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J Microbiol Biotechnol. 2015 Jul;25(7):953-62. doi: 10.4014/jmb.1412.12079.

Production of Biopharmaceuticals in E. coli: Current Scenario and Future Perspectives.

Author information

1
Department of Biological Sciences, Faculty of Science, King Abdulaziz University, Jeddah, 21589, Saudi Arabia.
2
Department of Biotechnology, Eternal University, Baru Sahib-173 101, Himachal Pradesh, India.
3
Nucleic Acids Research Department, Genetic Engineering and Biotechnology Research Institute (GEBRI), City for Scientific Research and Technology Applications, Alexandria 21934, Egypt.
4
Cell Biology Department, Genetic Engineering and Biotechnology Division, National Research Centre, Dokki-Cairo 12311, Egypt.
5
Protein Research Department, Genetic Engineering and Biotechnology Research Institute, City for Scientific Research and Applied Technology, New Borg AL-Arab, Alexandria 21934, Egypt.

Abstract

Escherichia coli is the most preferred microorganism to express heterologous proteins for therapeutic use, as around 30% of the approved therapeutic proteins are currently being produced using it as a host. Owing to its rapid growth, high yield of the product, cost-effectiveness, and easy scale-up process, E. coli is an expression host of choice in the biotechnology industry for large-scale production of proteins, particularly non-glycosylated proteins, for therapeutic use. The availability of various E. coli expression vectors and strains, relatively easy protein folding mechanisms, and bioprocess technologies, makes it very attractive for industrial applications. However, the codon usage in E. coli and the absence of post-translational modifications, such as glycosylation, phosphorylation, and proteolytic processing, limit its use for the production of slightly complex recombinant biopharmaceuticals. Several new technological advancements in the E. coli expression system to meet the biotechnology industry requirements have been made, such as novel engineered strains, genetically modifying E. coli to possess capability to glycosylate heterologous proteins and express complex proteins, including full-length glycosylated antibodies. This review summarizes the recent advancements that may further expand the use of the E. coli expression system to produce more complex and also glycosylated proteins for therapeutic use in the future.

KEYWORDS:

Biopharmaceuticals; Codon usage; E. coli; Molecular chaperones; Optimized protein production

PMID:
25737124
DOI:
10.4014/jmb.1412.12079
[Indexed for MEDLINE]
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