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Co-expression for intracellular processing in microbial protein production

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Abstract

The biological activity of a recombinant protein is highly dependent on its biophysical properties including post-translational modifications, solubility, and stability. Production of active recombinant proteins requires careful design of the expression strategy and purification schemes. This is often achieved by proper modification of the target protein during and/or after protein synthesis in the host cells. Such co-translational or post-translational processing of recombinant proteins is typically enabled by co-expressing the required enzymes, folding chaperones, co-factors and/or processing enzymes in the host. Various applications of the co-expression technology in protein production are discussed in this review with representative examples described.

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Acknowledgments

We thank Edward Appelbaum, Robert Ames, Angela Bridges, Andrew Fosberry, Murray Brown, and James Fornwald for critical reading of the manuscript. Support from authors’ line managers at GlaxoSmithKline is greatly appreciated.

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  1. Department of Biological Reagents & Assay Development, Platform Technology & Science, GlaxoSmithKline, 1250 South Collegeville Road, Collegeville, PA, 19426, USA

    Quinn Lu

  2. Microbial Cell Culture Development, BioPharm R&D, GlaxoSmithKline, 709 Swedeland Road, King of Prussia, PA, 19406, USA

    Juan C. Aon

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Correspondence to Quinn Lu.

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Lu, Q., Aon, J.C. Co-expression for intracellular processing in microbial protein production. Biotechnol Lett 36, 427–441 (2014). https://doi.org/10.1007/s10529-013-1379-z

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