The Cambridge, UK-based biotech firm has acquired the license for the exclusive rights to the CyDisCo (Cytoplasmic Disulphide bond formation in E. coli) protein production technology, developed by the University of Oulu.
The platform is an expression technology which enables E. coli to make biologically active products of proteins which have disulphide bonds in their structure, and according to BioSilta's R&D director Antti Vasala, around 30% of antibodies, growth hormone, interleukins have this characteristic.
“In CyDisCo, two key proteins of eukaryotic protein folding machinery have been introduced to E. coli,” he told Biopharma-Reporter.com. “These helper proteins are coexpressed with the recombinant protein being produced. As a result, the recombinant protein will reach a correctly folded conformation and accumulate inside the E. coli cell in high yields.”
The firm will combine the platform with its own EnPresso cultivation medium which he says greatly enhances the performance of CyDisCo system by providing slow growth to high cell densities through a patented enzymatic glucose release system.
Microbial vs Mammalian
Vasala told us that over 100 pharmaceutical proteins currently made using mammalian cell lines could benefit by changing to a microbial-based production platform.
“When compared to mammalian cell cultures, an efficient E. coli based system provides: faster development, higher yields, higher quality, lower batch-to-batch variation, better scaleability, and lower production costs.”
However, regulatory issues and facility set-up means drugmakers are reluctant to change their processes, despite – he continued - growing concerns over the quality of antibody based drugs.
“Due to variable growth conditions and large batch to batch variations, the biological activity of the pharmaceutical proteins may not meet the quality criteria – for example due to changed glycosylation pattern caused by variable cultivation conditions.
“E. coli systems are much better controlled and better scaleable, and in many cases protein glycosylation is not required.”