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Volumn 32, Issue 6, 2015, Pages 644-650

Going beyond E. coli: autotransporter based surface display on alternative host organisms

Author keywords

[No Author keywords available]

Indexed keywords

BIOCATALYSTS; BIOREMEDIATION; CATALYSIS; CELL MEMBRANES; ESCHERICHIA COLI; PROTEINS; RECOMBINANT PROTEINS;

EID: 84940963603     PISSN: 18716784     EISSN: 18764347     Source Type: Journal    
DOI: 10.1016/j.nbt.2014.12.008     Document Type: Review
Times cited : (23)

References (65)
  • 1
    • 84883272014 scopus 로고    scopus 로고
    • Biocatalysis in organic chemistry and biotechnology: past, present, and future
    • Reetz M.T. Biocatalysis in organic chemistry and biotechnology: past, present, and future. J Am Chem Soc 2013, 135(34):12480-12496.
    • (2013) J Am Chem Soc , vol.135 , Issue.34 , pp. 12480-12496
    • Reetz, M.T.1
  • 2
    • 84864580201 scopus 로고    scopus 로고
    • Autodisplay of enzymes - molecular basis and perspectives
    • Jose J., Maas R.M., Teese M.G. Autodisplay of enzymes - molecular basis and perspectives. J Biotechnol 2012, 161(2):92-103.
    • (2012) J Biotechnol , vol.161 , Issue.2 , pp. 92-103
    • Jose, J.1    Maas, R.M.2    Teese, M.G.3
  • 4
    • 84920250270 scopus 로고    scopus 로고
    • Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application
    • Schuurmann J., Quehl P., Festel G., Jose J. Bacterial whole-cell biocatalysts by surface display of enzymes: toward industrial application. Appl Microbiol Biotechnol 2014, 98(19):8031-8046.
    • (2014) Appl Microbiol Biotechnol , vol.98 , Issue.19 , pp. 8031-8046
    • Schuurmann, J.1    Quehl, P.2    Festel, G.3    Jose, J.4
  • 5
    • 0037212403 scopus 로고    scopus 로고
    • Microbial cell-surface display
    • Lee S.Y., Choi J.H., 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
  • 6
    • 35648988968 scopus 로고    scopus 로고
    • Are bacterial 'autotransporters' really transporters?
    • Bernstein H.D. Are bacterial 'autotransporters' really transporters?. Trends Microbiol 2007, 15(10):441-447.
    • (2007) Trends Microbiol , vol.15 , Issue.10 , pp. 441-447
    • Bernstein, H.D.1
  • 7
    • 84903639586 scopus 로고    scopus 로고
    • A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes
    • Leyton D.L., Johnson M.D., Thapa R., Huysmans G.H., Dunstan R.A., Celik N., et al. A mortise-tenon joint in the transmembrane domain modulates autotransporter assembly into bacterial outer membranes. Nat Commun 2014, 5:4239.
    • (2014) Nat Commun , vol.5 , pp. 4239
    • Leyton, D.L.1    Johnson, M.D.2    Thapa, R.3    Huysmans, G.H.4    Dunstan, R.A.5    Celik, N.6
  • 8
    • 33846296644 scopus 로고    scopus 로고
    • A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism
    • Desvaux M., Scott-Tucker A., Turner S.M., Cooper L.M., Huber D., Nataro J.P., et al. A conserved extended signal peptide region directs posttranslational protein translocation via a novel mechanism. Microbiology 2007, 153(Pt 1):59-70.
    • (2007) Microbiology , vol.153 , pp. 59-70
    • Desvaux, M.1    Scott-Tucker, A.2    Turner, S.M.3    Cooper, L.M.4    Huber, D.5    Nataro, J.P.6
  • 9
    • 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 J.H., Szabady R.L., Bernstein H.D. 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, 281(14):9038-9048.
