Glycoengineering in CHO Cells: Advances in Systems Biology

Glycoengineering in CHO Cells: Advances in Systems Biology IntroductionChinese hamster ovary (CHO) cells are the most widely used host for manufacturing complex biopharmaceuticals due to their ability to replicate folding and post‐translational modifications, including glycosylation patterns, found in human proteins. CHO cells also grow robustly in suspension in serum‐free media and have a long history of regulatory approval and an established track record for producing safe, efficacious products. In 1987, the US Food and Drug Administration (FDA) approved the first CHO‐derived recombinant protein, tissue plasminogen activator (t‐PA) for use as a therapeutic. Since this approval, CHO cells have been the clearly preferred choice for commercial production of glycoprotein biologics, ranging from antibodies to hormones to cytokines. In 2016, 5 of the top 10 biopharmaceuticals were produced in CHO cells while 10 out of the 15 biopharmaceuticals approved by the FDA in 2016 were produced in CHO cells, including 3 biosimilars.Correct glycan structures are crucial for potency and control of pharmacokinetic and pharmacodynamic properties of glycoprotein biologics and therapeutic carbohydrates. Protein glycosylation and synthesis of the glycosaminoglycan (GAG) portion of proteoglycans are non‐templated, and thus, significant heterogeneity can arise from organism to organism, cell type to cell type, and even between different culture conditions. While CHO cells produce http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biotechnology Journal Wiley

Glycoengineering in CHO Cells: Advances in Systems Biology

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Publisher
Wiley Subscription Services, Inc., A Wiley Company
Copyright
© 2018 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim
ISSN
1860-6768
eISSN
1860-7314
D.O.I.
10.1002/biot.201700234
Publisher site
See Article on Publisher Site

Abstract

IntroductionChinese hamster ovary (CHO) cells are the most widely used host for manufacturing complex biopharmaceuticals due to their ability to replicate folding and post‐translational modifications, including glycosylation patterns, found in human proteins. CHO cells also grow robustly in suspension in serum‐free media and have a long history of regulatory approval and an established track record for producing safe, efficacious products. In 1987, the US Food and Drug Administration (FDA) approved the first CHO‐derived recombinant protein, tissue plasminogen activator (t‐PA) for use as a therapeutic. Since this approval, CHO cells have been the clearly preferred choice for commercial production of glycoprotein biologics, ranging from antibodies to hormones to cytokines. In 2016, 5 of the top 10 biopharmaceuticals were produced in CHO cells while 10 out of the 15 biopharmaceuticals approved by the FDA in 2016 were produced in CHO cells, including 3 biosimilars.Correct glycan structures are crucial for potency and control of pharmacokinetic and pharmacodynamic properties of glycoprotein biologics and therapeutic carbohydrates. Protein glycosylation and synthesis of the glycosaminoglycan (GAG) portion of proteoglycans are non‐templated, and thus, significant heterogeneity can arise from organism to organism, cell type to cell type, and even between different culture conditions. While CHO cells produce

Journal

Biotechnology JournalWiley

Published: Jan 1, 2018

Keywords: ; ; ; ;

References

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