Improved Product Quality of Biosimilars in the Cellca CHO Expression Platform
15th December 2017
By: Cornelia Lindner - Team Leader, Dr Christoph Zehe - Lead Scientist, Johannes Wirth - Scientist, Marina Putanko - Scientist,
Due to the high number of patent expirations for first generation biopharmaceuticals, the production of biosimilars is a fast growing market. Biosimilars require finger-print like similarity to their originator drug with respect to product quality. One important aspect of product quality is a comparable glycosylation pattern, as glycosylation influences serum clearance, immunogenicity, as well as activity.
The α-2,6 sialyltransferase is essential for terminal sialylation. However, CHO DG44 cells lack the α-2,6 sialyltransferase, therefore, in many cases sialylation is one of the glycosylation parameters which differs most from the originator when biosimilars are expressed in CHO DG44. Although the standard Cellca CHO DG44 host shows a rather weak sialylation, the top 12 clones of our glycoengineering approach showed a sialylation pattern highly similar to the originator drug (Figure 1).
Want to know how we achieved an increased sialylation? Click here to download our scientific poster.