    • (2006) J Biol Chem , vol.281 , Issue.14 , pp. 9038-9048
    • Peterson, J.H.1    Szabady, R.L.2    Bernstein, H.D.3
  • 10
    • 39149133696 scopus 로고    scopus 로고
    • Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases
    • Xie K., Dalbey R.E. Inserting proteins into the bacterial cytoplasmic membrane using the Sec and YidC translocases. Nat Rev Microbiol 2008, 6(3):234-244.
    • (2008) Nat Rev Microbiol , vol.6 , Issue.3 , pp. 234-244
    • Xie, K.1    Dalbey, R.E.2
  • 11
    • 84857148914 scopus 로고    scopus 로고
    • From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis
    • Leyton D.L., Rossiter A.E., Henderson I.R. From self sufficiency to dependence: mechanisms and factors important for autotransporter biogenesis. Nat Rev Microbiol 2012, 10(3):213-225.
    • (2012) Nat Rev Microbiol , vol.10 , Issue.3 , pp. 213-225
    • Leyton, D.L.1    Rossiter, A.E.2    Henderson, I.R.3
  • 12
    • 34547643207 scopus 로고    scopus 로고
    • IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA
    • Purdy G.E., Fisher C.R., Payne S.M. IcsA surface presentation in Shigella flexneri requires the periplasmic chaperones DegP, Skp, and SurA. J Bacteriol 2007, 189(15):5566-5573.
    • (2007) J Bacteriol , vol.189 , Issue.15 , pp. 5566-5573
    • Purdy, G.E.1    Fisher, C.R.2    Payne, S.M.3
  • 13
    • 70350470007 scopus 로고    scopus 로고
    • Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae
    • Ruiz-Perez F., Henderson I.R., Leyton D.L., Rossiter A.E., Zhang Y., Nataro J.P. Roles of periplasmic chaperone proteins in the biogenesis of serine protease autotransporters of Enterobacteriaceae. J Bacteriol 2009, 191(21):6571-6583.
    • (2009) J Bacteriol , vol.191 , Issue.21 , pp. 6571-6583
    • Ruiz-Perez, F.1    Henderson, I.R.2    Leyton, D.L.3    Rossiter, A.E.4    Zhang, Y.5    Nataro, J.P.6
  • 14
    • 60749102331 scopus 로고    scopus 로고
    • Membrane protein architects: the role of the BAM complex in outer membrane protein assembly
    • Knowles T.J., Scott-Tucker A., Overduin M., Henderson I.R. Membrane protein architects: the role of the BAM complex in outer membrane protein assembly. Nat Rev Microbiol 2009, 7(3):206-214.
    • (2009) Nat Rev Microbiol , vol.7 , Issue.3 , pp. 206-214
    • Knowles, T.J.1    Scott-Tucker, A.2    Overduin, M.3    Henderson, I.R.4
  • 15
    • 79961138396 scopus 로고    scopus 로고
    • The essential beta-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis
    • Rossiter A.E., Leyton D.L., Tveen-Jensen K., Browning D.F., Sevastsyanovich Y., Knowles T.J., et al. The essential beta-barrel assembly machinery complex components BamD and BamA are required for autotransporter biogenesis. J Bacteriol 2011, 193(16):4250-4253.
    • (2011) J Bacteriol , vol.193 , Issue.16 , pp. 4250-4253
    • Rossiter, A.E.1    Leyton, D.L.2    Tveen-Jensen, K.3    Browning, D.F.4    Sevastsyanovich, Y.5    Knowles, T.J.6
  • 16
    • 79960258056 scopus 로고    scopus 로고
    • Structures and functions of autotransporter proteins in microbial pathogens
    • Benz I., Schmidt M.A. Structures and functions of autotransporter proteins in microbial pathogens. Int J Med Microbiol 2011, 301(6):461-468.
    • (2011) Int J Med Microbiol , vol.301 , Issue.6 , pp. 461-468
    • Benz, I.1    Schmidt, M.A.2
  • 17
    • 84902182781 scopus 로고    scopus 로고
    • Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli
    • Gawarzewski I., DiMaio F., Winterer E., Tschapek B., Smits S.H., Jose J., et al. Crystal structure of the transport unit of the autotransporter adhesin involved in diffuse adherence from Escherichia coli. J Struct Biol 2014, 187(1):20-29.
