IN-PART staff picks: Top oncology innovations
Head of Industry Partnering
Katie completed a PhD in Bioprocess Engineering at the University of Sheffield in 2016. In her PhD, Katie investigated novel methods to increase the production titres of high-value biological therapeutics. After spending a few years doing industry-linked post-doctoral research, Katie joined IN-PART in 2019 and now leads our Discover team.
Her interest in biopharmaceutical production, immunotherapy and associated technologies has remained over the years, and Katie always keeps an eye out for related oncology innovations being published on IN-PART’s matchmaking platform, Connect. In this article, we showcase her top oncology innovations from the last few years.
Katie’s top oncology innovations…
Boosting the production of monoclonal antibodies
Proteins for therapeutics, research and diagnostics are part of a rapidly growing market worth more than $100 billion worldwide. Of the 140 currently marketed recombinant proteins, approximately half are being produced in mammalian cells. This can be a costly process in upstream manufacturing. And so, there is a clear industrial need for a technology to enhance protein production in mammalian cells.
This is where researchers at the University Health Network (UHN), a public research and hospital network in Toronto, come in. A team at UHN have developed a method to boost protein expression and production of monoclonal antibodies by as much as three-fold. They achieved this through the overexpression of ABC50 – a protein involved in the initiation of protein translation. This oncology innovation can facilitate the generation of cell lines with improved protein production and survival properties for industrial biopharmaceutical production, in addition to being used in other sectors, including reagent manufacturing for in vitro research and diagnostics.
Read the full non-confidential summary article to learn more about this protein expression technology, part of our top oncology innovations.
Scaling up the production of therapeutic proteins
Both glycosylation and sialylation are instrumental processes involved in oncogenesis and immune responses. This is because they can affect the half-life, immunogenicity, and efficacy of therapeutic proteins, including erythropoietin and recombinant antibodies.
Current glycoengineering approaches employ Chinese Hamster Ovary (CHO) cells to mimic human-like glycosylation and sialylation. This requires expensive culture for comparatively low product yield. To tackle this problem, a team of researchers at the University of British Columbia have engineered a novel strain of E. coli capable of highly efficient human-like glycosylation and sialylation of recombinant proteins. This new platform allows for a broad range of therapeutic proteins, amongst other simple peptides, to benefit from improved serum stability, enhanced activity, or reduced immune response.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Optimising the production of biologics and RNA therapies for cancer
Proteins expressed by individual cell lines, such as yeast or CHO cells, are used to develop biologics to treat cancer. To optimise the process of expression, and to reduce the cost of producing biologics and RNA therapies, the rate of protein synthesis within the cell lines must be predictable and tunable.
With this in mind, researchers at Case Western Reserve University have developed a mechanism at the level of mRNA stability. This mechanism can be exploited to increase the production of proteins. The researchers are able to predict the influence of codons on ribosome speed and use nucleotide combinations to determine the amino acids and sequence of a protein to be translated. This ensures that selected proteins can be synthesized faster.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Upgrading protein therapeutics
Glycosylation reactions can be used to create protein-based drugs for cancer treatments. Presently, naturally-occurring glycosylation patterns are most commonly exploited by industry. However, this natural mechanism limits the development of novel protein therapeutics.
A new system invented by researchers at Johns Hopkins University introduces N-linked glycosylation sites to protein drug candidates. Thereby creating bespoke glycosylation patterns in genetically modified cell lines. Using an innovative methodology to precisely engineer the glycosylation profiles of protein drugs allows for the production of therapeutics with improved therapeutic properties, manufacturability, and efficacy.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Declumping bioreactors for more higher-throughput therapeutic production
Suspension cultures are the most common way to manufacture biological agents such as recombinant proteins and viral agents. However, they are prone to aggregation and clumping, which decreases cell viability and efficiency. While commercial anti-clumping agents are available to add to suspension cultures, they are not operable at high cell densities and under certain environmental conditions.
To address this problem, researchers at Cornell University have developed new recombinant genes. These genes express mucins, a class of glycosylated membrane proteins with strong anti-adhesive properties. These mucin coatings allow existing bioreactor systems to reach higher cell densities that are not currently achievable. Additionally, they are less expensive.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Novel nutrient-deprivation system for cell line selection
There are many disadvantages to using a cytotoxic drug as a selective agent in selection systems for CHO cell lines transfected with an exogenous gene, including the possibility of random mutagenesis and in-process toxicity.
To overcome these challenges, researchers at Dublin City University have developed an alternative nutrient deprivation selection system based on a putrescine starvation model. Mammalian cell clones that express biopharmaceutically relevant or other recombinant proteins are generated, eliminating the addition of toxic chemicals.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Method to increase the shelf-life of cancer therapeutics
Biological therapeutics are used to treat a range of medical conditions, including many cancers. Yet, there are still limitations on how these therapeutics with active ingredients can be stored. Typically, polypeptides are stored in a lyophilized state to maintain their stability. However, there is still the possibility they may denature or form soluble and insoluble aggregates.
Scientists at The University of North Carolina at Charlotte have developed a simple and inexpensive method to prepare and store therapeutic polypeptides. Consequently extending the shelf life of these products while maintaining biological activity. The proteins produced are more stable, without an increase in cytotoxicity and reducing pH. Therefore, making the therapeutic more available to patients.
Read the full non-confidential summary article to learn more about this novel storage method to store therapeutic proteins, part of our top oncology innovations.
Enhanced genome stability in CHO Cell Lines
The CHO cell line is the most frequently used in the commercial production of biopharmaceuticals for cancer. However, due to their low expression, there is constant subculturing to produce higher expression levels. This leaves the cell lines more susceptible to genome instability.
Researchers at the University of Delaware have developed a novel tool to increase the genome stability of CHO cells. Subsequently increasing the reliability of the manufacturing process. By producing more stable cell lines, the manufacturing systems are more reliable. Subsequently reducing production loss and the associated costs and making therapeutics cheaper to produce.
Read the full non-confidential summary article to learn more about this novel engineering of therapeutic proteins, part of our top oncology innovations.
Written by Frances Wilkinson and Ella Cliff. Edited by Alex Stockham, Katie Syddall.
Copyrights reserved unless otherwise agreed – IN-PART Publishing Ltd., 2022: ‘Staff picks: Top oncology innovations’
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