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Volumn 68, Issue 7, 2000, Pages 4049-4054

Importance of holotoxin assembly in Ptl-mediated secretion of pertussis toxin from Bordetella pertussis

Author keywords

[No Author keywords available]

Indexed keywords

PERTUSSIS TOXIN;

EID: 0033931948     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.68.7.4049-4054.2000     Document Type: Article
Times cited : (43)

References (32)
  • 1
    • 0025338668 scopus 로고
    • Roles of the disulfide bond and the carboxy-terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin
    • Antoine, R., and C. Locht. 1990. Roles of the disulfide bond and the carboxy-terminal region of the S1 subunit in the assembly and biosynthesis of pertussis toxin. Infect. Immun. 58:1518-1526.
    • (1990) Infect. Immun. , vol.58 , pp. 1518-1526
    • Antoine, R.1    Locht, C.2
  • 2
    • 0025965870 scopus 로고
    • Bordetella pertussis adenylate cyclase toxin and hemolytic activities require a second gene, cyaC, for activation
    • Barry, E. M., A. A. Weiss, I. E. Ehrmann, M. C. Gray, E. L. Hewlett, and M. S. M. Goodwin. 1991. Bordetella pertussis adenylate cyclase toxin and hemolytic activities require a second gene, cyaC, for activation. J. Bacteriol. 173:720-726.
    • (1991) J. Bacteriol. , vol.173 , pp. 720-726
    • Barry, E.M.1    Weiss, A.A.2    Ehrmann, I.E.3    Gray, M.C.4    Hewlett, E.L.5    Goodwin, M.S.M.6
  • 3
    • 0016700103 scopus 로고
    • Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages
    • Brickman, E., and J. Beckwith. 1975. Analysis of the regulation of Escherichia coli alkaline phosphatase synthesis using deletions and φ80 transducing phages. J. Mol. Biol. 96:307-316.
    • (1975) J. Mol. Biol. , vol.96 , pp. 307-316
    • Brickman, E.1    Beckwith, J.2
  • 5
    • 0019551730 scopus 로고
    • "Western blotting": Electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A
    • Burnette, W. N. 1981. "Western blotting": electrophoretic transfer of proteins from sodium dodecyl sulfate-polyacrylamide gels to unmodified nitrocellulose and radiographic detection with antibody and radioiodinated protein A. Anal. Biochem. 112:195-203.
    • (1981) Anal. Biochem. , vol.112 , pp. 195-203
    • Burnette, W.N.1
  • 7
    • 0030978939 scopus 로고    scopus 로고
    • Agrobacterium tumefaciens T-complex transport apparatus: A paradigm for a new family of multifunctional transporters in eubacteria
    • Christie, P. J. 1997. Agrobacterium tumefaciens T-complex transport apparatus: a paradigm for a new family of multifunctional transporters in eubacteria. J. Bacteriol. 179:3085-3094.
    • (1997) J. Bacteriol. , vol.179 , pp. 3085-3094
    • Christie, P.J.1
  • 8
    • 0032909861 scopus 로고    scopus 로고
    • Identification and characterization of PtlC, an essential component of the pertussis toxin secretion system
    • Cook, D. M., K. M. Farizo, and D. L. Burns. 1999. Identification and characterization of PtlC, an essential component of the pertussis toxin secretion system. Infect. Immun. 67:754-759.
    • (1999) Infect. Immun. , vol.67 , pp. 754-759
    • Cook, D.M.1    Farizo, K.M.2    Burns, D.L.3
  • 9
    • 0027570304 scopus 로고
    • Gene-for-genes interactions between cotton R genes and Xanthomonas campestris pv. malvacearum avr genes
    • DeFeyter, R., Y. Yang, and D. W. Gabriel. 1993. Gene-for-genes interactions between cotton R genes and Xanthomonas campestris pv. malvacearum avr genes. Mol. Plant-Microbe Interact. 6:225-237.
    • (1993) Mol. Plant-Microbe Interact. , vol.6 , pp. 225-237
    • DeFeyter, R.1    Yang, Y.2    Gabriel, D.W.3
  • 10
    • 0000527903 scopus 로고
    • Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans
