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Volumn 33, Issue 6, 1999, Pages 1232-1243

Probing secretion and translocation of a β-autotransporter using a reporter single-chain Fv as a cognate passenger domain

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; BACTERIAL PROTEIN; CARRIER PROTEIN; CHIMERIC PROTEIN; IMMUNOGLOBULIN A; OUTER MEMBRANE PROTEIN; PROTEINASE;

EID: 0032854025     PISSN: 0950382X     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-2958.1999.01571.x     Document Type: Article
Times cited : (77)

References (50)
  • 1
    • 0002438459 scopus 로고    scopus 로고
    • Vectors for phage display
    • Kay, B.K., Winter, J., and McCafferty, J. (eds). San Diego: Academic Press
    • Armstrong, N., Adey, N.B., McConnell, S.J., and Kay, B.K. (1996). Vectors for phage display. In Phage Display of Peptides and Proteins. Kay, B.K., Winter, J., and McCafferty, J. (eds). San Diego: Academic Press, pp. 35-53.
    • (1996) Phage Display of Peptides and Proteins , pp. 35-53
    • Armstrong, N.1    Adey, N.B.2    McConnell, S.J.3    Kay, B.K.4
  • 3
    • 0028028387 scopus 로고
    • Building bridges: Disulphide bond formation in the cell
    • Bardwell, J.C.A. (1994) Building bridges: disulphide bond formation in the cell. Mol Microbiol 14: 199-205.
    • (1994) Mol Microbiol , vol.14 , pp. 199-205
    • Bardwell, J.C.A.1
  • 4
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell, J.C.A., McGovern, K., and Beckwith, J. (1991) Identification of a protein required for disulfide bond formation in vivo. Cell 67: 581-589.
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 5
    • 0028282814 scopus 로고
    • Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi
    • Botoli-German, I., Brun, E., Py, B., Chippaux, M., and Barras, F. (1994) Periplasmic disulphide bond formation is essential for cellulase secretion by the plant pathogen Erwinia chrysanthemi. Mol Microbiol 11: 545-553.
    • (1994) Mol Microbiol , vol.11 , pp. 545-553
    • Botoli-German, I.1    Brun, E.2    Py, B.3    Chippaux, M.4    Barras, F.5
  • 6
    • 0000182975 scopus 로고
    • XL1-blue: A high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection
    • Bullock, W.O., Fernández, J.M., and Short, J.M. (1987). XL1-blue: a high efficiency plasmid transforming recA Escherichia coli strain with beta-galactosidase selection. Biotechniques 4: 376-378.
    • (1987) Biotechniques , vol.4 , pp. 376-378
    • Bullock, W.O.1    Fernández, J.M.2    Short, J.M.3
  • 7
    • 0030049029 scopus 로고    scopus 로고
    • Nondisruptive detection of activity of catabolic promoters of pseudomonas putida with an antigenic surface reporter system
    • Cebolla, A., de Guzman, C., and Lorenzo, V. (1996) Nondisruptive detection of activity of catabolic promoters of Pseudomonas putida with an antigenic surface reporter system. Appl Environ Microbiol 62: 214-220.
    • (1996) Appl Environ Microbiol , vol.62 , pp. 214-220
    • Cebolla, A.1    De Guzman, C.2    Lorenzo, V.3
  • 8
    • 0026572809 scopus 로고
    • The disulfide bonds in antibody variable domains: Effects on stability, folding in vitro, and functional expression in Escherichia coli
    • Glockshuber, R., Schimidt, T., and Plückthun, A. (1992). The disulfide bonds in antibody variable domains: effects on stability, folding in vitro, and functional expression in Escherichia coli. Biochemistry 31: 1270-1279.
    • (1992) Biochemistry , vol.31 , pp. 1270-1279
    • Glockshuber, R.1    Schimidt, T.2    Plückthun, A.3
  • 10
    • 0023840230 scopus 로고
    • OmpT encodes the Eschericha coli outer membrane protease that cleaves T7 RNA polymerase during purification
    • Grodberg, J., and Dunn, J.J. (1988) OmpT encodes the Eschericha coli outer membrane protease that cleaves T7 RNA polymerase during purification. J Bacteriol 170: 1245-1253.
