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Volumn 5, Issue , 2006, Pages

Surface display of proteins by Gram-negative bacterial autotransporters

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; PEPTIDE LIBRARY; POLYPEPTIDE; SIGNAL PEPTIDE;

EID: 33747120540     PISSN: 14752859     EISSN: 14752859     Source Type: Journal    
DOI: 10.1186/1475-2859-5-22     Document Type: Review
Times cited : (39)

References (116)
  • 1
    • 0037212403 scopus 로고    scopus 로고
    • Microbial cell-surface display
    • Lee SY, Choi JH, Xu Z: Microbial cell-surface display. Trends Biotechnol 2003, 21(1):45-52.
    • (2003) Trends Biotechnol , vol.21 , Issue.1 , pp. 45-52
    • Lee, S.Y.1    Choi, J.H.2    Xu, Z.3
  • 3
    • 0344837302 scopus 로고    scopus 로고
    • Autodisplay: Development of an efficacious system for surface display of antigenic determinants in Salmonella vaccine strains
    • Kramer U, Rizos K, Apfel H, Autenrieth IB, Lattemann CT: Autodisplay: development of an efficacious system for surface display of antigenic determinants in Salmonella vaccine strains. Infect Immun 2003, 71(4):1944-1952.
    • (2003) Infect Immun , vol.71 , Issue.4 , pp. 1944-1952
    • Kramer, U.1    Rizos, K.2    Apfel, H.3    Autenrieth, I.B.4    Lattemann, C.T.5
  • 4
    • 31144465702 scopus 로고    scopus 로고
    • Autodisplay: Efficient bacterial surface display of recombinant proteins
    • Jose J: Autodisplay: efficient bacterial surface display of recombinant proteins. Appl Microbiol Biotechnol 2006, 69(6):607-614.
    • (2006) Appl Microbiol Biotechnol , vol.69 , Issue.6 , pp. 607-614
    • Jose, J.1
  • 5
    • 3242687055 scopus 로고    scopus 로고
    • Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars
    • Jose J, von Schwichow S: Autodisplay of active sorbitol dehydrogenase (SDH) yields a whole cell biocatalyst for the synthesis of rare sugars. Chembiochem 2004, 5(4):491-499.
    • (2004) Chembiochem , vol.5 , Issue.4 , pp. 491-499
    • Jose, J.1    von Schwichow, S.2
  • 6
    • 0037161614 scopus 로고    scopus 로고
    • Cellular surface display of dimeric Adx and whole cell P450-mediated steroid synthesis on E. coli
    • Jose J, Bernhardt R, Hannemann F: Cellular surface display of dimeric Adx and whole cell P450-mediated steroid synthesis on E. coli. J Biotechnol 2002, 95(3):257-268.
    • (2002) J Biotechnol , vol.95 , Issue.3 , pp. 257-268
    • Jose, J.1    Bernhardt, R.2    Hannemann, F.3
  • 7
    • 0034045457 scopus 로고    scopus 로고
    • Engineering a mouse metallothionein on the cell surface of Ralstonia eutropha CH34 for immobilization of heavy metals in soil
    • Valls M, Atrian S, de Lorenzo V, Fernandez LA: Engineering a mouse metallothionein on the cell surface of Ralstonia eutropha CH34 for immobilization of heavy metals in soil. Nat Biotechnol 2000, 18(6):661-665.
    • (2000) Nat Biotechnol , vol.18 , Issue.6 , pp. 661-665
    • Valls, M.1    Atrian, S.2    de Lorenzo, V.3    Fernandez, L.A.4
  • 8
    • 0037026254 scopus 로고    scopus 로고
    • Cell-Surface display of heterologous proteins: From high-throughput screening to environmental applications
    • Chen W, Georgiou G: Cell-Surface display of heterologous proteins: From high-throughput screening to environmental applications. Biotechnol Bioeng 2002, 79(5):496-503.
    • (2002) Biotechnol Bioeng , vol.79 , Issue.5 , pp. 496-503
    • Chen, W.1    Georgiou, G.2
  • 9
    • 0033597789 scopus 로고    scopus 로고
    • Sequence requirements of the GPNG beta-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening
    • Wentzel A, Christmann A, Kratzner R, Kolmar H: Sequence requirements of the GPNG beta-turn of the Ecballium elaterium trypsin inhibitor II explored by combinatorial library screening. J Biol Chem 1999, 274(30):21037-21043.
    • (1999) J Biol Chem , vol.274 , Issue.30 , pp. 21037-21043
    • Wentzel, A.1    Christmann, A.2    Kratzner, R.3    Kolmar, H.4
  • 10
    • 33645049557 scopus 로고    scopus 로고
    • Protein cell surface display in Gram-positive bacteria: From single protein to macromolecular protein structure
    • Desvaux M, Dumas E, Chafsey I, Hebraud M: Protein cell surface display in Gram-positive bacteria: from single protein to macromolecular protein structure. FEMS Microbiol Lett 2006, 256(1):1-15.
    • (2006) FEMS Microbiol Lett , vol.256 , Issue.1 , pp. 1-15
    • Desvaux, M.1    Dumas, E.2    Chafsey, I.3    Hebraud, M.4
  • 11
    • 0242320522 scopus 로고    scopus 로고
    • The bacterial translocase: A dynamic protein channel complex
    • de Keyzer J, van der Does C, Driessen AJ: The bacterial translocase: a dynamic protein channel complex. Cell Mol Life Sci 2003, 60(10):2034-2052.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.10 , pp. 2034-2052
    • de Keyzer, J.1    van der Does, C.2    Driessen, A.J.3
  • 12
    • 16244380460 scopus 로고    scopus 로고
    • Export of complex cofactor-containing proteins by the bacterial Tat pathway
    • Palmer T, Sargent F, Berks BC: Export of complex cofactor-containing proteins by the bacterial Tat pathway. Trends Microbiol 2005, 13(4):175-180.
    • (2005) Trends Microbiol , vol.13 , Issue.4 , pp. 175-180
    • Palmer, T.1    Sargent, F.2    Berks, B.C.3
  • 13
    • 0037428132 scopus 로고    scopus 로고
    • Role of a highly conserved bacterial protein in outer membrane protein assembly
    • Voulhoux R, Bos MP, Geurtsen J, Mols M, Tommassen J: Role of a highly conserved bacterial protein in outer membrane protein assembly. Science 2003, 299(5604):262-265.
    • (2003) Science , vol.299 , Issue.5604 , pp. 262-265
    • Voulhoux, R.1    Bos, M.P.2    Geurtsen, J.3    Mols, M.4    Tommassen, J.5
  • 14
    • 17444381980 scopus 로고    scopus 로고
    • Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli
    • Wu T, Malinverni J, Ruiz N, Kim S, Silhavy TJ, Kahne D: Identification of a multicomponent complex required for outer membrane biogenesis in Escherichia coli. Cell 2005, 121(2):235-245.
