The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Optimal and consistent protein glycosylation in mammalian cell culture
Abstract
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.
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Cites
Intracellular Functions of N-Linked Glycans
Helenius, A., & Aebi, A. M. (2001) · Science · doi:10.1126/science.291.5512.2364 · Cited by 2,405
Production of recombinant protein therapeutics in cultivated mammalian cells
Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032
Shields, R. L., Lai, J., Keck, R., O'Connell, L. Y., Hong, K., Meng, Y. G., Weikert, S. H. A., & Presta, L. G. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202069200 · Cited by 1,835
Umaña, P., Jean–Mairet, J., Moudry, R., Amstutz, H., & Bailey, J. E. (1999) · Nature Biotechnology · doi:10.1038/6179 · Cited by 764
Davies, J., Jiang, L., Pan, L., LaBarre, M. J., Anderson, D., & Reff, M. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1119 · Cited by 327
Metabolic control of recombinant protein N‐glycan processing in NS0 and CHO cells
Baker, K. N., Rendall, M. H., Hills, A. E., Hoare, M., Freedman, R. B., & James, D. C. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1051 · Cited by 184
Borys, M. C., Linzer, D. I. H., & Papoutsakis, E. T. (1993) · Nature Biotechnology · doi:10.1038/nbt0693-720 · Cited by 171
A mathematical model of N-linked glycosylation
Krambeck, F. J., & Betenbaugh, M. J. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20645 · Cited by 171
High-level expression of recombinant IgG in the human cell line per.c6
Jones, D., Kroos, N., Anema, R., Van Montfort, B., Vooys, A., Kraats, S. V. D., Helm, E. V. D., Smits, S., Schouten, J., Brouwer, K., et al. (2003) · Biotechnology Progress · doi:10.1021/bp025574h · Cited by 158
Thorens, B., & Vassalli, P. (1986) · Nature · doi:10.1038/321618a0 · Cited by 147
Cited by
The genomic sequence of the Chinese hamster ovary (CHO)-K1 cell line
Xu, X., Nagarajan, H., Lewis, N. E., Pan, S., Cai, Z., Liu, X., Chen, W., Xie, M., Wang, W., Hammond, S., et al. (2011) · Nature Biotechnology · doi:10.1038/nbt.1932 · Cited by 785
Recent advances in large-scale production of monoclonal antibodies and related proteins
Shukla, A. A., & Thömmes, J. (2010) · Trends in Biotechnology · doi:10.1016/j.tibtech.2010.02.001 · Cited by 578
Expression systems for therapeutic glycoprotein production
Durocher, Y., & Butler, M. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.10.008 · Cited by 386
Trends in Upstream and Downstream Process Development for Antibody Manufacturing
Gronemeyer, P., Ditz, R., & Strube, J. (2014) · Bioengineering · doi:10.3390/bioengineering1040188 · Cited by 329
Therapeutic glycoprotein production in mammalian cells
Lalonde, M.-E., & Durocher, Y. (2017) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2017.04.028 · Cited by 296
Metadata
- Authors
- Hossler, P., Khattak, S. F., & Li, Z. J.
- Venue
- Glycobiology
- Publisher
- Oxford University Press (OUP)
- Published
- 2009-06-03
- Volume
- 19
- Issue
- 9
- Pages
- 936-949
- ISSN
- 0959-6658 (ISSN-L)
- 1460-2423
- OpenAlex
- W2146981871
- Cited by
- 669
- References
- 10
- FWCI
- 12.72
- Type
- journal article
- Language
- en
- Open access
- closed
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- Hossler, P., Khattak, S. F., & Li, Z. J. (2009). Optimal and consistent protein glycosylation in mammalian cell culture. Glycobiology. https://doi.org/10.1093/glycob/cwp079
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