Engineering of efficient escherichia coli excretion systems for the production of heterologous proteins for commercial applications

被引：0
作者：
Wong, W.K.R. [1 ]
Fu, Zhibiao [2 ]
Wang, Yule Y. [1 ]
Ng, K.L. [1 ]
Chan, Anthony K.N. [1 ]
机构：
[1] Division of Life Science, The Hong Kong University of Science and Technology, Clear Water Bay, Kowloon, Hong Kong
[2] GlaxoSmithKline, Microbial and Cell Culture Development, King of Prussia, PA 19406
来源：
Recent Patents on Chemical Engineering | 2012年 / 5卷 / 01期
关键词：
Diabetic foot ulcers; Escherichia coli; Excretion; HEGF; Heterologous proteins; Periplasm; Secretion; SecYEG pathway; Skincare applications;
D O I：
10.2174/1874478811205010045
中图分类号：
学科分类号：
摘要：
Extracellular production of recombinant proteins using bacterial systems such as Escherichia coli has many advantages, including preferred protein properties, e.g. N-terminal authenticity, correct disulfide linkages, high product bioactivity and stability, and simplified downstream processing. This approach offers an impressive choice to the expression of naturally secretory proteins of which posttranslational modifications are non-essential for biological functions. In this communication, we review recent advances and patents obtained in excretory production of recombinant proteins in E. coli, making use of human epidermal growth factor (hEGF) as a model protein to illustrate how this approach has facilitated efficient production of hEGF. This enables affordable supply for an elaborate assessment of the biological functions of hEGF and subsequently its application to the development of a wide range of skincare and medically-oriented products for commercial applications. © 2012 Bentham Science Publishers.
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页码：45 / 55
页数：10
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共 85 条
  • [1] Sheridan C., Fresh from the biologic pipeline-2009, Nat. Biotechnol, 28, pp. 307-310, (2010)
  • [2] Walsh G., Biopharmaceutical benchmarks 2006, Nat. Biotechnol, 24, pp. 769-776, (2006)
  • [3] Recombinant protein expression in Escherichia coli, Curr. Opin. Biotechnol, 10, pp. 411-421, (1999)
  • [4] Swartz J.R., Advances in Escherichia coli production of therapeutic proteins, Curr. Opin. Biotechnol, 12, pp. 195-201, (2001)
  • [5] Walsh G., Biopharmaceutical benchmarks 2010, Nat. Biotechnol, 28, pp. 917-924, (2010)
  • [6] Singh S.M., Panda A.K., Solubilization and refolding of bacterial inclusion body proteins, J. Biosci. Bioeng, 99, pp. 303-310, (2005)
  • [7] Burgess R.R., Refolding solubilized inclusion body proteins, Methods Enzymol, 463, pp. 259-282, (2009)
  • [8] Choi J.H., Jeong K.J., Kim S.C., Lee S.Y., Efficient secretory production of alkaline phosphatase by high cell density culture of recom-binant Escherichia coli using the Bacillus sp. endoxylanase signal sequence, Appl. Microbiol. Biotechnol, 53, pp. 640-645, (2000)
  • [9] Joly J.C., Protease-deficient Cells, (2005)
  • [10] Natale P., Bruser T., Driessen A.J.M., Sec-and Tat-mediated protein secretion across the bacterial cytoplasmic membrane--distinct translocases and mechanisms, Biochim. Biophys. Acta, 1778, pp. 1735-1756, (2008)
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