    • (1988) J Bacteriol , vol.170 , pp. 1245-1253
    • Grodberg, J.1    Dunn, J.J.2
  • 11
    • 0021455107 scopus 로고
    • IgA protease of Neisseria gonorrhoeae: Isolation and characterization of the gene and its extracellular product
    • Halter, R., Pohlner, J., and Meyer, T.F. (1984) IgA protease of Neisseria gonorrhoeae: isolation and characterization of the gene and its extracellular product. EMBO J 3: 1595-1601.
    • (1984) EMBO J , vol.3 , pp. 1595-1601
    • Halter, R.1    Pohlner, J.2    Meyer, T.F.3
  • 12
    • 0024443109 scopus 로고
    • Mosaic-like organization of IgA protease genes in Neisseria gonorrhoeae generated by horizontal genetic exchange in vivo
    • Halter, R., Pohlner, J., and Meyer, T.F. (1989) Mosaic-like organization of IgA protease genes in Neisseria gonorrhoeae generated by horizontal genetic exchange in vivo. EMBO J 8: 2737-2744.
    • (1989) EMBO J , vol.8 , pp. 2737-2744
    • Halter, R.1    Pohlner, J.2    Meyer, T.F.3
  • 13
    • 0002588630 scopus 로고
    • Coordinated assembly of multisubunit proteins: Oligomerization of bacterial enterotoxins in vivo and in vitro
    • Hardy, S.J., Holmgren, J., Johansson, S., Sanchez, J., and Hirst, T.R. (1988) Coordinated assembly of multisubunit proteins: oligomerization of bacterial enterotoxins in vivo and in vitro. Proc Natl Acad Sci USA 85: 109-113.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 109-113
    • Hardy, S.J.1    Holmgren, J.2    Johansson, S.3    Sanchez, J.4    Hirst, T.R.5
  • 14
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • Henderson, I.R., Navarro-Garcia, F., and Nataro, J.P. (1998) The great escape: structure and function of the autotransporter proteins. Trends Microbiol 6: 370-378.
    • (1998) Trends Microbiol , vol.6 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 15
    • 0023449557 scopus 로고
    • Conformation of protein secreted across bacterial outer membranes: A study of enterotoxin translocation from Vibrio cholerae
    • Hirst, T.R., and Holmgren, J. (1987a) Conformation of protein secreted across bacterial outer membranes: a study of enterotoxin translocation from Vibrio cholerae. Proc Natl Acad Sci USA 84: 7418-7422.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7418-7422
    • Hirst, T.R.1    Holmgren, J.2
  • 16
    • 0023144553 scopus 로고
    • Transient entry of enterotoxin subunits into the periplasm occurs during their secretion from Vibrio cholerae
    • Hirst, T.R., and Holmgren, J. (1987b) Transient entry of enterotoxin subunits into the periplasm occurs during their secretion from Vibrio cholerae. J Bacteriol 169: 1037-1045.
    • (1987) J Bacteriol , vol.169 , pp. 1037-1045
    • Hirst, T.R.1    Holmgren, J.2
  • 18
    • 0000938404 scopus 로고    scopus 로고
    • Bacterial adhesins and their assembly
    • Neidhardt, F.C., et al. (eds). Washington DC: American Society for Microbiology Press
    • Hultgren, S.J., Jones, C.H., and Normark, S. (1996) Bacterial adhesins and their assembly. In Escherichia coli and Salmonella: Cellular and Molecular Biology. Neidhardt, F.C., et al. (eds). Washington DC: American Society for Microbiology Press, pp. 2730-2756.
    • (1996) Escherichia Coli and Salmonella: Cellular and Molecular Biology , pp. 2730-2756
    • Hultgren, S.J.1    Jones, C.H.2    Normark, S.3
  • 20
    • 0030608368 scopus 로고    scopus 로고
    • Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Igaβ autotransporter pathway
    • Jose, J., Krämer, J., Klauser, T., Pohlner, J., and Meyer, T.F. (1996) Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Igaβ autotransporter pathway. Gene 178: 107-110.
    • (1996) Gene , vol.178 , pp. 107-110
    • Jose, J.1    Krämer, J.2    Klauser, T.3    Pohlner, J.4    Meyer, T.F.5
  • 21
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: Conformation-dependent outer membrane translocation
    • Klauser, T., Pohlner, J., and Meyer, T.F. (1990) Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: conformation-dependent outer membrane translocation. EMBO J 9: 1991-1999.