    • (2005) Cell , vol.121 , Issue.2 , pp. 235-245
    • Wu, T.1    Malinverni, J.2    Ruiz, N.3    Kim, S.4    Silhavy, T.J.5    Kahne, D.6
  • 15
    • 0022814620 scopus 로고
    • Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; expression at the cell surface
    • Charbit A, Boulain JC, Ryter A, Hofnung M: Probing the topology of a bacterial membrane protein by genetic insertion of a foreign epitope; expression at the cell surface. Embo J 1986, 5(11):3029-3037.
    • (1986) Embo J , vol.5 , Issue.11 , pp. 3029-3037
    • Charbit, A.1    Boulain, J.C.2    Ryter, A.3    Hofnung, M.4
  • 16
    • 0023042026 scopus 로고
    • Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12
    • Freudl R, MacIntyre S, Degen M, Henning U: Cell surface exposure of the outer membrane protein OmpA of Escherichia coli K-12. J Mol Biol 1986, 188(3):491-494.
    • (1986) J Mol Biol , vol.188 , Issue.3 , pp. 491-494
    • Freudl, R.1    MacIntyre, S.2    Degen, M.3    Henning, U.4
  • 17
    • 0023520878 scopus 로고
    • Use of outer membrane protein PhoE as a carrier for the transport of a foreign antigenic determinant to the cell surface of Escherichia coli K-12
    • Agterberg M, Adriaanse H, Tommassen J: Use of outer membrane protein PhoE as a carrier for the transport of a foreign antigenic determinant to the cell surface of Escherichia coli K-12. Gene 1987, 59(1):145-150.
    • (1987) Gene , vol.59 , Issue.1 , pp. 145-150
    • Agterberg, M.1    Adriaanse, H.2    Tommassen, J.3
  • 18
    • 0344560614 scopus 로고    scopus 로고
    • Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif
    • Xu Z, Lee SY: Display of polyhistidine peptides on the Escherichia coli cell surface by using outer membrane protein C as an anchoring motif. Appl Environ Microbiol 1999, 65(11):5142-5147.
    • (1999) Appl Environ Microbiol , vol.65 , Issue.11 , pp. 5142-5147
    • Xu, Z.1    Lee, S.Y.2
  • 19
    • 0344096509 scopus 로고    scopus 로고
    • Expression of foreign antigens on the surface of Escherichia coli by fusion to the outer membrane protein tra T
    • Chang HJ, Sheu SY, Lo SJ: Expression of foreign antigens on the surface of Escherichia coli by fusion to the outer membrane protein tra T. J Biomed Sci 1999, 6(1):64-70.
    • (1999) J Biomed Sci , vol.6 , Issue.1 , pp. 64-70
    • Chang, H.J.1    Sheu, S.Y.2    Lo, S.J.3
  • 20
    • 0035174836 scopus 로고    scopus 로고
    • Bacterial phage receptors, versatile tools for display of polypeptides on the cell surface
    • Etz H, Minh DB, Schellack C, Nagy E, Meinke A: Bacterial phage receptors, versatile tools for display of polypeptides on the cell surface. J Bacteriol 2001, 183(23):6924-6935.
    • (2001) J Bacteriol , vol.183 , Issue.23 , pp. 6924-6935
    • Etz, H.1    Minh, D.B.2    Schellack, C.3    Nagy, E.4    Meinke, A.5
  • 21
    • 0035212525 scopus 로고    scopus 로고
    • Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA
    • Wentzel A, Christmann A, Adams T, Kolmar H: Display of passenger proteins on the surface of Escherichia coli K-12 by the enterohemorrhagic E. coli intimin EaeA. J Bacteriol 2001, 183(24):7273-7284.
    • (2001) J Bacteriol , vol.183 , Issue.24 , pp. 7273-7284
    • Wentzel, A.1    Christmann, A.2    Adams, T.3    Kolmar, H.4
  • 22
    • 0031863713 scopus 로고    scopus 로고
    • Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae
    • Jung HC, Lebeault JM, Pan JG: Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat Biotechnol 1998, 16(6):576-580.
    • (1998) Nat Biotechnol , vol.16 , Issue.6 , pp. 576-580
    • Jung, H.C.1    Lebeault, J.M.2    Pan, J.G.3
  • 23
    • 0033861792 scopus 로고    scopus 로고
    • Peptide display on bacterial flagella: Principles and applications
    • Westerlund-Wikstrom B: Peptide display on bacterial flagella: principles and applications. Int J Med Microbiol 2000, 290(3):223-230.
    • (2000) Int J Med Microbiol , vol.290 , Issue.3 , pp. 223-230
    • Westerlund-Wikstrom, B.1
  • 24
    • 0030841922 scopus 로고    scopus 로고
    • Authentic display of a cholera toxin epitope by chimeric type I fimbriae: Effects of insert position and host background
    • Stentebjerg-Olesen B, Pallesen L, Jensen LB, Christiansen G, Klemm P: Authentic display of a cholera toxin epitope by chimeric type I fimbriae: effects of insert position and host background. Microbiology 1997, 143(Pt6):2027-2038.
    • (1997) Microbiology , vol.143 , Issue.PART 6 , pp. 2027-2038
    • Stentebjerg-Olesen, B.1    Pallesen, L.2    Jensen, L.B.3    Christiansen, G.4    Klemm, P.5
  • 25
    • 0030730501 scopus 로고    scopus 로고
    • Cell-surface display of a Pseudomonas aeruginosa strain K pilin peptide within the paracrystalline S-layer of Caulobacter crescentus
    • Bingle WH, Nomellini JF, Smit J: Cell-surface display of a Pseudomonas aeruginosa strain K pilin peptide within the paracrystalline S-layer of Caulobacter crescentus. Mol Microbiol 1997, 26(2):277-288.
    • (1997) Mol Microbiol , vol.26 , Issue.2 , pp. 277-288
    • Bingle, W.H.1    Nomellini, J.F.2    Smit, J.3
  • 26
    • 0035878128 scopus 로고    scopus 로고
    • Protein secretion and the pathogenesis of bacterial infections
    • Lee VT, Schneewind O: Protein secretion and the pathogenesis of bacterial infections. Genes Dev 2001, 15(14):1725-1752.
    • (2001) Genes Dev , vol.15 , Issue.14 , pp. 1725-1752
    • Lee, V.T.1    Schneewind, O.2
  • 27
    • 8844269404 scopus 로고    scopus 로고
    • The underlying mechanisms of type II protein secretion
    • Filloux A: The underlying mechanisms of type II protein secretion. Biochim Biophys Acta 2004, 1694(1-3):163-179.
    • (2004) Biochim Biophys Acta , vol.1694 , Issue.1-3 , pp. 163-179
    • Filloux, A.1
  • 28
    • 0025122755 scopus 로고
    • The normally periplasmic enzyme beta-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase
    • Kornacker MG, Pugsley AP: The normally periplasmic enzyme beta-lactamase is specifically and efficiently translocated through the Escherichia coli outer membrane when it is fused to the cell-surface enzyme pullulanase. Mol Microbiol 1990, 4(7):1101-1109.
