Escherichia coli is the organism 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 recombinant 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.

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Recombinant protein expression in Escherichia coli: advances and challenges.

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.

Recombinant protein folding and misfolding in Escherichia coli.

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In order for any biological system to function effectively, it is essential to avoid the inherent tendency of proteins to aggregate and form potentially harmful deposits. In each of the various pathological conditions associated with protein deposition, such as Alzheimer's and Parkinson's diseases, a specific peptide or protein that is normally soluble is deposited as insoluble aggregates generally referred to as amyloid. It is clear that the aggregation process is generally initiated from partially or completely unfolded forms of the peptides and proteins associated with each disease. Here we show that the intrinsic effects of specific mutations on the rates of aggregation of unfolded polypeptide chains can be correlated to a remarkable extent with changes in simple physicochemical properties such as hydrophobicity, secondary structure propensity and charge. This approach allows the pathogenic effects of mutations associated with known familial forms of protein deposition diseases to be rationalized, and more generally enables prediction of the effects of mutations on the aggregation propensity of any polypeptide chain.

/pdf/rationalization-of-the-effects-of-mutations-on-peptide-and-ud2nqo1h21.pdf

Rationalization of the effects of mutations on peptide and protein aggregation rates.

http://teachline.ls.huji.ac.il/72682/Publications/Sorensen2005.pdf

Advanced genetic strategies for recombinant protein expression in Escherichia coli.

Protein aggregation is an ordinary consequence of thermal stress. In recombinant bacteria, the over-expression of plasmid-encoded genes triggers transcription of heat-shock genes and other stress responses and often results in the aggregation of the encoded protein as inclusion bodies. The formation of these deposits represents a major obstacle for the production of biologically active polypeptides and restricts the spectrum of protein products being available for the industrial-biomedical market. Inclusion body formation was formerly considered to occur passively by the irretrievable deposition of partially-folded intermediates. Increasing evidence, however, indicates that protein aggregation in bacteria occurs as a reversible process deeply integrated in the cell mechanisms for coping with thermal stress, and that inclusion bodies are structurally dynamic structures. Inclusion body formation might actually be supported by the cellular machinery that when operated under specific stress conditions, transiently stores misfolded polypeptides until they could be further processed: either refolded or proteolysed. A better understanding of protein aggregation in cell physiology could allow not only inclusion body formation to be minimized more efficiently for a higher soluble yield, but also to comprehend in detail the intricacy of cell mechanisms committed to handling the misfolding danger.

Protein aggregation in recombinant bacteria: biological role of inclusion bodies

Amyloid-like Properties of Bacterial Inclusion Bodies

Construction and deconstruction of bacterial inclusion bodies.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2801%2902073-7

Protein aggregation as bacterial inclusion bodies is reversible.

https://febs.onlinelibrary.wiley.com/doi/pdf/10.1016/S0014-5793%2800%2901357-0

Mar Carrió

Papers

Protein aggregation in recombinant bacteria: biological role of inclusion bodies

Amyloid-like Properties of Bacterial Inclusion Bodies

Construction and deconstruction of bacterial inclusion bodies.

Protein aggregation as bacterial inclusion bodies is reversible.

Fine architecture of bacterial inclusion bodies