    • (2014) J Struct Biol , vol.187 , Issue.1 , pp. 20-29
    • Gawarzewski, I.1    DiMaio, F.2    Winterer, E.3    Tschapek, B.4    Smits, S.H.5    Jose, J.6
  • 19
    • 84874594746 scopus 로고    scopus 로고
    • Mechanistic link between beta barrel assembly and the initiation of autotransporter secretion
    • Pavlova O., Peterson J.H., Ieva R., Bernstein H.D. Mechanistic link between beta barrel assembly and the initiation of autotransporter secretion. Proc Natl Acad Sci U S A 2013, 110(10):E938-E947.
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.10 , pp. E938-E947
    • Pavlova, O.1    Peterson, J.H.2    Ieva, R.3    Bernstein, H.D.4
  • 20
    • 77957354322 scopus 로고    scopus 로고
    • Extracellular production of recombinant proteins using bacterial autotransporters
    • Jong W.S., Sauri A., Luirink J. Extracellular production of recombinant proteins using bacterial autotransporters. Curr Opin Biotechnol 2010, 21(5):646-652.
    • (2010) Curr Opin Biotechnol , vol.21 , Issue.5 , pp. 646-652
    • Jong, W.S.1    Sauri, A.2    Luirink, J.3
  • 21
    • 84921732024 scopus 로고    scopus 로고
    • Autotransporter-based cell surface display in Gram-negative bacteria
    • Nicolay T., Vanderleyden J., Spaepen S. Autotransporter-based cell surface display in Gram-negative bacteria. Crit Rev Microbiol 2013, 10.3109/1040841X.2013.804032.
    • (2013) Crit Rev Microbiol
    • Nicolay, T.1    Vanderleyden, J.2    Spaepen, S.3
  • 23
    • 84865048949 scopus 로고    scopus 로고
    • A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters
    • Celik N., Webb C.T., Leyton D.L., Holt K.E., Heinz E., Gorrell R., et al. A bioinformatic strategy for the detection, classification and analysis of bacterial autotransporters. PLoS ONE 2012, 7(8):432-445.
    • (2012) PLoS ONE , vol.7 , Issue.8 , pp. 432-445
    • Celik, N.1    Webb, C.T.2    Leyton, D.L.3    Holt, K.E.4    Heinz, E.5    Gorrell, R.6
  • 24
    • 79955813920 scopus 로고    scopus 로고
    • Strain engineering for improved expression of recombinant proteins in bacteria
    • Makino T., Skretas G., Georgiou G. Strain engineering for improved expression of recombinant proteins in bacteria. Microb Cell Fact 2011, 10:32.
    • (2011) Microb Cell Fact , vol.10 , pp. 32
    • Makino, T.1    Skretas, G.2    Georgiou, G.3
  • 25
    • 3543063987 scopus 로고    scopus 로고
    • Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts
    • Becker S., Schmoldt H.U., Adams T.M., Wilhelm S., Kolmar H. Ultra-high-throughput screening based on cell-surface display and fluorescence-activated cell sorting for the identification of novel biocatalysts. Curr Opin Biotechnol 2004, 15(4):323-329.
    • (2004) Curr Opin Biotechnol , vol.15 , Issue.4 , pp. 323-329
    • Becker, S.1    Schmoldt, H.U.2    Adams, T.M.3    Wilhelm, S.4    Kolmar, H.5
  • 26
    • 33947142544 scopus 로고    scopus 로고
    • Pilot-scale production of 1,3-propanediol using Klebsiella pneumoniae
    • Cheng K.K., Zhang J.A., Liu D.H., Sun Y., Liu H.J., Yang M.D., et al. Pilot-scale production of 1,3-propanediol using Klebsiella pneumoniae. Process Biochem 2007, 42(4):740-744.
