The past 20 years have seen enormous progress in the understanding of the mechanisms used by the enteric bacterium Escherichia coli to promote protein folding, support protein translocation and handle protein misfolding. Insights from these studies have been exploited to tackle the problems of inclusion body formation, proteolytic degradation and disulfide bond generation that have long impeded the production of complex heterologous proteins in a properly folded and biologically active form. The application of this information to industrial processes, together with emerging strategies for creating designer folding modulators and performing glycosylation all but guarantee that E. coli will remain an important host for the production of both commodity and high value added proteins.
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This work was supported by National Science Fund award BES-0097430.
The authors declare no competing financial interests.
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Baneyx, F., Mujacic, M. Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22, 1399–1408 (2004). https://doi.org/10.1038/nbt1029
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