Glycosylation can have a big effect on the yields and on the biologic and clinical properties of proteins and vaccines. Hans Baumeister, director clinical immunomonitoring, and Steffen Goletz, ceo, cso and founder of Glycotope, explain how glyco-engineering can be used to optimise their characteristics.
Back when the first therapeutic proteins were developed, glycosylation was largely ignored and glycoproteins were most likely to be excluded from the list of drug candidates. Today, many examples demonstrate that glycosylation not only affects the bioavailability of biopharmaceuticals but strongly influences the activity, immunogenicity, antigenicity, solubility and stability of proteins too.1, 2 Therefore, the aim within the industry is to improve biopharmaceuticals by optimisation and humanisation of their glycosylation and maintain consistency from batch to batch.
Currently, there are at least four suitable approaches:
- Enzymatic modification of the glycosylation after production
- Control of cell culture and production conditions
- Protein engineering to add or eliminate sites for attachment of glycans
- Cell line engineering for a modified glycosylation profile
This article focuses on the small number of companies with novel glyco-engineered cell lines. For example Glycart, acquired by Roche in 2005, and Kyowa (BioWa in the US), which has been part of the Kirin Holding since 2008, developed genetically modified Chinese Hamster Ovary (CHO) cell lines to produce higher active therapeutic antibodies; and GlycoFi (now MSD), Biolex or Greenovation, engineer plant or yeast systems that combine a very high yield with a cost-effective production system using a glycosylation that is similar to a human glycosylation.
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