    • (1990) Mol Microbiol , vol.4 , Issue.7 , pp. 1101-1109
    • Kornacker, M.G.1    Pugsley, A.P.2
  • 29
    • 10344249890 scopus 로고    scopus 로고
    • Process of protein transport by the type III secretion system
    • Ghosh P: Process of protein transport by the type III secretion system. Microbiol Mol Biol Rev 2004, 68(4):771-795.
    • (2004) Microbiol Mol Biol Rev , vol.68 , Issue.4 , pp. 771-795
    • Ghosh, P.1
  • 30
    • 20444411167 scopus 로고    scopus 로고
    • Molecular basis of antigenic polymorphism of EspA filaments: Development of a peptide display technology
    • Crepin VF, Shaw R, Knutton S, Frankel G: Molecular basis of antigenic polymorphism of EspA filaments: development of a peptide display technology. J Mol Biol 2005, 350(1):42-52.
    • (2005) J Mol Biol , vol.350 , Issue.1 , pp. 42-52
    • Crepin, V.F.1    Shaw, R.2    Knutton, S.3    Frankel, G.4
  • 32
    • 0023128808 scopus 로고
    • Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease
    • Pohlner J, Halter R, Beyreuther K, Meyer TF: Gene structure and extracellular secretion of Neisseria gonorrhoeae IgA protease. Nature 1987, 325(6103):458-462.
    • (1987) Nature , vol.325 , Issue.6103 , pp. 458-462
    • Pohlner, J.1    Halter, R.2    Beyreuther, K.3    Meyer, T.F.4
  • 33
    • 0028824728 scopus 로고
    • Common structural features of IgAI protease-like outer membrane protein autotransporters
    • Jose J, Jahnig F, Meyer TF: Common structural features of IgAI protease-like outer membrane protein autotransporters. Mol Microbiol 1995, 18(2):378-380.
    • (1995) Mol Microbiol , vol.18 , Issue.2 , pp. 378-380
    • Jose, J.1    Jahnig, F.2    Meyer, T.F.3
  • 34
    • 2442507008 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hia Autotransporter Contains an Unusually Short Trimeric Translocator Domain
    • Surana NK, Cutter D, Barenkamp SJ, St Geme JW 3rd: The Haemophilus influenzae Hia Autotransporter Contains an Unusually Short Trimeric Translocator Domain. J Biol Chem 2004, 279(15):14679-14685.
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14679-14685
    • Surana, N.K.1    Cutter, D.2    Barenkamp, S.J.3    St Geme III, J.W.4
  • 35
    • 33745743311 scopus 로고    scopus 로고
    • Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter
    • Meng G, Surana NK, St Geme JW, Waksman G: Structure of the outer membrane translocator domain of the Haemophilus influenzae Hia trimeric autotransporter. Embo J 2006.
    • (2006) Embo J
    • Meng, G.1    Surana, N.K.2    St Geme, J.W.3    Waksman, G.4
  • 36
    • 1942535748 scopus 로고    scopus 로고
    • Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter
    • Yeo HJ, Cotter SE, Laarmann S, Juehne T, St Geme JW, Waksman G: Structural basis for host recognition by the Haemophilus influenzae Hia autotransporter. Embo J 2004, 23(6):1245-1256.
    • (2004) Embo J , vol.23 , Issue.6 , pp. 1245-1256
    • Yeo, H.J.1    Cotter, S.E.2    Laarmann, S.3    Juehne, T.4    St Geme, J.W.5    Waksman, G.6
  • 37
    • 18044363515 scopus 로고    scopus 로고
    • Trimeric autotransporters: A distinct subfamily of autotransporter proteins
    • Cotter SE, Surana NK, St Geme JW 3rd: Trimeric autotransporters: a distinct subfamily of autotransporter proteins. Trends Microbiol 2005, 13(5):199-205.
    • (2005) Trends Microbiol , vol.13 , Issue.5 , pp. 199-205
    • Cotter, S.E.1    Surana, N.K.2    St Geme III, J.W.3
  • 38
    • 8844235655 scopus 로고    scopus 로고
    • Protein secretion through autotransporter and two-partner pathways
    • Jacob-Dubuisson F, Fernandez R, Coutte L: Protein secretion through autotransporter and two-partner pathways. Biochim Biophys Acta 2004, 1694(1-3):235-257.
    • (2004) Biochim Biophys Acta , vol.1694 , Issue.1-3 , pp. 235-257
    • Jacob-Dubuisson, F.1    Fernandez, R.2    Coutte, L.3
  • 39
    • 0027136213 scopus 로고
    • Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion
    • Klauser T, Kramer J, Otzelberger K, Pohlner J, Meyer TF: Characterization of the Neisseria Iga beta-core. The essential unit for outer membrane targeting and extracellular protein secretion. J Mol Biol 1993, 234(3):579-593.
    • (1993) J Mol Biol , vol.234 , Issue.3 , pp. 579-593
    • Klauser, T.1    Kramer, J.2    Otzelberger, K.3    Pohlner, J.4    Meyer, T.F.5
  • 40
    • 0030688998 scopus 로고    scopus 로고
    • A novel family of channel-forming, autotransporting, bacterial virulence factors
    • Loveless BJ, Saier MH Jr: A novel family of channel-forming, autotransporting, bacterial virulence factors. Mol Membr Biol 1997, 14(3):113-123.
    • (1997) Mol Membr Biol , vol.14 , Issue.3 , pp. 113-123
    • Loveless, B.J.1    Saier Jr., M.H.2
  • 41
    • 0030693901 scopus 로고    scopus 로고
    • Structural determinants of processing and secretion of the Haemophilus influenzae hap protein
    • Hendrixson DR, de la Morena ML, Stathopoulos C, St Geme JW 3rd: Structural determinants of processing and secretion of the Haemophilus influenzae hap protein. Mol Microbiol 1997, 26(3):505-518.
    • (1997) Mol Microbiol , vol.26 , Issue.3 , pp. 505-518
    • Hendrixson, D.R.1    de la Morena, M.L.2    Stathopoulos, C.3    St Geme III, J.W.4
  • 42
    • 0037224652 scopus 로고    scopus 로고
    • Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter
    • Oliver DC, Huang G, Fernandez RC: Identification of secretion determinants of the Bordetella pertussis BrkA autotransporter. J Bacteriol 2003, 185(2):489-495.
    • (2003) J Bacteriol , vol.185 , Issue.2 , pp. 489-495
    • Oliver, D.C.1    Huang, G.2    Fernandez, R.C.3
  • 43
    • 0037338681 scopus 로고    scopus 로고
    • A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain
    • Oliver DC, Huang G, Nodel E, Pleasance S, Fernandez RC: A conserved region within the Bordetella pertussis autotransporter BrkA is necessary for folding of its passenger domain. Mol Microbiol 2003, 47(5):1367-1383.
    • (2003) Mol Microbiol , vol.47 , Issue.5 , pp. 1367-1383
    • Oliver, D.C.1    Huang, G.2    Nodel, E.3    Pleasance, S.4    Fernandez, R.C.5
  • 44
    • 15544366859 scopus 로고    scopus 로고
    • Barriers to folding of the transmembrane domain of the Escherichia coli autotransporter adhesin involved in diffuse adherence
    • Mogensen JE, Tapadar D, Schmidt MA, Otzen DE: Barriers to folding of the transmembrane domain of the Escherichia coli autotransporter adhesin involved in diffuse adherence. Biochemistry 2005, 44(11):4533-4545.
