Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
Review
. 2014 Apr 17:5:172.
doi: 10.3389/fmicb.2014.00172. eCollection 2014.

Recombinant protein expression in Escherichia coli: advances and challenges

Germán L Rosano  1 , Eduardo A Ceccarelli  1
Affiliations
Review

Recombinant protein expression in Escherichia coli: advances and challenges

Germán L Rosano et al. Front Microbiol. .

Abstract

Escherichia coli is one of the organisms of choice for the production of recombinant proteins. Its use as a cell factory is well-established and it has become the most popular expression platform. For this reason, there are many molecular tools and protocols at hand for the high-level production of heterologous proteins, such as a vast catalog of expression plasmids, a great number of engineered strains and many cultivation strategies. We review the different approaches for the synthesis of recombinant proteins in E. coli and discuss recent progress in this ever-growing field.

Keywords: E. coli expression strains; Escherichia coli; affinity tags; expression plasmid; inclusion bodies; recombinant protein expression.

PubMed Disclaimer

Figures

FIGURE 1
FIGURE 1
Anatomy of an expression vector. The figure depicts the major features present in common expression vectors. All of them are described in the text. The affinity tags and coding sequences for their removal were positioned arbitrarily at the N-terminus for simplicity. MCS, multiple cloning site. Striped patterned box: coding sequence for the desired protein.
See this image and copyright information in PMC

Comment in

References

    1. Adrio J. L., Demain A. L. (2010). Recombinant organisms for production of industrial products. Bioeng. Bugs 1 116–131 10.4161/bbug.1.2.10484 - DOI - PMC - PubMed
    1. Alibolandi M., Mirzahoseini H. (2011). Chemical assistance in refolding of bacterial inclusion bodies. Biochem. Res. Int. 2011:631607 10.1155/2011/631607 - DOI - PMC - PubMed
    1. Andreev Y. A., Kozlov S. A., Vassilevski A. A., Grishin E. V. (2010). Cyanogen bromide cleavage of proteins in salt and buffer solutions. Anal. Biochem. 407 144–146 10.1016/j.ab.2010.07.023 - DOI - PubMed
    1. Angov E., Legler P. M., Mease R. M. (2011). Adjustment of codon usage frequencies by codon harmonization improves protein expression and folding. Methods Mol. Biol. 705 1–13 10.1007/978-1-61737-967-3_1 - DOI - PubMed
    1. Atlas R. M. (2004). Handbook of Microbiological Media, 3rd Edn. Boca Raton, FL: Taylor & Francis