Over the past decade, notable advances in the characterization and control of post-translational modifications (PTMs) to enhance therapeutic properties have continued to drive the development of many next-generation biopharmaceuticals. It has been widely reported that the quality of secreted therapeutic proteins is dependent on the consistency of attached glycan moieties. Insufficient glycosylation potentially impairs efficacy and safety. Our particular interest lies in identifying critical raw materials that rescue N-linked glycosylation profiles of therapeutic proteins from selected high-producing clones. This study represents an important step towards establishing cGMP-ready chemically defined supplements that significantly and reproducibly adjust glycan moieties. In addition, the multivariate profiling process described here represents a pivotal tool in the upstream characterization of biopharmaceutical platforms.
Chinese hamster ovary (CHO) cells are used extensively in the biopharmaceutical industry to produce recombinant proteins that require post-translation modification for full biological functionality. Optimization of culture conditions for recombinant CHO cell lines presents challenges in light of the diverse nutritional requirements observed with different clonally derived cell lines.