    • (2005) Biochemistry , vol.44 , Issue.11 , pp. 4533-4545
    • Mogensen, J.E.1    Tapadar, D.2    Schmidt, M.A.3    Otzen, D.E.4
  • 45
    • 0028670436 scopus 로고
    • Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme
    • Ohnishi Y, Nishiyama M, Horinouchi S, Beppu T: Involvement of the COOH-terminal pro-sequence of Serratia marcescens serine protease in the folding of the mature enzyme. J Biol Chem 1994, 269(52):32800-32806.
    • (1994) J Biol Chem , vol.269 , Issue.52 , pp. 32800-32806
    • Ohnishi, Y.1    Nishiyama, M.2    Horinouchi, S.3    Beppu, T.4
  • 46
    • 3843078622 scopus 로고    scopus 로고
    • Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger
    • Velarde JJ, Nataro JP: Hydrophobic residues of the autotransporter EspP linker domain are important for outer membrane translocation of its passenger. J Biol Chem 2004, 279(30):31495-31504.
    • (2004) J Biol Chem , vol.279 , Issue.30 , pp. 31495-31504
    • Velarde, J.J.1    Nataro, J.P.2
  • 47
    • 0032169654 scopus 로고    scopus 로고
    • The great escape: Structure and function of the autotransporter proteins
    • Henderson IR, Navarro-Garcia F, Nataro JP: The great escape: structure and function of the autotransporter proteins. Trends Microbiol 1998, 6(9):370-378.
    • (1998) Trends Microbiol , vol.6 , Issue.9 , pp. 370-378
    • Henderson, I.R.1    Navarro-Garcia, F.2    Nataro, J.P.3
  • 48
    • 0029930053 scopus 로고    scopus 로고
    • Identification of a second family of high-molecular-weight adhesion proteins expressed by non-typable Haemophilus influenzae
    • Barenkamp SJ, St Geme JW 3rd: Identification of a second family of high-molecular-weight adhesion proteins expressed by non-typable Haemophilus influenzae. Mol Microbiol 1996, 19(6):1215-1223.
    • (1996) Mol Microbiol , vol.19 , Issue.6 , pp. 1215-1223
    • Barenkamp, S.J.1    St Geme III, J.W.2
  • 49
    • 0029861822 scopus 로고    scopus 로고
    • Characterization of the genetic locus encoding Haemophilus influenzae type b surface fibrils
    • St Geme JW 3rd, Cutter D, Barenkamp SJ: Characterization of the genetic locus encoding Haemophilus influenzae type b surface fibrils. J Bacteriol 1996, 178(21):6281-6287.
    • (1996) J Bacteriol , vol.178 , Issue.21 , pp. 6281-6287
    • St Geme III, J.W.1    Cutter, D.2    Barenkamp, S.J.3
  • 50
    • 0028122022 scopus 로고
    • Genes encoding high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clusters
    • Barenkamp SJ, St Geme JW 3rd: Genes encoding high-molecular-weight adhesion proteins of nontypeable Haemophilus influenzae are part of gene clusters. Infect Immun 1994, 62(8):3320-3328.
    • (1994) Infect Immun , vol.62 , Issue.8 , pp. 3320-3328
    • Barenkamp, S.J.1    St Geme III, J.W.2
  • 51
    • 0031798664 scopus 로고    scopus 로고
    • N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin
    • Lambert-Buisine C, Willery E, Locht C, Jacob-Dubuisson F: N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin. Mol Microbiol 1998, 28(6):1283-1293.
    • (1998) Mol Microbiol , vol.28 , Issue.6 , pp. 1283-1293
    • Lambert-Buisine, C.1    Willery, E.2    Locht, C.3    Jacob-Dubuisson, F.4
  • 52
    • 8844239874 scopus 로고    scopus 로고
    • SRP-mediated protein trageting: Structure and function revisited
    • Luirink J, Sinning I: SRP-mediated protein trageting: structure and function revisited. Biochim Biophys Acta 2004, 1694(1-3):17-35.
    • (2004) Biochim Biophys Acta , vol.1694 , Issue.1-3 , pp. 17-35
    • Luirink, J.1    Sinning, I.2
  • 53
    • 0037799238 scopus 로고    scopus 로고
    • Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein
    • Sijbrandi R, Urbanus ML, ten Hagen-Jongman CM, Bernstein HD, Oudega B, Otto BR, Luirink J: Signal recognition particle (SRP)-mediated targeting and Sec-dependent translocation of an extracellular Escherichia coli protein. J Biol Chem 2003, 278(7):4654-4659.
    • (2003) J Biol Chem , vol.278 , Issue.7 , 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
  • 54
    • 0242412456 scopus 로고    scopus 로고
    • Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle
    • Peterson JH, Woolhead CA, Bernstein HD: Basic amino acids in a distinct subset of signal peptides promote interaction with the signal recognition particle. J Biol Chem 2003, 278(46):46155-46162.
    • (2003) J Biol Chem , vol.278 , Issue.46 , pp. 46155-46162
    • Peterson, J.H.1    Woolhead, C.A.2    Bernstein, H.D.3
  • 55
    • 0141484348 scopus 로고    scopus 로고
    • IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed
    • Brandon LD, Goehring N, Janakiraman A, Yan AW, Wu T, Beckwith J, Goldberg MB: IcsA, a polarly localized autotransporter with an atypical signal peptide, uses the Sec apparatus for secretion, although the Sec apparatus is circumferentially distributed. Mol Microbiol 2003, 50(1):45-60.
    • (2003) Mol Microbiol , vol.50 , Issue.1 , pp. 45-60
    • Brandon, L.D.1    Goehring, N.2    Janakiraman, A.3    Yan, A.W.4    Wu, T.5    Beckwith, J.6    Goldberg, M.B.7
  • 56
    • 11844280919 scopus 로고    scopus 로고
    • An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter
    • Szabady RL, Peterson JH, Skillman KM, Bernstein HD: An unusual signal peptide facilitates late steps in the biogenesis of a bacterial autotransporter. Proc Natl Acad Sci USA 2005, 102(1):221-226.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.1 , pp. 221-226
    • Szabady, R.L.1    Peterson, J.H.2    Skillman, K.M.3    Bernstein, H.D.4
  • 57
    • 33646918973 scopus 로고    scopus 로고
    • An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor and the SecYEG complex
    • Peterson JH, Szabady RL, Bernstein HD: An unusual signal peptide extension inhibits the binding of bacterial presecretory proteins to the signal recognition particle, trigger factor and the SecYEG complex. J Biol Chem 2006.
    • (2006) J Biol Chem
    • Peterson, J.H.1    Szabady, R.L.2    Bernstein, H.D.3
  • 58
    • 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, Schmidt MA: Glycosylation with heptose residues mediated by the aah gene product is essential for adherence of the AIDA-I adhesin. Mol Microbiol 2001, 40(6):1403-1413.