    • (2007) Process Biochem , vol.42 , Issue.4 , pp. 740-744
    • Cheng, K.K.1    Zhang, J.A.2    Liu, D.H.3    Sun, Y.4    Liu, H.J.5    Yang, M.D.6
  • 27
    • 79952694448 scopus 로고    scopus 로고
    • Microbial 2,3-butanediol production: a state-of-the-art review
    • Ji X.J., Huang H., Ouyang P.K. Microbial 2,3-butanediol production: a state-of-the-art review. Biotechnol Adv 2011, 29(3):351-364.
    • (2011) Biotechnol Adv , vol.29 , Issue.3 , pp. 351-364
    • Ji, X.J.1    Huang, H.2    Ouyang, P.K.3
  • 28
    • 34447511485 scopus 로고    scopus 로고
    • Today's and tomorrow's bio-based bulk chemicals from white biotechnology - a techno-economic analysis
    • Hermann B.G., Patel M. Today's and tomorrow's bio-based bulk chemicals from white biotechnology - a techno-economic analysis. Appl Biochem Biotechnol 2007, 136(3):361-388.
    • (2007) Appl Biochem Biotechnol , vol.136 , Issue.3 , pp. 361-388
    • Hermann, B.G.1    Patel, M.2
  • 30
    • 33845252930 scopus 로고    scopus 로고
    • Fuels of the future
    • Reisch M.S. Fuels of the future. Chem Eng News 2006, 84(47):30-32.
    • (2006) Chem Eng News , vol.84 , Issue.47 , pp. 30-32
    • Reisch, M.S.1
  • 31
    • 84940953332 scopus 로고    scopus 로고
    • DuPont Cellulosic Ethanol Biorefinery Project
    • United States of America. [accessed 15.10.14].
    • chemicals-technology.com. DuPont Cellulosic Ethanol Biorefinery Project. United States of America. [accessed 15.10.14]. http://www.chemicals-technology.com/projects/dupont-cellulosic-ethanol-biorefinery-project/.
  • 32
    • 45849142238 scopus 로고    scopus 로고
    • Biotechnological applications of acetic acid bacteria
    • Raspor P., Goranovic D. Biotechnological applications of acetic acid bacteria. Crit Rev Biotechnol 2008, 28(2):101-124.
    • (2008) Crit Rev Biotechnol , vol.28 , Issue.2 , pp. 101-124
    • Raspor, P.1    Goranovic, D.2
  • 33
    • 84912054030 scopus 로고    scopus 로고
    • Autotransporter mediated esterase display on Zymomonas mobilis and Zymobacter palmae
    • Tozakidis I.E., Sichwart S., Teese M.G., Jose J. Autotransporter mediated esterase display on Zymomonas mobilis and Zymobacter palmae. J Biotechnol 2014, 10.1016/j.jbiotec.2014.07.009.
    • (2014) J Biotechnol
    • Tozakidis, I.E.1    Sichwart, S.2    Teese, M.G.3    Jose, J.4
  • 34
    • 38549133764 scopus 로고    scopus 로고
    • EhaA is a novel autotransporter protein of enterohemorrhagic Escherichia coli O157:H7 that contributes to adhesion and biofilm formation
    • Wells T.J., Sherlock O., Rivas L., Mahajan A., Beatson S.A., Torpdahl M., et al. EhaA is a novel autotransporter protein of enterohemorrhagic Escherichia coli O157:H7 that contributes to adhesion and biofilm formation. Environ Microbiol 2008, 10(3):589-604.
    • (2008) Environ Microbiol , vol.10 , Issue.3 , pp. 589-604
    • Wells, T.J.1    Sherlock, O.2    Rivas, L.3    Mahajan, A.4    Beatson, S.A.5    Torpdahl, M.6
  • 35
    • 84865167599 scopus 로고    scopus 로고
    • Production host selection for asymmetric styrene epoxidation: Escherichia coli vs. solvent-tolerant Pseudomonas
    • Kuhn D., Buhler B., Schmid A. Production host selection for asymmetric styrene epoxidation: Escherichia coli vs. solvent-tolerant Pseudomonas. J Ind Microbiol Biotechnol 2012, 39(8):1125-1133.
