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Glycobiology Advance Access originally published online on June 3, 2009
Glycobiology 2009 19(9):936-949; doi:10.1093/glycob/cwp079
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Review

Optimal and consistent protein glycosylation in mammalian cell culture

Patrick Hossler3,4,2, Sarwat F Khattak3,4 and Zheng Jian Li1,4

4 Process Sciences Upstream, Technical Operations, Bristol-Myers Squibb Company, East Syracuse, NY 13057, USA

1 To whom correspondence should be addressed: Tel: +1-315-432-2131; e-mail: zhengjian.li{at}bms.com

Received on April 6, 2009; revised on June 1, 2009; accepted on June 1, 2009

In the biopharmaceutical industry, mammalian cell culture systems, especially Chinese hamster ovary (CHO) cells, are predominantly used for the production of therapeutic glycoproteins. Glycosylation is a critical protein quality attribute that can modulate the efficacy of a commercial therapeutic glycoprotein. Obtaining a consistent glycoform profile in production is desired due to regulatory concerns because a molecule can be defined by its carbohydrate structures. An optimal profile may involve a spectrum of product glycans that confers a desired therapeutic efficacy, or a homogeneous glycoform profile that can be systemically screened for. Studies have shown some degree of protein glycosylation control in mammalian cell culture, through cellular, media, and process effects. Studies upon our own bioprocesses to produce fusion proteins and monoclonal antibodies have shown an intricate relationship between these variables and the resulting protein quality. Glycosylation optimization will improve therapeutic efficacy and is an ongoing goal for researchers in academia and industry alike. This review will focus on the advancements made in glycosylation control in a manufacturing process, as well as the next steps in understanding and controlling protein glycosylation.

Key words: bioprocessing / mammalian cell culture / protein glycosylation / protein therapeutics / protein quality

2 Present address: Abbott Bioresearch Center, Abbot Laboratories, Worcester, MA 01605, USA.

3 These authors contributed equally to this work.


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