    • (2001) Mol Microbiol , vol.40 , Issue.6 , pp. 1403-1413
    • Benz, I.1    Schmidt, M.A.2
  • 59
    • 0035151832 scopus 로고    scopus 로고
    • Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA
    • Brandon LD, Goldberg MB: Periplasmic transit and disulfide bond formation of the autotransported Shigella protein IcsA. J Bacteriol 2001, 183(3):951-958.
    • (2001) J Bacteriol , vol.183 , Issue.3 , pp. 951-958
    • Brandon, L.D.1    Goldberg, M.B.2
  • 60
    • 0025353145 scopus 로고
    • Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: Conformation-dependent outer membrane translocation
    • Klauser T, Pohlner J, Meyer TF: Extracellular transport of cholera toxin B subunit using Neisseria IgA protease beta-domain: conformation-dependent outer membrane translocation. Embo J 1990, 9(6):1991-1999.
    • (1990) Embo J , vol.9 , Issue.6 , pp. 1991-1999
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 61
    • 0026511122 scopus 로고
    • Selective extracellular release of cholera toxin B subunit by Escherichia coli: Dissection of Neisseria Iga beta-mediated outer membrane transport
    • Klauser T, Pohlner J, Meyer TF: Selective extracellular release of cholera toxin B subunit by Escherichia coli: dissection of Neisseria Iga beta-mediated outer membrane transport. Embo J 1992, 11(6):2327-2335.
    • (1992) Embo J , vol.11 , Issue.6 , pp. 2327-2335
    • Klauser, T.1    Pohlner, J.2    Meyer, T.F.3
  • 62
    • 0034051291 scopus 로고    scopus 로고
    • Autodisplay: Functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter
    • Lattemann CT, Maurer J, Gerland E, Meyer TF: Autodisplay: functional display of active beta-lactamase on the surface of Escherichia coli by the AIDA-I autotransporter. J Bacteriol 2000, 182(13):3726-3733.
    • (2000) J Bacteriol , vol.182 , Issue.13 , pp. 3726-3733
    • Lattemann, C.T.1    Maurer, J.2    Gerland, E.3    Meyer, T.F.4
  • 63
    • 0029621229 scopus 로고
    • Extracellular transport of VirG protein in Shigella
    • Suzuki T, Lett MC, Sasakawa C: Extracellular transport of VirG protein in Shigella. J Biol Chem 1995, 270(52):30874-30880.
    • (1995) J Biol Chem , vol.270 , Issue.52 , pp. 30874-30880
    • Suzuki, T.1    Lett, M.C.2    Sasakawa, C.3
  • 64
    • 21344432762 scopus 로고    scopus 로고
    • Autodisplay of the protease inhibitor aprotinin in Escherichia coli
    • Jose J, Zangen D: Autodisplay of the protease inhibitor aprotinin in Escherichia coli. Biochem Biophys Res Commun 2005, 333(4):1218-1226.
    • (2005) Biochem Biophys Res Commun , vol.333 , Issue.4 , pp. 1218-1226
    • Jose, J.1    Zangen, D.2
  • 65
    • 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 Iga beta autotransporter pathway
    • Jose J, Kramer J, Klauser T, Pohlner J, Meyer TF: Absence of periplasmic DsbA oxidoreductase facilitates export of cysteine-containing passenger proteins to the Escherichia coli cell surface via the Iga beta autotransporter pathway. Gene 1996, 178(1-2):107-110.
    • (1996) Gene , vol.178 , Issue.1-2 , pp. 107-110
    • Jose, J.1    Kramer, J.2    Klauser, T.3    Pohlner, J.4    Meyer, T.F.5
  • 66
    • 0032854025 scopus 로고    scopus 로고
    • Probing secretion and translocation of a beta-autotransporter using a reporter single-chain Fv as a cognate passenger domain
    • Veiga E, de Lorenzo V, Fernandez LA: Probing secretion and translocation of a beta-autotransporter using a reporter single-chain Fv as a cognate passenger domain. Mol Microbiol 1999, 33(6):1232-1243.
    • (1999) Mol Microbiol , vol.33 , Issue.6 , pp. 1232-1243
    • Veiga, E.1    de Lorenzo, V.2    Fernandez, L.A.3
  • 67
    • 3142680440 scopus 로고    scopus 로고
    • Structural tolerance of bacterial autotransporters for folded passenger protein domains
    • Veiga E, de Lorenzo V, Fernandez LA: Structural tolerance of bacterial autotransporters for folded passenger protein domains. Mol Microbiol 2004, 52(4):1069-1080.
    • (2004) Mol Microbiol , vol.52 , Issue.4 , pp. 1069-1080
    • Veiga, E.1    de Lorenzo, V.2    Fernandez, L.A.3
  • 68
    • 0034015838 scopus 로고    scopus 로고
    • Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system
    • Konieczny MP, Suhr M, Noll A, Autenrieth IB, Alexander Schmidt M: Cell surface presentation of recombinant (poly-) peptides including functional T-cell epitopes by the AIDA autotransporter system. FEMS Immunol Med Microbiol 2000, 27(4):321-332.
    • (2000) FEMS Immunol Med Microbiol , vol.27 , Issue.4 , pp. 321-332
    • Konieczny, M.P.1    Suhr, M.2    Noll, A.3    Autenrieth, I.B.4    Alexander Schmidt, M.5
  • 69
    • 27944445725 scopus 로고    scopus 로고
    • Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter
    • Skillman KM, Barnard TJ, Peterson JH, Ghirlando R, Bernstein HD: Efficient secretion of a folded protein domain by a monomeric bacterial autotransporter. Mol Microbiol 2005, 58(4):945-958.
    • (2005) Mol Microbiol , vol.58 , Issue.4 , pp. 945-958
    • Skillman, K.M.1    Barnard, T.J.2    Peterson, J.H.3    Ghirlando, R.4    Bernstein, H.D.5
  • 71
    • 0035822622 scopus 로고    scopus 로고
    • Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins
    • Welker E, Wedemeyer WJ, Narayan M, Scheraga HA: Coupling of conformational folding and disulfide-bond reactions in oxidative folding of proteins. Biochemistry 2001, 40(31):9059-9064.
    • (2001) Biochemistry , vol.40 , Issue.31 , pp. 9059-9064
    • Welker, E.1    Wedemeyer, W.J.2    Narayan, M.3    Scheraga, H.A.4
  • 72
    • 15744389448 scopus 로고    scopus 로고
    • Sensing external stress: Watchdogs of the Escherichia coli cell envelope
    • Ruiz N, Silhavy TJ: Sensing external stress: watchdogs of the Escherichia coli cell envelope. Curr Opin Microbiol 2005, 8(2):122-126.
    • (2005) Curr Opin Microbiol , vol.8 , Issue.2 , pp. 122-126
    • Ruiz, N.1    Silhavy, T.J.2
  • 73
    • 0025005885 scopus 로고
    • Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization
    • Tani K, Tokuda H, Mizushima S: Translocation of ProOmpA possessing an intramolecular disulfide bridge into membrane vesicles of Escherichia coli. Effect of membrane energization. J Biol Chem 1990, 265(28):17341-17347.