    • (2012) J Ind Microbiol Biotechnol , vol.39 , Issue.8 , pp. 1125-1133
    • Kuhn, D.1    Buhler, B.2    Schmid, A.3
  • 37
    • 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 L.A. 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
  • 38
    • 84864693945 scopus 로고    scopus 로고
    • Synthetic phytochelatin surface display in Cupriavidus metallidurans CH34 for enhanced metals bioremediation
    • Biondo R., da Silva F.A., Vicente E.J., Souza Sarkis J.E., Schenberg A.C. Synthetic phytochelatin surface display in Cupriavidus metallidurans CH34 for enhanced metals bioremediation. Environ Sci Technol 2012, 46(15):8325-8332.
    • (2012) Environ Sci Technol , vol.46 , Issue.15 , pp. 8325-8332
    • Biondo, R.1    da Silva, F.A.2    Vicente, E.J.3    Souza Sarkis, J.E.4    Schenberg, A.C.5
  • 39
    • 0034732652 scopus 로고    scopus 로고
    • Engineering outer-membrane proteins in Pseudomonas putida for enhanced heavy-metal bioadsorption
    • Valls M., de Lorenzo V., Gonzalez-Duarte R., Atrian S. Engineering outer-membrane proteins in Pseudomonas putida for enhanced heavy-metal bioadsorption. J Inorg Biochem 2000, 79(1-4):219-223.
    • (2000) J Inorg Biochem , vol.79 , Issue.1-4 , pp. 219-223
    • Valls, M.1    de Lorenzo, V.2    Gonzalez-Duarte, R.3    Atrian, S.4
  • 43
    • 84864096711 scopus 로고    scopus 로고
    • Enhanced 2,3-butanediol production in recombinant Klebsiella pneumoniae via overexpression of synthesis-related genes
    • Kim B., Lee S., Park J., Lu M., Oh M., Kim Y., et al. Enhanced 2,3-butanediol production in recombinant Klebsiella pneumoniae via overexpression of synthesis-related genes. J Microbiol Biotechnol 2012, 22(9):1258-1263.
    • (2012) J Microbiol Biotechnol , vol.22 , Issue.9 , pp. 1258-1263
    • Kim, B.1    Lee, S.2    Park, J.3    Lu, M.4    Oh, M.5    Kim, Y.6
  • 44
    • 0942288120 scopus 로고    scopus 로고
    • Bacteria engineered for fuel ethanol production: current status
    • Dien B.S., Cotta M.A., Jeffries T.W. Bacteria engineered for fuel ethanol production: current status. Appl Microbiol Biotechnol 2003, 63(3):258-266.
    • (2003) Appl Microbiol Biotechnol , vol.63 , Issue.3 , pp. 258-266
    • Dien, B.S.1    Cotta, M.A.2    Jeffries, T.W.3
  • 45
    • 0025806975 scopus 로고
    • Molecular biology of Erwinia - from soft-rot to antileukemics
    • Robertbaudouy J. Molecular biology of Erwinia - from soft-rot to antileukemics. Trends Biotechnol 1991, 9(9):325-329.
    • (1991) Trends Biotechnol , vol.9 , Issue.9 , pp. 325-329
    • Robertbaudouy, J.1
  • 46
    • 34548589193 scopus 로고    scopus 로고
    • The genus Gluconobacter oxydans: comprehensive overview of biochemistry and biotechnological applications
    • De Muynck C., Pereira C.S.S., Naessens M., Parmentier S., Soetaert W., Vandamme E.J. The genus Gluconobacter oxydans: comprehensive overview of biochemistry and biotechnological applications. Crit Rev Biotechnol 2007, 27(3):147-171.