    • (1990) EMBO J , vol.9 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 22
    • 0026511122 scopus 로고
    • Selective extracellular release of cholera toxin B subunit by Escherichia coli: Dissection of Neisseria Igaβ-mediated outer membrane transport
    • Klauser, T., Pohlner, J., and Meyer, T.F. (1992) Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria Igaβ-mediated outer membrane transport. EMBO J 11: 2327-2335.
    • (1992) EMBO J , vol.11 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 23
    • 0027136213 scopus 로고
    • Characterization of the Neisseria Igaβ-core. The essential unit for outer membrane targeting and extracellular protein secretion
    • Klauser, T., Krämer, J., Otzelberger, K., Pohlner, J., and Meyer, T.F. (1993) Characterization of the Neisseria Igaβ-core. The essential unit for outer membrane targeting and extracellular protein secretion. J Mol Biol 234: 579-593.
    • (1993) J Mol Biol , vol.234 , pp. 579-593
    • Klauser, T.1    Krämer, J.2    Otzelberger, K.3    Pohlner, J.4    Meyer, T.F.5
  • 24
    • 0028073310 scopus 로고
    • An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments
    • Knappik, A., and Plückthun, A. (1994) An improved affinity tag based on the FLAG peptide for the detection and purification of recombinant antibody fragments. Biotechniques 17: 754-761.
    • (1994) Biotechniques , vol.17 , pp. 754-761
    • Knappik, A.1    Plückthun, A.2
  • 25
    • 0031035521 scopus 로고    scopus 로고
    • Specific detection of His-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv fusions
    • Lindner, P., Bauer, K., Krebber, A., Nieba, L., Kremmer, E., Krebber, C., et al. (1997) Specific detection of His-tagged proteins with recombinant anti-His tag scFv-phosphatase or scFv fusions. Biotechniques 22: 140-149.
    • (1997) Biotechniques , vol.22 , pp. 140-149
    • Lindner, P.1    Bauer, K.2    Krebber, A.3    Nieba, L.4    Kremmer, E.5    Krebber, C.6
  • 26
    • 0028911149 scopus 로고
    • Comparative characterization of the iga gene encoding IgA1 protease in Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae
    • Lomholt, H., Poulsen, K., and Kilian, M. (1995) Comparative characterization of the iga gene encoding IgA1 protease in Neisseria meningitidis, Neisseria gonorrhoeae and Haemophilus influenzae. Mol Microbiol 15: 495-506.
    • (1995) Mol Microbiol , vol.15 , pp. 495-506
    • Lomholt, H.1    Poulsen, K.2    Kilian, M.3
  • 27
    • 0031988031 scopus 로고    scopus 로고
    • Secretion of proteins and assembly of bacteral surface organelles: Shared pathways of extracellular protein targeting
    • Lory S (1998) Secretion of proteins and assembly of bacteral surface organelles: shared pathways of extracellular protein targeting. Curr Opin Microbiol 1: 27-35.
    • (1998) Curr Opin Microbiol , vol.1 , pp. 27-35
    • Lory, S.1
  • 29
    • 0029765609 scopus 로고    scopus 로고
    • New components of protein folding in extracytoplasmic compartments of Esccherichia coli SurA, FkpA and Skp/OmpH
    • Missiakas, D., Betton, J.M., and Raina, S. (1996). New components of protein folding in extracytoplasmic compartments of Esccherichia coli SurA, FkpA and Skp/OmpH. Mol Microbiol 21: 871-884.
    • (1996) Mol Microbiol , vol.21 , pp. 871-884
    • Missiakas, D.1    Betton, J.M.2    Raina, S.3
  • 30
    • 0028298380 scopus 로고
    • Isolation of outer membranes
    • Nikaido, H. (1994a) Isolation of outer membranes. Methods Enzymol 235: 225-234.
    • (1994) Methods Enzymol , vol.235 , pp. 225-234
    • Nikaido, H.1
  • 31
    • 0028025336 scopus 로고
    • Porins and specific diffusion channels in acterial outer membranes
    • Nikaido, H. (1994b) Porins and specific diffusion channels in acterial outer membranes. J Biol Chem 269: 3905-3908.
    • (1994) J Biol Chem , vol.269 , pp. 3905-3908
    • Nikaido, H.1
  • 32
    • 0015523228 scopus 로고
    • Mechanism of assembly of the outer membrane of Salmenella typhimurium
    • Osborn, M.J., Gander, J.E., Parisi, E., and Carson, J. (1972) Mechanism of assembly of the outer membrane of Salmenella typhimurium. J Biol Chem 247: 3962-3972.
