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Volumn 73, Issue 7, 2005, Pages 3851-3859

Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface

Author keywords

[No Author keywords available]

Indexed keywords

ADHESIN; AUTOTRANSPORTER ADHESIN INVOLVED IN DIFFUSE ADHERENCE PROTEIN; CARRIER PROTEIN; DIMER; HYBRID PROTEIN; MONOMER; OLIGOMER; OUTER MEMBRANE PROTEIN; OUTER MEMBRANE PROTEIN OMP85; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 21544468024     PISSN: 00199567     EISSN: None     Source Type: Journal    
DOI: 10.1128/IAI.73.7.3851-3859.2005     Document Type: Article
Times cited : (24)

References (43)
  • 1
    • 0024517699 scopus 로고
    • Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli
    • Benz, I., and M. A. Schmidt. 1989. Cloning and expression of an adhesin (AIDA-I) involved in diffuse adherence of enteropathogenic Escherichia coli. Infect. Immun. 57:1506-1511.
    • (1989) Infect. Immun. , vol.57 , pp. 1506-1511
    • Benz, I.1    Schmidt, M.A.2
  • 2
    • 0026742008 scopus 로고
    • AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule
    • Benz, I., and M. A. Schmidt. 1992. AIDA-I, the adhesin involved in diffuse adherence of the diarrhoeagenic Escherichia coli strain 2787 (O126:H27), is synthesized via a precursor molecule. Mol. Microbiol. 6:1539-1546.
    • (1992) Mol. Microbiol. , vol.6 , pp. 1539-1546
    • Benz, I.1    Schmidt, M.A.2
  • 3
    • 0026558312 scopus 로고
    • Isolation and serologic characterization of AIDA-I, the adhesin mediating the diffuse adherence phenotype of the diarrhea-associated Escherichia coli strain 2787 (O126:H27)
    • Benz, I., and M. A. Schmidt. 1992. Isolation and serologic characterization of AIDA-I, the adhesin mediating the diffuse adherence phenotype of the diarrhea-associated Escherichia coli strain 2787 (O126:H27). Infect. Immun. 60:13-18.
    • (1992) Infect. Immun. , vol.60 , pp. 13-18
    • Benz, I.1    Schmidt, M.A.2
  • 4
    • 0034939563 scopus 로고    scopus 로고
    • Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin
    • Benz, I., and M. A. Schmidt. 2001. Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin. Mol. Microbiol. 40:1403-1413.
    • (2001) Mol. Microbiol. , vol.40 , pp. 1403-1413
    • Benz, I.1    Schmidt, M.A.2
  • 5
    • 0036067107 scopus 로고    scopus 로고
    • Never say never again: Protein glycosylation in pathogenic bacteria
    • Benz, I., and M. A. Schmidt. 2003. Never say never again: protein glycosylation in pathogenic bacteria. Mol. Microbiol. 45:267-276.
    • (2003) Mol. Microbiol. , vol.45 , pp. 267-276
    • Benz, I.1    Schmidt, M.A.2
  • 6
    • 21544482703 scopus 로고    scopus 로고
    • The AIDA system-the bacterial AIDA autotransporter as a presentation module for the development of live oral vaccines
    • Benz, I., D. Tapadar, C. Buddenborg, T. Voß, and M. A. Schmidt. 2003. The AIDA system-the bacterial AIDA autotransporter as a presentation module for the development of live oral vaccines. BIOforum Eur. 6:335-337.
    • (2003) BIOforum Eur. , vol.6 , pp. 335-337
    • Benz, I.1    Tapadar, D.2    Buddenborg, C.3    Voß, T.4    Schmidt, M.A.5
  • 7
    • 0036892189 scopus 로고    scopus 로고
    • Invasion activity of a Mycobacterium tuberculosis peptide presented by the Escherichia coli AIDA autotransporter
    • Casali, N., M. Konieczny, M. A. Schmidt, and L. W. Riley. 2002. Invasion activity of a Mycobacterium tuberculosis peptide presented by the Escherichia coli AIDA autotransporter. Infect. Immun. 70:6846-6852.
    • (2002) Infect. Immun. , vol.70 , pp. 6846-6852
    • Casali, N.1    Konieczny, M.2    Schmidt, M.A.3    Riley, L.W.4
  • 8
    • 0043073264 scopus 로고    scopus 로고
    • Folding of a monomeric porin, OmpG, in detergent solution