    • (2007) Crit Rev Biotechnol , vol.27 , Issue.3 , pp. 147-171
    • De Muynck, C.1    Pereira, C.S.S.2    Naessens, M.3    Parmentier, S.4    Soetaert, W.5    Vandamme, E.J.6
  • 47
    • 68049135724 scopus 로고    scopus 로고
    • Engineering alternative butanol production platforms in heterologous bacteria
    • Nielsen D.R., Leonard E., Yoon S.H., Tseng H.C., Yuan C., Prather K.L. Engineering alternative butanol production platforms in heterologous bacteria. Metab Eng 2009, 11(4/5):262-273.
    • (2009) Metab Eng , vol.11 , Issue.4-5 , pp. 262-273
    • Nielsen, D.R.1    Leonard, E.2    Yoon, S.H.3    Tseng, H.C.4    Yuan, C.5    Prather, K.L.6
  • 48
    • 27844581254 scopus 로고    scopus 로고
    • Production of recombinant proteins by high cell density culture of Escherichia coli
    • Choi J.H., Keum K.C., Lee S.Y. Production of recombinant proteins by high cell density culture of Escherichia coli. Chem Eng Sci 2006, 61(3):876-885.
    • (2006) Chem Eng Sci , vol.61 , Issue.3 , pp. 876-885
    • Choi, J.H.1    Keum, K.C.2    Lee, S.Y.3
  • 49
    • 8144220709 scopus 로고    scopus 로고
    • High-cell-density cultivation of Pseudomonas putida IPT 046 and medium-chain-length polyhydroxyalkanoate production from sugarcane carbohydrates
    • Diniz S.C., Taciro M.K., Gomez J.G., da Cruz Pradella J.G. High-cell-density cultivation of Pseudomonas putida IPT 046 and medium-chain-length polyhydroxyalkanoate production from sugarcane carbohydrates. Appl Biochem Biotechnol 2004, 119(1):51-70.
    • (2004) Appl Biochem Biotechnol , vol.119 , Issue.1 , pp. 51-70
    • Diniz, S.C.1    Taciro, M.K.2    Gomez, J.G.3    da Cruz Pradella, J.G.4
  • 50
    • 0036956671 scopus 로고    scopus 로고
    • A novel high-cell-density protein expression system based on Ralstonia eutropha
    • Srinivasan S., Barnard G.C., Gerngross T.U. A novel high-cell-density protein expression system based on Ralstonia eutropha. Appl Environ Microbiol 2002, 68(12):5925-5932.
    • (2002) Appl Environ Microbiol , vol.68 , Issue.12 , pp. 5925-5932
    • Srinivasan, S.1    Barnard, G.C.2    Gerngross, T.U.3
  • 51
    • 20444491993 scopus 로고    scopus 로고
    • Ethanol production from cellobiose by Zymobacter palmae carrying the Ruminocuccus albus beta-glucosidase gene
    • Yanase H., Yamamoto K., Sato D., Okamoto K. Ethanol production from cellobiose by Zymobacter palmae carrying the Ruminocuccus albus beta-glucosidase gene. J Biotechnol 2005, 118(1):35-43.
    • (2005) J Biotechnol , vol.118 , Issue.1 , pp. 35-43
    • Yanase, H.1    Yamamoto, K.2    Sato, D.3    Okamoto, K.4
  • 52
    • 0035104458 scopus 로고    scopus 로고
    • Mobilization function of the pBHR1 plasmid, a derivative of the broad-host-range plasmid pBBR1
    • Szpirer C.Y., Faelen M., Couturier M. Mobilization function of the pBHR1 plasmid, a derivative of the broad-host-range plasmid pBBR1. J Bacteriol 2001, 183(6):2101-2110.
    • (2001) J Bacteriol , vol.183 , Issue.6 , pp. 2101-2110
    • Szpirer, C.Y.1    Faelen, M.2    Couturier, M.3
  • 53
    • 84892950934 scopus 로고    scopus 로고
    • Autodisplay for the co-expression of lipase and foldase on the surface of E. coli: washing with designer bugs
    • Kranen E., Detzel C., Weber T., Jose J. Autodisplay for the co-expression of lipase and foldase on the surface of E. coli: washing with designer bugs. Microb Cell Fact 2014, 13(1):19.