    • (1972) J Biol Chem , vol.247 , pp. 3962-3972
    • Osborn, M.J.1    Gander, J.E.2    Parisi, E.3    Carson, J.4
  • 33
    • 0026668342 scopus 로고
    • Characterization of a periplasmic thiol: Disulfide Interchange protein required or the functional maturation of secreted virulence factors of Vibro cholerae
    • Peek, J.A., and Taylor, R.K. (1992) Characterization of a periplasmic thiol: disulfide Interchange protein required or the functional maturation of secreted virulence factors of Vibro cholerae. Proc Natl Acad Sci USA 89: 6210-6214.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6210-6214
    • Peek, J.A.1    Taylor, R.K.2
  • 34
    • 0003046374 scopus 로고    scopus 로고
    • Producing antibodies in Ischerichia coli: From PCR to fermentation
    • McCafferty, J., and Hoogenboom, H.R. (eds). Oxford: IRL Press
    • Plüchthun, A., Krebber, C., Krebber, U., Horn, U., Knüpfer, J., Wenderoth, R., et al. (1996). Producing antibodies in Ischerichia coli: from PCR to fermentation. In Antibody Engineering: a Practical Approach. McCafferty, J., and Hoogenboom, H.R. (eds). Oxford: IRL Press, pp. 203-252.
    • (1996) Antibody Engineering: A Practical Approach , pp. 203-252
    • Plüchthun, A.1    Krebber, C.2    Krebber, U.3    Horn, U.4    Knüpfer, J.5    Wenderoth, R.6
  • 35
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoea IgA protease
    • Pohlner, J., Halter, R., Beyreuther, K., and Meyer, T.F. (1987) Gene structure and extracellular secretion of Neisseria gonorrhoea IgA protease. Nature 325: 458-462.
    • (1987) Nature , vol.325 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 36
    • 0027450561 scopus 로고
    • The complete general secretory pathway in Gram-negative bacteria
    • Puasley, A.P. (1993) The complete general secretory pathway in Gram-negative bacteria. Microbiol Rev 57:50-108.
    • (1993) Microbiol Rev , vol.57 , pp. 50-108
    • Puasley, A.P.1
  • 37
    • 0031018135 scopus 로고    scopus 로고
    • Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells
    • Quintela, J.C., Pedro, M.A.D., Zöllner, P., Allmaier, G., and Portillo, F.G.-D. (1997) Peptidoglycan structure of Salmonella typhimurium growing within cultured mammalian cells. Mol Microbiol 23: 693-704.
    • (1997) Mol Microbiol , vol.23 , pp. 693-704
    • Quintela, J.C.1    Pedro, M.A.D.2    Zöllner, P.3    Allmaier, G.4    Portillo, F.G.-D.5
  • 38
    • 0030765627 scopus 로고    scopus 로고
    • Making and breaking disulfide bonds
    • Raina, S., and Missiakas, D. (1997) Making and breaking disulfide bonds. Annu Rev Microbiol 51: 179-202.
    • (1997) Annu Rev Microbiol , vol.51 , pp. 179-202
    • Raina, S.1    Missiakas, D.2
  • 39
    • 0023901061 scopus 로고
    • Three-dimensional structure of cholera toxin penetrating a lipid membrane
    • Ribi, H.O., Ludwig, D.S., Mercer, K.L., Schoolnik, G.K., and Kornberg, R.D. (1988) Three-dimensional structure of cholera toxin penetrating a lipid membrane. Science 239: 1272-1276.
    • (1988) Science , vol.239 , pp. 1272-1276
    • Ribi, H.O.1    Ludwig, D.S.2    Mercer, K.L.3    Schoolnik, G.K.4    Kornberg, R.D.5
  • 40
    • 0032511192 scopus 로고    scopus 로고
    • Macromolecular assembly and secretion across the bacterial cell envelope: Type II secretion systems
    • Russel, M. (1998) Macromolecular assembly and secretion across the bacterial cell envelope: type II secretion systems. J Mol Biol 279: 485-499.
    • (1998) J Mol Biol , vol.279 , pp. 485-499
    • Russel, M.1
  • 41
    • 0027506049 scopus 로고
    • A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholera
    • Sandkvist, M., Morales, V., and Bagdasarian, M. (1993) A protein required for secretion of cholera toxin through the outer membrane of Vibrio cholera. Gene 123: 81-86.
