Abstract
Metabolic engineering of mammalian cells for optimized glycosylation is usually done to improve activity and the pharmacokinetic features of glycoprotein therapeutics. The field is mainly focused around engineering of N-glycans. We have created a platform in which recombinant mucin-type immunoglobulin fusion proteins are used as scaffolds for multivalent expression of O-glycans with diagnostic or therapeutic potential. The methods used to make stable CHO cell lines secreting a mucin-type fusion protein with blood group A or B determinants following expression of up to five different cDNAs are described.
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Acknowledgements
This work was supported by AbSorber AB and in part by grants to J.H. from the Swedish Research Council/Medicine (K2011-65X-3031-01-6) and the County Council of Västra Götaland (ALF).
Conflicts of interest. J.H. is founder, board member, and part-time medical director of AbSorber AB. He is also a shareholder in Allenex AB, the main owner of AbSorber AB.
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Lindberg, L., Liu, J., Holgersson, J. (2013). Engineering of Therapeutic and Diagnostic O-Glycans on Recombinant Mucin-Type Immunoglobulin Fusion Proteins Expressed in CHO Cells. In: Beck, A. (eds) Glycosylation Engineering of Biopharmaceuticals. Methods in Molecular Biology, vol 988. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-327-5_1
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DOI: https://doi.org/10.1007/978-1-62703-327-5_1
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Publisher Name: Humana Press, Totowa, NJ
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