    • (2014) Microb Cell Fact , vol.13 , Issue.1 , pp. 19
    • Kranen, E.1    Detzel, C.2    Weber, T.3    Jose, J.4
  • 54
    • 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 T.F. 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
  • 55
    • 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
  • 56
    • 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 T.F. 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
  • 57
    • 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 T.F. 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
  • 58
    • 37349047429 scopus 로고    scopus 로고
    • The autodisplay story, from discovery to biotechnical and biomedical applications
    • Jose J., Meyer T.F. The autodisplay story, from discovery to biotechnical and biomedical applications. Microbiol Mol Biol Rev 2007, 71(4):600-619.
    • (2007) Microbiol Mol Biol Rev , vol.71 , Issue.4 , pp. 600-619
    • Jose, J.1    Meyer, T.F.2
  • 59
    • 33751056360 scopus 로고    scopus 로고
    • Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif
    • Robert V., Volokhina E.B., Senf F., Bos M.P., Van Gelder P., Tommassen J. Assembly factor Omp85 recognizes its outer membrane protein substrates by a species-specific C-terminal motif. PLoS Biol 2006, 4(11):e377.
    • (2006) PLoS Biol , vol.4 , Issue.11 , pp. e377
    • Robert, V.1    Volokhina, E.B.2    Senf, F.3    Bos, M.P.4    Van Gelder, P.5    Tommassen, J.6
  • 60
    • 13844257519 scopus 로고    scopus 로고
    • A generic system for the Escherichia coli cell-surface display of lipolytic enzymes
    • Becker S., Theile S., Heppeler N., Michalczyk A., Wentzel A., Wilhelm S., et al. A generic system for the Escherichia coli cell-surface display of lipolytic enzymes. FEBS Lett 2005, 579(5):1177-1182.
    • (2005) FEBS Lett , vol.579 , Issue.5 , pp. 1177-1182
    • Becker, S.1    Theile, S.2    Heppeler, N.3    Michalczyk, A.4    Wentzel, A.5    Wilhelm, S.6
  • 61
    • 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 T.H., Pan J.G., Seo Y.S., Rhee J.S. 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
  • 62
    • 78049375319 scopus 로고    scopus 로고
    • Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters
    • Marin E., Bodelon G., Fernandez L.A. Comparative analysis of the biochemical and functional properties of C-terminal domains of autotransporters. J Bacteriol 2010, 192(21):5588-5602.
    • (2010) J Bacteriol , vol.192 , Issue.21 , pp. 5588-5602
    • Marin, E.1    Bodelon, G.2    Fernandez, L.A.3
  • 63
    • 84870864144 scopus 로고    scopus 로고
    • Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15
    • Nicolay T., Lemoine L., Lievens E., Balzarini S., Vanderleyden J., Spaepen S. Probing the applicability of autotransporter based surface display with the EstA autotransporter of Pseudomonas stutzeri A15. Microb Cell Fact 2012, 11:158.
    • (2012) Microb Cell Fact , vol.11 , pp. 158
    • Nicolay, T.1    Lemoine, L.2    Lievens, E.3    Balzarini, S.4    Vanderleyden, J.5    Spaepen, S.6
  • 64
    • 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
  • 65
    • 62249123251 scopus 로고    scopus 로고
    • Surface display of the receptor-binding domain of the F17a-G fimbrial adhesin through the autotransporter AIDA-I leads to permeability of bacterial cells
    • Van Gerven N., Sleutel M., Deboeck F., De Greve H., Hernalsteens J.P. Surface display of the receptor-binding domain of the F17a-G fimbrial adhesin through the autotransporter AIDA-I leads to permeability of bacterial cells. Microbiology 2009, 155(Pt 2):468-476.
    • (2009) Microbiology , vol.155 , pp. 468-476
    • Van Gerven, N.1    Sleutel, M.2    Deboeck, F.3    De Greve, H.4    Hernalsteens, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.