    • (1990) J Biol Chem , vol.265 , Issue.28 , pp. 17341-17347
    • Tani, K.1    Tokuda, H.2    Mizushima, S.3
  • 74
    • 33744746602 scopus 로고    scopus 로고
    • The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation
    • Rutherford N, Charbonneau ME, Berthiaume F, Betton JM, Mourez M: The periplasmic folding of a cysteineless autotransporter passenger domain interferes with its outer membrane translocation. J Bacteriol 2006, 188(11):4111-4116.
    • (2006) J Bacteriol , vol.188 , Issue.11 , pp. 4111-4116
    • Rutherford, N.1    Charbonneau, M.E.2    Berthiaume, F.3    Betton, J.M.4    Mourez, M.5
  • 75
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between folding factors and bacterial outer membrane proteins
    • Mogensen JE, Otzen DE: Interactions between folding factors and bacterial outer membrane proteins. Mol Microbiol 2005, 57(2):326-346.
    • (2005) Mol Microbiol , vol.57 , Issue.2 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 76
    • 0032698497 scopus 로고    scopus 로고
    • Characterization of the essential transport function of the AIDA-I autotransporter and evidence supporting structural predictions
    • Maurer J, Jose J, Meyer TF: Characterization of the essential transport function of the AIDA-I autotransporter and evidence supporting structural predictions. J Bacteriol 1999, 181(22):7014-7020.
    • (1999) J Bacteriol , vol.181 , Issue.22 , pp. 7014-7020
    • Maurer, J.1    Jose, J.2    Meyer, T.F.3
  • 78
    • 0032882546 scopus 로고    scopus 로고
    • The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes
    • Shannon JL, Fernandez RC: The C-terminal domain of the Bordetella pertussis autotransporter BrkA forms a pore in lipid bilayer membranes. J Bacteriol 1999, 181(18):5838-5842.
    • (1999) J Bacteriol , vol.181 , Issue.18 , pp. 5838-5842
    • Shannon, J.L.1    Fernandez, R.C.2
  • 79
    • 0036565670 scopus 로고    scopus 로고
    • Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains
    • Veiga E, Sugawara E, Nikaido H, de Lorenzo V, Fernandez LA: Export of autotransported proteins proceeds through an oligomeric ring shaped by C-terminal domains. Embo J 2002, 21(9):2122-2131.
    • (2002) Embo J , vol.21 , Issue.9 , pp. 2122-2131
    • Veiga, E.1    Sugawara, E.2    Nikaido, H.3    de Lorenzo, V.4    Fernandez, L.A.5
  • 80
    • 0038105549 scopus 로고    scopus 로고
    • The pore size of the autotransporter domain is critical for the active translocation of the passenger domain
    • Lee HW, Byun SM: The pore size of the autotransporter domain is critical for the active translocation of the passenger domain. Biochem Biophys Res Commun 2003, 307(4):820-825.
    • (2003) Biochem Biophys Res Commun , vol.307 , Issue.4 , pp. 820-825
    • Lee, H.W.1    Byun, S.M.2
  • 81
    • 33645525759 scopus 로고    scopus 로고
    • Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins
    • Junker M, Schuster CC, McDonnell AV, Sorg KA, Finn MC, Berger B, Clark PL: Pertactin beta-helix folding mechanism suggests common themes for the secretion and folding of autotransporter proteins. Proc Natl Acad Sci USA 2006, 103(13):4918-4923.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.13 , pp. 4918-4923
    • Junker, M.1    Schuster, C.C.2    McDonnell, A.V.3    Sorg, K.A.4    Finn, M.C.5    Berger, B.6    Clark, P.L.7
  • 82
    • 0029988488 scopus 로고    scopus 로고
    • Structure of Bordetella pertussis virulence factor P.69 pertactin
    • Emsley P, Charles IG, Fairweather NF, Isaacs NW: Structure of Bordetella pertussis virulence factor P.69 pertactin. Nature 1996, 381(6577):90-92.
    • (1996) Nature , vol.381 , Issue.6577 , pp. 90-92
    • Emsley, P.1    Charles, I.G.2    Fairweather, N.F.3    Isaacs, N.W.4
  • 83
    • 20444435483 scopus 로고    scopus 로고
    • Crystal Structure of Hemoglobin Protease, a Heme Binding Autotransporter Protein from Pathogenic Escherichia coli
    • Otto BR, Sijbrandi R, Luirink J, Oudega B, Heddle JG, Mizutani K, Park SY, Tame JR: Crystal Structure of Hemoglobin Protease, a Heme Binding Autotransporter Protein from Pathogenic Escherichia coli. J Biol Chem 2005, 280(17):17339-17345.
    • (2005) J Biol Chem , vol.280 , Issue.17 , pp. 17339-17345
    • Otto, B.R.1    Sijbrandi, R.2    Luirink, J.3    Oudega, B.4    Heddle, J.G.5    Mizutani, K.6    Park, S.Y.7    Tame, J.R.8
  • 84
    • 21544468024 scopus 로고    scopus 로고
    • Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface
    • Muller D, Benz I, Tapadar D, Buddenborg C, Greune L, Schmidt MA: Arrangement of the translocator of the autotransporter adhesin involved in diffuse adherence on the bacterial surface. Infect Immun 2005, 73(7):3851-3859.
    • (2005) Infect Immun , vol.73 , Issue.7 , pp. 3851-3859
    • Muller, D.1    Benz, I.2    Tapadar, D.3    Buddenborg, C.4    Greune, L.5    Schmidt, M.A.6
  • 85
    • 0036893427 scopus 로고    scopus 로고
    • Functional comparison of serine protease autotransporters of enterobacteriaceae
    • Dutta PR, Cappello R, Navarro-Garcia F, Nataro JP: Functional comparison of serine protease autotransporters of enterobacteriaceae. Infect Immun 2002, 70(12):7105-7113.
    • (2002) Infect Immun , vol.70 , Issue.12 , pp. 7105-7113
    • Dutta, P.R.1    Cappello, R.2    Navarro-Garcia, F.3    Nataro, J.P.4
  • 86
    • 0037371554 scopus 로고    scopus 로고
    • Chromosomal expression of the Haemophilus influenzae Hap autotransporter allows fine-tuned regulation of adhesive potential via inhibition of intermolecular autoproteolysis
    • Fink DL, St Geme JW 3rd: Chromosomal expression of the Haemophilus influenzae Hap autotransporter allows fine-tuned regulation of adhesive potential via inhibition of intermolecular autoproteolysis. J Bacteriol 2003, 185(5):1608-1615.
    • (2003) J Bacteriol , vol.185 , Issue.5 , pp. 1608-1615
    • Fink, D.L.1    St Geme III, J.W.2
  • 87
    • 0032246189 scopus 로고    scopus 로고
    • The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein
    • Hendrixson DR, St Geme JW 3rd: The Haemophilus influenzae Hap serine protease promotes adherence and microcolony formation, potentiated by a soluble host protein. Mol Cell 1998, 2(6):841-850.