    • (1993) Gene , vol.123 , pp. 81-86
    • Sandkvist, M.1    Morales, V.2    Bagdasarian, M.3
  • 42
    • 0014879933 scopus 로고
    • Protein composition of the cell wall and cytoplasmic membrane of E. coli
    • Schnaitman, C.A. (1970) Protein composition of the cell wall and cytoplasmic membrane of E. coli. J Bacteriol 890: 890-901.
    • (1970) J Bacteriol , vol.890 , pp. 890-901
    • Schnaitman, C.A.1
  • 43
    • 0015133176 scopus 로고
    • Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli
    • Schnaitman, C.A. (1971a) Effect of ethylenediaminetetraacetic acid, Triton X-100, and lysozyme on the morphology and chemical composition of isolate cell walls of Escherichia coli. J Bacteriol 108: 553-563.
    • (1971) J Bacteriol , vol.108 , pp. 553-563
    • Schnaitman, C.A.1
  • 44
    • 0015132002 scopus 로고
    • Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100
    • Schnaitman, C.A. (1971b) Solubilization of the cytoplasmic membrane of Escherichia coli by Triton X-100. J Bacteriol 108: 545-552.
    • (1971) J Bacteriol , vol.108 , pp. 545-552
    • Schnaitman, C.A.1
  • 45
    • 0016696744 scopus 로고
    • Outer membrane of Salmonella typhimurium: Chemical analysis and freeze-fracture studied with lipopolysaccharide mutants
    • Smit, J., Kamio, Y., and Nikaido, H. (1975) Outer membrane of Salmonella typhimurium: chemical analysis and freeze-fracture studied with lipopolysaccharide mutants. J Bacteriol 124: 942-958.
    • (1975) J Bacteriol , vol.124 , pp. 942-958
    • Smit, J.1    Kamio, Y.2    Nikaido, H.3
  • 46
    • 0027385590 scopus 로고
    • Structure-function and biogenesis of type IV pili
    • Strom, M., and Low, S. (1993) Structure-function and biogenesis of type IV pili. Annu Rev Microbiol 47: 565-596.
    • (1993) Annu Rev Microbiol , vol.47 , pp. 565-596
    • Strom, M.1    Low, S.2
  • 47
    • 0029101962 scopus 로고
    • Molecular dissection of PapD interaction with PapG reveals two chaperone-binding sites
    • Xu, Z., Jones, C.H., Haslem, D., Pinkner, J.S., Dodson, K., Kihlberg, J., et al. (1995) Molecular dissection of PapD interaction with PapG reveals two chaperone-binding sites. Mol Microbiol 16: 1011-1020.
    • (1995) Mol Microbiol , vol.16 , pp. 1011-1020
    • Xu, Z.1    Jones, C.H.2    Haslem, D.3    Pinkner, J.S.4    Dodson, K.5    Kihlberg, J.6
  • 48
    • 0021943518 scopus 로고
    • Improved M13 phage cloning vectors and hosts strains: Nucleotide sequences of the M13mp18 and pU19 vectors
    • Yanisch-Perron, C., Vieira, J., and Messing, J. (1985) Improved M13 phage cloning vectors and hosts strains: nucleotide sequences of the M13mp18 and pU19 vectors. Gene 33: 103-119.
    • (1985) Gene , vol.33 , pp. 103-119
    • Yanisch-Perron, C.1    Vieira, J.2    Messing, J.3
  • 49
    • 0026633141 scopus 로고
    • A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae
    • Yu, J., Weeb, H., and Hirst, T.R. (1992) A homologue of the Escherichia coli DsbA protein involved in disulphide bond formation is required for enterotoxin biogenesis in Vibrio cholerae. Mol Microbiol 6: 1949-1958.
    • (1992) Mol Microbiol , vol.6 , pp. 1949-1958
    • Yu, J.1    Weeb, H.2    Hirst, T.R.3
  • 50
    • 0029774730 scopus 로고    scopus 로고
    • DsbA is required for stability of the type IV pilus of enteropathogenic Escherichia coli
    • Zhang, H.Z., and Donnenberg, M.S. (1996) DsbA is required for stability of the type IV pilus of enteropathogenic Escherichia coli. Mol Microbiol 21: 787-797.
    • (1996) Mol Microbiol , vol.21 , pp. 787-797
    • Zhang, H.Z.1    Donnenberg, M.S.2


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