Microbiol. , vol.36 , pp. 145-147
    • Schryvers, A.B.1    Gonzalez, G.C.2
  • 38
    • 0027432140 scopus 로고
    • Analysis of bacterial receptors for host iron binding proteins
    • Schryvers, A. B. & Lee, B. C. (1993). Analysis of bacterial receptors for host iron binding proteins. J Microbiol Methods 18, 255-266.
    • (1993) J. Microbiol. Methods , vol.18 , pp. 255-266
    • Schryvers, A.B.1    Lee, B.C.2
  • 39
    • 0023880568 scopus 로고
    • Identification and characterization of the human lactoferrin-binding protein from Neisseria meningitidis
    • Schryvers, A. B. & 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
  • 40
    • 0033064808 scopus 로고    scopus 로고
    • Iron acquisition systems in the pathogenic neisseria
    • Schryvers, A. B. & Stojiljkovic, I. (1999). Iron acquisition systems in the pathogenic neisseria. Mol Microbial 32, 1117-1123.
    • (1999) Mol. Microbial. , vol.32 , pp. 1117-1123
    • Schryvers, A.B.1    Stojiljkovic, I.2
  • 41
    • 0005342165 scopus 로고    scopus 로고
    • Bacterial lactoferrin receptors
    • Edited by K.-C. Shimazaki, H. Tsuda, M. Tomita, T. Kuwata & J.-P. Perraudin. Amsterdam: Elsevier
    • Schryvers, A. B. & Wong, H. (2000). Bacterial lactoferrin receptors. In Lactoferrin: Structure, Function and Applications, pp. 55-65. Edited by K.-C. Shimazaki, H. Tsuda, M. Tomita, T. Kuwata & J.-P. Perraudin. Amsterdam: Elsevier.
    • (2000) Lactoferrin: Structure, Function and Applications , pp. 55-65
    • Schryvers, A.B.1    Wong, H.2
  • 42
    • 14744300639 scopus 로고
    • Production of biologically active recombinant human lactoferrin in Aspergillus oryzae
    • Ward, P. P., Lo, J.-Y., Duke, M., May, G. S., Headon, D. R. & Conneely, O. M. (1992). Production of biologically active recombinant human lactoferrin in Aspergillus oryzae. Biotechnology 10, 784-789.
    • (1992) Biotechnology , vol.10 , pp. 784-789
    • Ward, P.P.1    Lo, J.-Y.2    Duke, M.3    May, G.S.4    Headon, D.R.5    Conneely, O.M.6
  • 43
    • 0018102319 scopus 로고
    • Iron and infection
    • Weinberg, E. D. (1978). Iron and infection. Microbial Rev 42, 45-66.
    • (1978) Microbial. Rev. , vol.42 , pp. 45-66
    • Weinberg, E.D.1
  • 44
    • 0036670736 scopus 로고    scopus 로고
    • Microbial siderophore-mediated transport
    • Winkelmann, G. (2002). Microbial siderophore-mediated transport. Biochem Soc Trans 30, 691-696.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 691-696
    • Winkelmann, G.1
  • 45
    • 0027264029 scopus 로고
    • Regions located in both the N-lobe and C-lobe of human lactoferrin participate in the binding interaction with bacterial lactoferrin receptors
    • Yu, R.-H. & Schryvers, A. B. (1993). Regions located in both the N-lobe and C-lobe of human lactoferrin participate in the binding interaction with bacterial lactoferrin receptors. Microb Pathog 14, 343-353.
    • (1993) Microb. Pathog. , vol.14 , pp. 343-353
    • Yu, R.-H.1    Schryvers, A.B.2
  • 46
    • 0028132653 scopus 로고
    • Transferrin receptors on ruminant pathogens vary in their interaction with the C-lobe and N-lobe of ruminant transferrins
    • Yu, R.-H. & Schryvers, A. B. (1994). Transferrin receptors on ruminant pathogens vary in their interaction with the C-lobe and N-lobe of ruminant transferrins. Can J Microbial 40, 532-540.
    • (1994) Can. J. Microbial. , vol.40 , pp. 532-540
    • Yu, R.-H.1    Schryvers, A.B.2


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