    • (1998) Mol Cell , vol.2 , Issue.6 , pp. 841-850
    • Hendrixson, D.R.1    St Geme III, J.W.2
  • 88
    • 0030061950 scopus 로고    scopus 로고
    • Lack of cleavage of IcsA in Shigella flexneri causes aberrant movement and allows demonstration of a cross-reactive eukaryotic protein
    • d'Hauteville H, Dufourcq Lagelouse R, Nato F, Sansonetti PJ: Lack of cleavage of IcsA in Shigella flexneri causes aberrant movement and allows demonstration of a cross-reactive eukaryotic protein. Infect Immun 1996, 64(2):511-517.
    • (1996) Infect Immun , vol.64 , Issue.2 , pp. 511-517
    • d'Hauteville, H.1    Dufourcq Lagelouse, R.2    Nato, F.3    Sansonetti, P.J.4
  • 89
    • 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, Schmidt MA: 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 1992, 6(11):1539-1546.
    • (1992) Mol Microbiol , vol.6 , Issue.11 , pp. 1539-1546
    • Benz, I.1    Schmidt, M.A.2
  • 90
    • 0032783142 scopus 로고    scopus 로고
    • Identification of a glycoprotein produced by enterotoxigenic Escherichia coli
    • Lindenthal C, Elsinghorst EA: Identification of a glycoprotein produced by enterotoxigenic Escherichia coli. Infect Immun 1999, 67(8):4084-4091.
    • (1999) Infect Immun , vol.67 , Issue.8 , pp. 4084-4091
    • Lindenthal, C.1    Elsinghorst, E.A.2
  • 91
    • 0035914443 scopus 로고    scopus 로고
    • The Hemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism
    • Fink DL, Cope LD, Hansen EJ, Geme JW 3rd: The Hemophilus influenzae Hap autotransporter is a chymotrypsin clan serine protease and undergoes autoproteolysis via an intermolecular mechanism. J Biol Chem 2001, 276(42):39492-39500.
    • (2001) J Biol Chem , vol.276 , Issue.42 , pp. 39492-39500
    • Fink, D.L.1    Cope, L.D.2    Hansen, E.J.3    Geme III, J.W.4
  • 92
    • 0031025789 scopus 로고    scopus 로고
    • SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri
    • Egile C, d'Hauteville H, Parsot C, Sansonetti PJ: SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri. Mol Microbiol 1997, 23(5):1063-1073.
    • (1997) Mol Microbiol , vol.23 , Issue.5 , pp. 1063-1073
    • Egile, C.1    d'Hauteville, H.2    Parsot, C.3    Sansonetti, P.J.4
  • 94
    • 0029846536 scopus 로고    scopus 로고
    • Processing of the AIDA-Iprecursor: Removal of AIDAc and evidence for the outer membrane anchoring as a beta-barrel structure
    • Suhr M, Benz I, Schmidt MA: Processing of the AIDA-Iprecursor: removal of AIDAc and evidence for the outer membrane anchoring as a beta-barrel structure. Mol Microbiol 1996, 22(1):31-42.
    • (1996) Mol Microbiol , vol.22 , Issue.1 , pp. 31-42
    • Suhr, M.1    Benz, I.2    Schmidt, M.A.3
  • 96
    • 0032983194 scopus 로고    scopus 로고
    • Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue
    • Odenbreit S, Till M, Hofreuter D, Faller G, Haas R: Genetic and functional characterization of the alpAB gene locus essential for the adhesion of Helicobacter pylori to human gastric tissue. Mol Microbiol 1999, 31(5):1537-1548.
    • (1999) Mol Microbiol , vol.31 , Issue.5 , pp. 1537-1548
    • Odenbreit, S.1    Till, M.2    Hofreuter, D.3    Faller, G.4    Haas, R.5
  • 97
    • 33644769605 scopus 로고    scopus 로고
    • Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein
    • Sherlock O, Dobrindt U, Jensen JB, Munk Vejborg R, Klemm P: Glycosylation of the self-recognizing Escherichia coli Ag43 autotransporter protein. J Bacteriol 2006, 188(5):1798-1807.
    • (2006) J Bacteriol , vol.188 , Issue.51 , pp. 798-1807
    • Sherlock, O.1    Dobrindt, U.2    Jensen, J.B.3    Munk Vejborg, R.4    Klemm, P.5
  • 98
    • 0036084379 scopus 로고    scopus 로고
    • Expression of the Plasmodium falciparum immunodominant epitope (NANP)(4) on the surface of Salmonella enterica using the autotransporter MisL
    • Ruiz-Perez F, Leon-Kempis R, Santiago-Machuca A, Ortega-Pierres G, Barry E, Levine M, Gonzalez-Bonilla C: Expression of the Plasmodium falciparum immunodominant epitope (NANP)(4) on the surface of Salmonella enterica using the autotransporter MisL. Infect Immun 2002, 70(7):3611-3620.
    • (2002) Infect Immun , vol.70 , Issue.7 , pp. 3611-3620
    • Ruiz-Perez, F.1    Leon-Kempis, R.2    Santiago-Machuca, A.3    Ortega-Pierres, G.4    Barry, E.5    Levine, M.6    Gonzalez-Bonilla, C.7
  • 99
    • 0242349643 scopus 로고    scopus 로고
    • Autodisplay: Efficacious surface exposure of antigenic UreA fragments from Helicobacter pylori in Salmonella vaccine strains
    • Rizos K, Lattemann CT, Bumann D, Meyer TF, Aebischer T: Autodisplay: efficacious surface exposure of antigenic UreA fragments from Helicobacter pylori in Salmonella vaccine strains. Infect Immun 2003, 71(11):6320-6328.
    • (2003) Infect Immun , vol.71 , Issue.11 , pp. 6320-6328
    • Rizos, K.1    Lattemann, C.T.2    Bumann, D.3    Meyer, T.F.4    Aebischer, T.5
  • 100
  • 102
    • 0033859563 scopus 로고    scopus 로고
    • Fimbriae-assisted bacterial surface display of heterologous peptides
    • Klemm P, Schembri MA: Fimbriae-assisted bacterial surface display of heterologous peptides. Int J Med Microbiol 2000, 290(3):215-221.
    • (2000) Int J Med Microbiol , vol.290 , Issue.3 , pp. 215-221
    • Klemm, P.1    Schembri, M.A.2
  • 103
    • 0023822867 scopus 로고
    • Versatility of a vector for expressing foreign polypeptides at the surface of gram-negative bacteria
    • Charbit A, Molla A, Saurin W, Hofnung M: Versatility of a vector for expressing foreign polypeptides at the surface of gram-negative bacteria. Gene 1988, 70(1):181-189.
    • (1988) Gene , vol.70 , Issue.1 , pp. 181-189
    • Charbit, A.1    Molla, A.2    Saurin, W.3    Hofnung, M.4
  • 104
    • 0029983637 scopus 로고    scopus 로고
    • Display of beta-lactamase on the Escherichia coli surface: Outer membrane phenotypes conferred by Lpp'-OmpA'-beta-lactamase fusions
    • Georgiou G, Stephens DL, Stathopoulos C, Poetschke HL, Mendenhall J, Earhart CF: Display of beta-lactamase on the Escherichia coli surface: outer membrane phenotypes conferred by Lpp'-OmpA'-beta-lactamase fusions. Protein Eng 1996, 9(2):239-247.