    • Figurski, D. H., and D. R. Helinski. 1979. Replication of an origin-containing derivative of plasmid RK2 dependent on a plasmid function provided in trans. Proc. Natl. Acad. Sci. USA 76:1648-1652.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 1648-1652
    • Figurski, D.H.1    Helinski, D.R.2
  • 11
    • 0021176155 scopus 로고
    • Interaction of monoclonal antibodies with pertussis toxin and its subunits
    • Frank, D. W., and C. D. Parker. 1984. Interaction of monoclonal antibodies with pertussis toxin and its subunits. Infect. Immun. 46:195-201.
    • (1984) Infect. Immun. , vol.46 , pp. 195-201
    • Frank, D.W.1    Parker, C.D.2
  • 12
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor generated signals
    • Gilman, A. G. 1987. G proteins: transducers of receptor generated signals. Annu. Rev. Biochem. 56:615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 13
    • 0029797481 scopus 로고    scopus 로고
    • Analysis of proteins encoded by the ptx and ptl genes of Bordetella bronchiseptica and Bordetella parapertussis
    • Hausman, S. Z., J. D. Cherry, U. Heininger, C. H. Wirsing von Konig, and D. L. Burns. 1996. Analysis of proteins encoded by the ptx and ptl genes of Bordetella bronchiseptica and Bordetella parapertussis. Infect. Immun. 64: 4020-4026.
    • (1996) Infect. Immun. , vol.64 , pp. 4020-4026
    • Hausman, S.Z.1    Cherry, J.D.2    Heininger, U.3    Wirsing Von Konig, C.H.4    Burns, D.L.5
  • 14
    • 0027933633 scopus 로고
    • Detection and subcellular localization of three Ptl proteins involved in the secretion of pertussis toxin from Bordetella pertussis
    • Johnson, F. D., and D. L. Burns. 1994. Detection and subcellular localization of three Ptl proteins involved in the secretion of pertussis toxin from Bordetella pertussis. J. Bacteriol. 176:5350-5356.
    • (1994) J. Bacteriol. , vol.176 , pp. 5350-5356
    • Johnson, F.D.1    Burns, D.L.2
  • 15
    • 0020791359 scopus 로고
    • The a promoter of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein
    • Katada, T., M. Tamura, and M. Ui. 1983. The A promoter of islet-activating protein, pertussis toxin, as an active peptide catalyzing ADP-ribosylation of a membrane protein. Arch. Biochem. Biophys. 224:290-298.
    • (1983) Arch. Biochem. Biophys. , vol.224 , pp. 290-298
    • Katada, T.1    Tamura, M.2    Ui, M.3
  • 16
    • 0020137319 scopus 로고
    • Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein
    • Katada, T., and M. Ui. 1982. Direct modification of the membrane adenylate cyclase system by islet-activating protein due to ADP-ribosylation of a membrane protein. Proc. Natl. Acad. Sci. USA 79:3129-3133.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 3129-3133
    • Katada, T.1    Ui, M.2
  • 17
    • 0023715368 scopus 로고
    • Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria
    • Keen, N. T., S. Tamaki, D. Kobayashi, and D. Trollinger. 1988. Improved broad-host-range plasmids for DNA cloning in Gram-negative bacteria. Gene 70:191-197.
    • (1988) Gene , vol.70 , pp. 191-197
    • Keen, N.T.1    Tamaki, S.2    Kobayashi, D.3    Trollinger, D.4
  • 19
    • 0024532991 scopus 로고
    • Epitopes on the S1 subunit of pertussis toxin recognized by monoclonal antibodies
    • Kim, K. J., W. N. Burnette, R. D. Sublett, C. R. Manclark, and J. G. Kenimer. 1989. Epitopes on the S1 subunit of pertussis toxin recognized by monoclonal antibodies. Infect. Immun. 57:944-950.
    • (1989) Infect. Immun. , vol.57 , pp. 944-950
    • Kim, K.J.1    Burnette, W.N.2    Sublett, R.D.3    Manclark, C.R.4    Kenimer, J.G.5
  • 20
    • 0030664965 scopus 로고    scopus 로고
    • Essential role of the consensus nucleotide-binding site of PtlH in secretion of pertussis toxin from Bordetella pertussis
