Chapter title |
Glycosylation Analysis of Therapeutic Glycoproteins Produced in CHO Cells
|
---|---|
Chapter number | 15 |
Book title |
Heterologous Protein Production in CHO Cells
|
Published in |
Methods in molecular biology, May 2017
|
DOI | 10.1007/978-1-4939-6972-2_15 |
Pubmed ID | |
Book ISBNs |
978-1-4939-6971-5, 978-1-4939-6972-2
|
Authors |
Carillo, Sara, Mittermayr, Stefan, Farrell, Amy, Albrecht, Simone, Bones, Jonathan, Sara Carillo, Stefan Mittermayr, Amy Farrell, Simone Albrecht, Jonathan Bones |
Editors |
Paula Meleady |
Abstract |
In the last decades, the number of approved therapeutic proteins drugs is increasing exponentially and a large number of new therapeutic entities are progressing through clinical trials, solidifying biologics as the most promising class of pharmaceuticals on the market. Several cell lines are available for biopharmaceutical processes but mammalian cells are preferred since they give fewer problems for immunogenicity as they produce human-like post-translational modifications (PTMs). Glycosylation is the most common and complex (for both bioprocess engineering and quality control) of these modifications. Obtaining the desired glycosylation pattern is crucial for therapeutic proteins as it can impact significantly stability, half-life and safety as well as driving molecular processes, modifying the way drug interacts with patients' cells. As a consequence, glycosylation (like other PTMs) needs to be regulated and accurately analyzed during biopharmaceutical production. Herein we describe and discuss the analytical approaches for glycosylation analysis of therapeutic glycoproteins produced in CHO (Chinese Hamster Ovary) cells. This chapter will describe glycoprotein purification after separation from producing cell lines, N-glycan release and their variants fine structural characterization through mass spectrometry techniques. |
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