    • Conlan, S., and H. Bayley. 2003. Folding of a monomeric porin, OmpG, in detergent solution. Biochemistry 42:9453-9465.
    • (2003) Biochemistry , vol.42 , pp. 9453-9465
    • Conlan, S.1    Bayley, H.2
  • 9
    • 0027328751 scopus 로고
    • Bacterial porins: Lessons from three high-resolution structures
    • Cowan, S. W. 1993. Bacterial porins: lessons from three high-resolution structures. Curr. Opin. Struct. Biol. 3:501-507.
    • (1993) Curr. Opin. Struct. Biol. , vol.3 , pp. 501-507
    • Cowan, S.W.1
  • 12
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • Henderson, I. R., F. Navarro-Garcia, and J. P. Nataro. 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
  • 13
    • 0035111746 scopus 로고    scopus 로고
    • Virulence functions of autotransporter proteins
    • Henderson, I. R., and J. P. Nataro. 2001. Virulence functions of autotransporter proteins. Infect. Immun. 69:1231-1243.
    • (2001) Infect. Immun. , vol.69 , pp. 1231-1243
    • Henderson, I.R.1    Nataro, J.P.2
  • 15
    • 0035802127 scopus 로고    scopus 로고
    • Functional display of active bovine adrenodoxin on the surface of E. coli by chemical incorporation of the [2Fe-2S] cluster
    • Jose, J., R. Bernhardt, and F. Hannemann. 2001. Functional display of active bovine adrenodoxin on the surface of E. coli by chemical incorporation of the [2Fe-2S] cluster. ChemBioChem 2:695-701.
    • (2001) ChemBioChem , vol.2 , pp. 695-701
    • Jose, J.1    Bernhardt, R.2    Hannemann, F.3
  • 16
    • 0037161614 scopus 로고    scopus 로고
    • Cellular surface display of dimeric Adx and whole cell P450-mediated steroid synthesis on E. coli
    • Jose, J., R. Bernhardt, and F. Hannemann. 2002. Cellular surface display of dimeric Adx and whole cell P450-mediated steroid synthesis on E. coli. J. Biotechnol. 95:257-268.
    • (2002) J. Biotechnol. , vol.95 , pp. 257-268
    • Jose, J.1    Bernhardt, R.2    Hannemann, F.3
  • 17
    • 3242687055 scopus 로고    scopus 로고
    • Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars
    • Jose, J., and S. von Schwichow. 2004. Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars. ChemBioChem 5:491-499.
    • (2004) ChemBioChem , vol.5 , pp. 491-499
    • Jose, J.1    Von Schwichow, S.2
  • 18
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: Conformation-dependent outer membrane translocation
    • Klauser, T., J. Pohlner, and T. F. Meyer. 1990. Extracellular transport of cholera toxin B subunit using Neisseria IgA protease β-domain: conformation-dependent outer membrane translocation. EMBO J. 11:2327-2335.
    • (1990) EMBO J. , vol.11 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 19
    • 0027136213 scopus 로고
    • Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion
    • Klauser, T., J. Kramer, K. Otzelberger, J. Pohlner, and T. F. Meyer. 1993. Characterization of the Neisseria Iga beta-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    Kramer, J.2    Otzelberger, K.3    Pohlner, J.4    Meyer, T.F.5
  • 20
    • 0027751445 scopus 로고
    • The secretion pathway of IgA protease-type proteins in Gram-negative bacteria
    • Klauser, T., J. Pohlner, and T. F. Meyer. 1993. The secretion pathway of IgA protease-type proteins in Gram-negative bacteria. Bioessays 15:799-805.
    • (1993) Bioessays , vol.15 , pp. 799-805
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 22
    • 21544478197 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Münster, Münster, Germany
    • Konieczny, M. P. J. 1999. Ph.D. thesis. University of Münster, Münster, Germany.
    • (1999)
    • Konieczny, M.P.J.1
  • 23
    • 0034015838 scopus 로고    scopus 로고
