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Many of the most effective new treatments for cancer, arthritis and other conditions are protein-based biologic drugs that have to be manufactured using living cells such as bacteria.
Escherichia coli is a widely used host for production of recombinant proteins for biologics. Although high levels of protein secretion can be achieved, this is often followed by low-yield down-stream processing to extract functional proteins. Furthermore, at higher protein yields (>10g/L), non-specific leakage of cytoplasmic content is often observed, which includes release of DNA that increases media viscosity, resulting in further decreased yields and higher production costs. Downstream processing represents a bottleneck within the Industrial Biotechnology industry and approaches to reduce costs of this step will grow in importance as higher product yields continue to be achieved.
Escherichia coli is a major workhorse organism used by industrial biotechnology as a cell factory for overproduction of diverse commercial protein products. This includes biopharmaceuticals (biologics) and industrial enzymes. However, relatively little is known of physiology during high-level protein production or secretion.
Bacterial “cell factories” can sometimes release these therapeutic proteins prematurely, which could account for the low yield observed in some cases. This research aimed to investigate the phenomenon further, leading to a better understanding of biologic drug production in bacterial cells.
Industrial Biotechnology increasingly uses genetically-enhanced production cells to biosynthesise non-native chemical products. Being non-native and high concentration, such products often are toxic to the production cell.
This being so, many putative products applied externally to test for compatibility with the production cell will not cross the membrane, so intracellular cytotoxicity – the key IB question – is not assayed.