    • Kotob, S. I., and D. L. Burns. 1997. Essential role of the consensus nucleotide-binding site of PtlH in secretion of pertussis toxin from Bordetella pertussis. J. Bacteriol. 179:7577-7580.
    • (1997) J. Bacteriol. , vol.179 , pp. 7577-7580
    • Kotob, S.I.1    Burns, D.L.2
  • 21
    • 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 (London) 227:680-685.
    • (1970) Nature (London) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0022492403 scopus 로고
    • Pertussis toxin gene: Nucleotide sequence and genetic organization
    • Locht, C., and J. M. Keith. 1986. Pertussis toxin gene: nucleotide sequence and genetic organization. Science 232:1258-1264.
    • (1986) Science , vol.232 , pp. 1258-1264
    • Locht, C.1    Keith, J.M.2
  • 25
    • 0021027842 scopus 로고
    • A broad host range mobilization system for in vivo genetic engineering: Transposon mutagenesis in Gram negative bacteria
    • Simon, R., U. Priefer, and A. Puhler. 1983. A broad host range mobilization system for in vivo genetic engineering: transposon mutagenesis in Gram negative bacteria. Bio/Technology 1:784-790.
    • (1983) Bio/Technology , vol.1 , pp. 784-790
    • Simon, R.1    Priefer, U.2    Puhler, A.3
  • 27
    • 0028275229 scopus 로고
    • Use of conditionally counterselectable suicide vectors for allelic exchange
    • Stibitz, S. 1994. Use of conditionally counterselectable suicide vectors for allelic exchange. Methods Enzymol. 235:458-465.
    • (1994) Methods Enzymol. , vol.235 , pp. 458-465
    • Stibitz, S.1
  • 28
    • 0025893376 scopus 로고
    • Subcellular localization and immunochemical detection of proteins encoded by the vir locus of Bordetella pertussis
    • Stibitz, S., and M.-S. Yang. 1991. Subcellular localization and immunochemical detection of proteins encoded by the vir locus of Bordetella pertussis. J. Bacteriol. 173:4288-4296.
    • (1991) J. Bacteriol. , vol.173 , pp. 4288-4296
    • Stibitz, S.1    Yang, M.-S.2
  • 29
    • 0020362248 scopus 로고
    • Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model
    • Tamura, M., K. Nogimori, S. Murai, M. Yajima, K. Ito, T. Katada, M. Ui, and S. Ishii. 1982. Subunit structure of islet-activating protein, pertussis toxin, in conformity with the A-B model. Biochemistry 21:5516-5522.
    • (1982) Biochemistry , vol.21 , pp. 5516-5522
    • Tamura, M.1    Nogimori, K.2    Murai, S.3    Yajima, M.4    Ito, K.5    Katada, T.6    Ui, M.7    Ishii, S.8
  • 30
    • 0027518747 scopus 로고
    • Molecular characterization of an operon required for pertussis toxin secretion
    • Weiss, A. A., F. D. Johnson, and D. L. Burns. 1993. Molecular characterization of an operon required for pertussis toxin secretion. Proc. Natl. Acad. Sci. USA 90:2970-2974.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 2970-2974
    • Weiss, A.A.1    Johnson, F.D.2    Burns, D.L.3
  • 31
    • 0024341328 scopus 로고
    • Use of the promoter fusion transposon Tn5 lac to identify mutations in Bordetella pertussis vir-regulated genes
    • Weiss, A. A., A. R. Melton, K. E. Walker, C. Andraos-Selim, and J. J. Meidl. 1989. Use of the promoter fusion transposon Tn5 lac to identify mutations in Bordetella pertussis vir-regulated genes. Infect. Immun. 57:2674-2682.
    • (1989) Infect. Immun. , vol.57 , pp. 2674-2682
    • Weiss, A.A.1    Melton, A.R.2    Walker, K.E.3    Andraos-Selim, C.4    Meidl, J.J.5
  • 32
    • 0029968272 scopus 로고    scopus 로고
    • Adaptation of a conjugal transfer system for the export of pathogenic macromolecules
    • Winans, S. C., D. L. Burns, and P. J. Christie. 1996. Adaptation of a conjugal transfer system for the export of pathogenic macromolecules. Trends Microbiol. 4:64-68.
    • (1996) Trends Microbiol. , vol.4 , pp. 64-68
    • Winans, S.C.1    Burns, D.L.2    Christie, P.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.