    • Cell surface presentation of recombinant (poly-)peptides including functional T cell epitopes by the AIDA autotransporter system
    • Konieczny, M. P. J., M. Suhr, A. Noll, I. B. Autenrieth, and M. A. Schmidt. 2000. Cell surface presentation of recombinant (poly-)peptides including functional T cell epitopes by the AIDA autotransporter system. FEMS Immunol. Med. Microbiol. 27:321-332.
    • (2000) FEMS Immunol. Med. Microbiol. , vol.27 , pp. 321-332
    • Konieczny, M.P.J.1    Suhr, M.2    Noll, A.3    Autenrieth, I.B.4    Schmidt, M.A.5
  • 24
    • 0035173780 scopus 로고    scopus 로고
    • Modular organization of the AIDA autotransporter translocator: The N-terminal β1-domain is surface-exposed and stabilizes the transmembrane β2-domain
    • Konieczny, M. P. J., I. Benz, B. Hollinderbäumer, C. Beinke, M. Niederweis, and M. A. Schmidt. 2001. Modular organization of the AIDA autotransporter translocator: the N-terminal β1-domain is surface-exposed and stabilizes the transmembrane β2-domain. Antonie Leeuwenhoek 80:19-34.
    • (2001) Antonie Leeuwenhoek , vol.80 , pp. 19-34
    • Konieczny, M.P.J.1    Benz, I.2    Hollinderbäumer, B.3    Beinke, C.4    Niederweis, M.5    Schmidt, M.A.6
  • 25
    • 0035161265 scopus 로고    scopus 로고
    • The AIDA autotransporter system is associated with F18 and stx2e in Escherichia coli isolates from pigs diagnosed with edema disease and postweaning diarrhea
    • Niewerth, U., A. Frey, T. Voss, C. Le Bouguénec, G. Baljer, S. Franke, and M. A. Schmidt. 2001. The AIDA autotransporter system is associated with F18 and stx2e in Escherichia coli isolates from pigs diagnosed with edema disease and postweaning diarrhea. Clin. Diagn. Lab. Immunol. 8:143-149.
    • (2001) Clin. Diagn. Lab. Immunol. , vol.8 , pp. 143-149
    • Niewerth, U.1    Frey, A.2    Voss, T.3    Le Bouguénec, C.4    Baljer, G.5    Franke, S.6    Schmidt, M.A.7
  • 26
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of outer membrane permeability revisited
    • Nikaido, H. 2003. Molecular basis of outer membrane permeability revisited. Microbiol. Mol. Biol. Rev. 67:593-656.
    • (2003) Microbiol. Mol. Biol. Rev. , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 27
    • 0037224652 scopus 로고    scopus 로고
    • Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter
    • Oliver, D. C., G. Huang, and R. C. Fernandez. 2003. Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter. J. Bacteriol. 185:489-495.
    • (2003) J. Bacteriol. , vol.185 , pp. 489-495
    • Oliver, D.C.1    Huang, G.2    Fernandez, R.C.3
  • 28
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver, D. C., G. Huang, E. Nodel, S. Pleacance, and R. C. Fernandez. 2003. A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol. Microbiol. 47:1367-1383.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleacance, S.4    Fernandez, R.C.5
  • 31
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner, J., R. Halter, K. Beyreuther, and T. F. Meyer. 1987. Gene structure and extracellular secretion of Neisseria gonorrhoeae 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
  • 32
    • 0031857538 scopus 로고    scopus 로고
    • General and specific porins from bacterial outer membranes
    • Schirmer, T. 1997. General and specific porins from bacterial outer membranes. J. Struct. Biol. 121:101-109.
    • (1997) J. Struct. Biol. , vol.121 , pp. 101-109
    • Schirmer, T.1
  • 33
    • 0345059167 scopus 로고    scopus 로고
    • Sweet new world: Glycoproteins in bacterial pathogens
    • Schmidt, M. A., L. W. Riley, and I. Benz. 2003. Sweet new world: glycoproteins in bacterial pathogens. Trends Microbiol. 11:554-561.
    • (2003) Trends Microbiol. , vol.11 , pp. 554-561
    • Schmidt, M.A.1    Riley, L.W.2    Benz, I.3
  • 34