    • (1996) Protein Eng , vol.9 , Issue.2 , pp. 239-247
    • Georgiou, G.1    Stephens, D.L.2    Stathopoulos, C.3    Poetschke, H.L.4    Mendenhall, J.5    Earhart, C.F.6
  • 105
    • 0026345777 scopus 로고
    • Phage-enzymes: Epression and affinity chromatography of functional alkaline phosphatase on the surface of bacteriophage
    • McCafferty J, Jackson RH, Chiswell DJ: Phage-enzymes: expression and affinity chromatography of functional alkaline phosphatase on the surface of bacteriophage. Protein Eng 1991, 4(8):955-961.
    • (1991) Protein Eng , vol.4 , Issue.8 , pp. 955-961
    • McCafferty, J.1    Jackson, R.H.2    Chiswell, D.J.3
  • 106
    • 0036068104 scopus 로고    scopus 로고
    • Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system
    • Kjaergaard K, Hasman H, Schembri MA, Klemm P: Antigen 43-mediated autotransporter display, a versatile bacterial cell surface presentation system. J Bacteriol 2002, 184(15):4197-4204.
    • (2002) J Bacteriol , vol.184 , Issue.15 , pp. 4197-4204
    • Kjaergaard, K.1    Hasman, H.2    Schembri, M.A.3    Klemm, P.4
  • 107
    • 0026594374 scopus 로고
    • Transport and anchoring of beta-lactamase to the external surface of Escherichia coli
    • Francisco JA, Earhart CF, Georgiou G: Transport and anchoring of beta-lactamase to the external surface of Escherichia coli. Proc Natl Acad Sci USA 1992, 89(7):2713-2717.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.7 , pp. 2713-2717
    • Francisco, J.A.1    Earhart, C.F.2    Georgiou, G.3
  • 108
    • 10444272492 scopus 로고    scopus 로고
    • Use of Pseudomonas putida EstA as an anchoring motif for display of a periplasmic enzyme on the surface of Escherichia coli
    • Yang TH, Pan JG, Seo YS, Rhee JS: Use of Pseudomonas putida EstA as an anchoring motif for display of a periplasmic enzyme on the surface of Escherichia coli. Appl Environ Microbiol 2004, 70(12):6968-6976.
    • (2004) Appl Environ Microbiol , vol.70 , Issue.12 , pp. 6968-6976
    • Yang, T.H.1    Pan, J.G.2    Seo, Y.S.3    Rhee, J.S.4
  • 109
    • 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, Bernhardt R, Hannemann F: Functional display of active bovine adrenodoxin on the surface of E. coli by chemical incorporation of the [2Fe-2S] cluster. Chembiochem 2001, 2(9):695-701.
    • (2001) Chembiochem , vol.2 , Issue.9 , pp. 695-701
    • Jose, J.1    Bernhardt, R.2    Hannemann, F.3
  • 110
    • 27644435170 scopus 로고    scopus 로고
    • Bacterial surface display library screening by target enzyme labeling: Identification of new human cathepsin G inhibitors
    • Jose J, Betscheider D, Zangen D: Bacterial surface display library screening by target enzyme labeling: Identification of new human cathepsin G inhibitors. Anal Biochem 2005, 346(2):258-267.
    • (2005) Anal Biochem , vol.346 , Issue.2 , pp. 258-267
    • Jose, J.1    Betscheider, D.2    Zangen, D.3
  • 111
    • 0034783458 scopus 로고    scopus 로고
    • Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori
    • Fischer W, Buhrdorf R, Gerland E, Haas R: Outer membrane targeting of passenger proteins by the vacuolating cytotoxin autotransporter of Helicobacter pylori. Infect Immun 2001, 69(11):6769-6775.
    • (2001) Infect Immun , vol.69 , Issue.11 , pp. 6769-6775
    • Fischer, W.1    Buhrdorf, R.2    Gerland, E.3    Haas, R.4
  • 112
    • 0028136066 scopus 로고
    • Extracellular transport of pseudoazurin of Alcaligenes faecalis in Escherichia coli using the COOH-terminal domain of Serratia marcescens serine protease
    • Shimada K, Ohnishi Y, Horinouchi S, Beppu T: Extracellular transport of pseudoazurin of Alcaligenes faecalis in Escherichia coli using the COOH-terminal domain of Serratia marcescens serine protease. J Biochem (Tokyo) 1994, 116(2):327-334.
    • (1994) J Biochem (Tokyo) , vol.116 , Issue.2 , pp. 327-334
    • Shimada, K.1    Ohnishi, Y.2    Horinouchi, S.3    Beppu, T.4
  • 113
    • 0036892189 scopus 로고    scopus 로고
    • Invasion activity of a Mycobacterium tuberculosis peptide presented by the Escherichia coli AIDA autotransporter
    • Casali N, Konieczny M, Schmidt MA, Riley LW: Invasion activity of a Mycobacterium tuberculosis peptide presented by the Escherichia coli AIDA autotransporter. Infect Immun 2002, 70(12):6846-6852.
    • (2002) Infect Immun , vol.70 , Issue.12 , pp. 6846-6852
    • Casali, N.1    Konieczny, M.2    Schmidt, M.A.3    Riley, L.W.4
  • 114
    • 0031034089 scopus 로고    scopus 로고
    • Autodisplay: One-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli
    • Maurer J, Jose J, Meyer TF: Autodisplay: one-component system for efficient surface display and release of soluble recombinant proteins from Escherichia coli. J Bacteriol 1997, 179(3):794-804.
    • (1997) J Bacteriol , vol.179 , Issue.3 , pp. 794-804
    • Maurer, J.1    Jose, J.2    Meyer, T.F.3
  • 115
    • 0042337192 scopus 로고    scopus 로고
    • Autotransporters as scaffolds for novel bacterial adhesins: Surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains
    • Veiga E, de Lorenzo V, Fernandez LA: Autotransporters as scaffolds for novel bacterial adhesins: surface properties of Escherichia coli cells displaying Jun/Fos dimerization domains. J Bacteriol 2003, 185(18):5585-5590.
    • (2003) J Bacteriol , vol.185 , Issue.18 , pp. 5585-5590
    • Veiga, E.1    de Lorenzo, V.2    Fernandez, L.A.3
  • 116
    • 0344304569 scopus 로고    scopus 로고
    • Neutralization of enteric coronaviruses with Escherichia coli cells expressing single-chain Fv-autotransporter fusions
    • Veiga E, De Lorenzo V, Fernandez LA: Neutralization of enteric coronaviruses with Escherichia coli cells expressing single-chain Fv-autotransporter fusions. J Virol 2003, 77(24):13396-13398.
    • (2003) J Virol , vol.77 , Issue.24 , pp. 13396-13398
    • Veiga, E.1    De Lorenzo, V.2    Fernandez, L.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.