Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein

Sommer B, Friehs K, Flaschel E, Reck M, Stahl F, Scheper T (2009)
JOURNAL OF BIOTECHNOLOGY 140(3-4): 194-202.

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Zeitschriftenaufsatz | Veröffentlicht | Englisch
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Abstract / Bemerkung
Recombinant proteins are essential products of today's industrial biotechnology. In this study we address two crucial factors in recombinant protein production: (i) product accessibility and (ii) product recovery. Escherichia coli, one of the most frequently used hosts for recombinant protein expression, does not inherently secrete proteins into the extracellular environment. The major drawback of this expression system is, therefore, to be found in the intracellular protein accumulation and hampered product accessibility. We have constructed a set of expression vectors in order to facilitate extracellular protein production and purification. The maltose binding protein from E call is used as fusion partner for several proteins of interest allowing an export to the bacteria's periplasm via both the Sec and the Tat pathway. Upon coexpression of a modified Cloacin DF13 bacteriocin release protein, the hybrid proteins are released into the culture medium. This essentially applies to a distinguished reporter molecule, the green fluorescent protein, for which an extracellular production was not reported so far. The sequestered proteins can be purified to approximate homogeneity by a simple, rapid and cheap procedure which utilizes the affinity of the maltose binding protein to alpha-1,4-glucans. (C) 2009 Elsevier B.V. All rights reserved.
Erscheinungsjahr
Zeitschriftentitel
JOURNAL OF BIOTECHNOLOGY
Band
140
Ausgabe
3-4
Seite(n)
194-202
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Sommer B, Friehs K, Flaschel E, Reck M, Stahl F, Scheper T. Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein. JOURNAL OF BIOTECHNOLOGY. 2009;140(3-4):194-202.
Sommer, B., Friehs, K., Flaschel, E., Reck, M., Stahl, F., & Scheper, T. (2009). Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein. JOURNAL OF BIOTECHNOLOGY, 140(3-4), 194-202. doi:10.1016/j.jbiotec.2009.01.010
Sommer, B., Friehs, K., Flaschel, E., Reck, M., Stahl, F., and Scheper, T. (2009). Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein. JOURNAL OF BIOTECHNOLOGY 140, 194-202.
Sommer, B., et al., 2009. Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein. JOURNAL OF BIOTECHNOLOGY, 140(3-4), p 194-202.
B. Sommer, et al., “Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein”, JOURNAL OF BIOTECHNOLOGY, vol. 140, 2009, pp. 194-202.
Sommer, B., Friehs, K., Flaschel, E., Reck, M., Stahl, F., Scheper, T.: Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein. JOURNAL OF BIOTECHNOLOGY. 140, 194-202 (2009).
Sommer, Benjamin, Friehs, Karl, Flaschel, Erwin, Reck, Michael, Stahl, Frank, and Scheper, Thomas. “Extracellular production and affinity purification of recombinant proteins with Escherichia coli using the versatility of the maltose binding protein”. JOURNAL OF BIOTECHNOLOGY 140.3-4 (2009): 194-202.

7 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

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37 References

Daten bereitgestellt von Europe PubMed Central.

Protein targeting by the bacterial twin-arginine translocation (Tat) pathway.
Berks BC, Palmer T, Sargent F., Curr. Opin. Microbiol. 8(2), 2005
PMID: 15802249
The complete genome sequence of Escherichia coli K-12.
Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y., Science 277(5331), 1997
PMID: 9278503
Hybrid bacillus endo-(1-3,1-4)-beta-glucanases: construction of recombinant genes and molecular properties of the gene products.
Borriss R, Olsen O, Thomsen KK, von Wettstein D., Carlsberg Res. Commun. 54(2), 1989
PMID: 2673278
Secretory and extracellular production of recombinant proteins using Escherichia coli.
Choi JH, Lee SY., Appl. Microbiol. Biotechnol. 64(5), 2004
PMID: 14966662
Improved green fluorescent protein by molecular evolution using DNA shuffling.
Crameri A, Whitehorn EA, Tate E, Stemmer WP., Nat. Biotechnol. 14(3), 1996
PMID: 9630892
Production and release of cloacin DF13 and related colicins.
De Graaf FK, Oudega B., Curr. Top. Microbiol. Immunol. 125(), 1986
PMID: 3527577
Precursor maltose-binding protein is active in binding substrate.
Ferenci T, Randall LL., J. Biol. Chem. 254(20), 1979
PMID: 385604
Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter.
Guzman LM, Belin D, Carson MJ, Beckwith J., J. Bacteriol. 177(14), 1995
PMID: 7608087
New method for generating deletions and gene replacements in Escherichia coli.
Hamilton CM, Aldea M, Washburn BK, Babitzke P, Kushner SR., J. Bacteriol. 171(9), 1989
PMID: 2548993
Barstar inhibits extracellular ribonucleases of Streptomyces and allows their production from recombinant genes
Hartley, Protein Peptide Lett. 3(), 1996
Fusions of secreted proteins to alkaline phosphatase: an approach for studying protein secretion.
Hoffman CS, Wright A., Proc. Natl. Acad. Sci. U.S.A. 82(15), 1985
PMID: 3860846
Functioning of the stable signal peptide of the pCloDF13-encoded bacteriocin release protein.
Luirink J, Duim B, de Gier JW, Oudega B., Mol. Microbiol. 5(2), 1991
PMID: 2041475
An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein.
Maina CV, Riggs PD, Grandea AG 3rd, Slatko BE, Moran LS, Tagliamonte JA, McReynolds LA, Guan CD., Gene 74(2), 1988
PMID: 3073105

Sambrook, 2001
Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli.
Shokri A, Sanden AM, Larsson G., Appl. Microbiol. Biotechnol. 60(6), 2002
PMID: 12664143

AUTHOR UNKNOWN, 0
Mutants of Escherichia coli constitutive for alkaline phosphatase.
TORRIANI A, ROTHMAN F., J. Bacteriol. 81(), 1961
PMID: 13777588
Bacteriocin release proteins: mode of action, structure, and biotechnological application.
van der Wal FJ, Luirink J, Oudega B., FEMS Microbiol. Rev. 17(4), 1995
PMID: 8845188
Production of supercoiled multimeric plasmid DNA for biopharmaceutical application.
Voss C, Schmidt T, Schleef M, Friehs K, Flaschel E., J. Biotechnol. 105(3), 2003
PMID: 14580792

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