    • 0037064291 scopus 로고    scopus 로고
    • The structure of bacterial outer membrane proteins
    • Schulz, G. E. 2002. The structure of bacterial outer membrane proteins. Biochim. Biophys. Acta 1565:308-317.
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 308-317
    • Schulz, G.E.1
  • 35
    • 0033932639 scopus 로고    scopus 로고
    • Barrel membrane proteins
    • Schulz, G. E. 2000. β-Barrel membrane proteins. Curr. Opin. Struct. Biol. 10:443-447.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 443-447
    • Schulz, G.E.1
  • 36
    • 0025141624 scopus 로고
    • In vitro trimerization of OmpF porin secreted by spheroblasts of Escherichia coli
    • Sen, K., and H. Nikaido. 1990. In vitro trimerization of OmpF porin secreted by spheroblasts of Escherichia coli. Proc. Natl. Acad. Sci. USA 87:743-747.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 743-747
    • Sen, K.1    Nikaido, H.2
  • 37
    • 0037799238 scopus 로고    scopus 로고
    • Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein
    • Sijbrandi, R., M. L. Urbanus, C. M. ten Hagen-Jongman, H. D. Bernstein, B. Oudega, B. R. Otto, and J. Luirink. 2003. Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein. J. Biol. Chem. 278:4654-4659.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4654-4659
    • Sijbrandi, R.1    Urbanus, M.L.2    Ten Hagen-Jongman, C.M.3    Bernstein, H.D.4    Oudega, B.5    Otto, B.R.6    Luirink, J.7
  • 38
    • 21544436165 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Münster, Münster, Germany
    • Suhr, M. 1998. Ph.D. thesis. University of Münster, Münster, Germany.
    • (1998)
    • Suhr, M.1
  • 39
    • 0029846536 scopus 로고    scopus 로고
    • Processing of the AIDA-I precursor: Removal of AIDAc and evidence for the outer membrane anchoring as a β-barrel structure
    • Suhr, M., I. Benz, and M. A. Schmidt. 1996. Processing of the AIDA-I precursor: removal of AIDAc and evidence for the outer membrane anchoring as a β-barrel structure. Mol. Microbiol. 22:31-42.
    • (1996) Mol. Microbiol. , vol.22 , pp. 31-42
    • Suhr, M.1    Benz, I.2    Schmidt, M.A.3
  • 40
    • 2442507008 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia autotransporter contains an unusually short, trimeric translocator domain
    • Surana, N. K., D. Cutter, S. J. Barenkamp, and J. W. St Geme 3rd. 2004. The Haemophilus influenzae Hia autotransporter contains an unusually short, trimeric translocator domain. J. Biol. Chem. 279:14679-14685.
    • (2004) J. Biol. Chem. , vol.279 , pp. 14679-14685
    • Surana, N.K.1    Cutter, D.2    Barenkamp, S.J.3    St. Geme III, J.W.4
  • 41
    • 21544469288 scopus 로고    scopus 로고
    • Ph.D. thesis. University of Münster, Münster, Germany
    • Tapadar, D. 2004. Ph.D. thesis. University of Münster, Münster, Germany.
    • (2004)
    • Tapadar, D.1
  • 42
    • 0032854025 scopus 로고    scopus 로고
    • Probing secretion and translocation of a β-autotransporter using a reporter single-chain Fv as a cognate passenger domain
    • Veiga, E., V. de Lorenzo, and L. A. Fernández. 1999. Probing secretion and translocation of a β-autotransporter using a reporter single-chain Fv as a cognate passenger domain. Mol. Microbiol. 33:1232-12443.
    • (1999) Mol. Microbiol. , vol.33 , pp. 1232-12443
    • Veiga, E.1    De Lorenzo, V.2    Fernández, L.A.3
  • 43
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga, E., E. Sugawara, H. Nikaido, V. de Lorenzo, and L. A. Fernández. 2002. Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. EMBO J. 9:2122-2131.
    • (2002) EMBO J. , vol.9 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    De Lorenzo, V.4    Fernández, L.A.5


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