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Customized protein glycosylation to improve biopharmaceutical function and targeting

Linde Van Landuyt (UGent) , Chiara Lonigro (UGent) , Leander Meuris (UGent) and Nico Callewaert (UGent)
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Abstract
For a long time, glycoprotein production has been limited by the inherent properties of production hosts. Glycosylation of biopharmaceuticals has been regarded as a necessary evil, often needed for protein folding or function, but also a source of heterogeneity, complicating downstream processing and product characterization. This has strongly determined the choice of production hosts. Over the last few decades, numerous glycoengineering efforts have helped solving this problem. Moreover, insights from fundamental studies have made it possible to improve therapeutic protein functionality through careful glycoengineering. Here, we will focus on how production host and in vitro glycoengineering approaches allow to design biopharmaceuticals with glycans that impart improved functionality. An important branch of research explores how glycosylation can be tuned to improve pharmacokinetics and reduce glycan heterogeneity of therapeutics. Furthermore, antibody glycoengineering to obtain homogeneous, defined glycan structures has been a major focus. An example of this is the production of Fc glycans without core fucose, exhibiting tremendously improved Antibody-Dependent Cell Cytotoxicity (ADCC). In the last part, glycoforrns that allow for improved (subcellular) targeting and cellular uptake, a field that opens possibilities for enzyme replacement therapies and vaccine development, will be highlighted.
Keywords
HAMSTER OVARY CELLS, C VIRUS-VACCINE, N-GLYCAN, CHO-CELLS, ANTIINFLAMMATORY ACTIVITY, CHEMOENZYMATIC SYNTHESIS, NEUTRALIZING ANTIBODIES, FC-GALACTOSYLATION, CHEMICAL-SYNTHESIS, LYSOSOMAL-ENZYMES

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MLA
Van Landuyt, Linde, et al. “Customized Protein Glycosylation to Improve Biopharmaceutical Function and Targeting.” CURRENT OPINION IN BIOTECHNOLOGY, edited by Yvonne Chen and James A Van Deventer, vol. 60, 2019, pp. 17–28.
APA
Van Landuyt, L., Lonigro, C., Meuris, L., & Callewaert, N. (2019). Customized protein glycosylation to improve biopharmaceutical function and targeting. CURRENT OPINION IN BIOTECHNOLOGY, 60, 17–28.
Chicago author-date
Van Landuyt, Linde, Chiara Lonigro, Leander Meuris, and Nico Callewaert. 2019. “Customized Protein Glycosylation to Improve Biopharmaceutical Function and Targeting.” Edited by Yvonne Chen and James A Van Deventer. CURRENT OPINION IN BIOTECHNOLOGY 60: 17–28.
Chicago author-date (all authors)
Van Landuyt, Linde, Chiara Lonigro, Leander Meuris, and Nico Callewaert. 2019. “Customized Protein Glycosylation to Improve Biopharmaceutical Function and Targeting.” Ed by. Yvonne Chen and James A Van Deventer. CURRENT OPINION IN BIOTECHNOLOGY 60: 17–28.
Vancouver
1.
Van Landuyt L, Lonigro C, Meuris L, Callewaert N. Customized protein glycosylation to improve biopharmaceutical function and targeting. Chen Y, Van Deventer JA, editors. CURRENT OPINION IN BIOTECHNOLOGY. 2019;60:17–28.
IEEE
[1]
L. Van Landuyt, C. Lonigro, L. Meuris, and N. Callewaert, “Customized protein glycosylation to improve biopharmaceutical function and targeting,” CURRENT OPINION IN BIOTECHNOLOGY, vol. 60, pp. 17–28, 2019.
@article{8599921,
  abstract     = {For a long time, glycoprotein production has been limited by the inherent properties of production hosts. Glycosylation of biopharmaceuticals has been regarded as a necessary evil, often needed for protein folding or function, but also a source of heterogeneity, complicating downstream processing and product characterization. This has strongly determined the choice of production hosts. Over the last few decades, numerous glycoengineering efforts have helped solving this problem. Moreover, insights from fundamental studies have made it possible to improve therapeutic protein functionality through careful glycoengineering. Here, we will focus on how production host and in vitro glycoengineering approaches allow to design biopharmaceuticals with glycans that impart improved functionality. An important branch of research explores how glycosylation can be tuned to improve pharmacokinetics and reduce glycan heterogeneity of therapeutics. Furthermore, antibody glycoengineering to obtain homogeneous, defined glycan structures has been a major focus. An example of this is the production of Fc glycans without core fucose, exhibiting tremendously improved Antibody-Dependent Cell Cytotoxicity (ADCC). In the last part, glycoforrns that allow for improved (subcellular) targeting and cellular uptake, a field that opens possibilities for enzyme replacement therapies and vaccine development, will be highlighted.},
  author       = {Van Landuyt, Linde and Lonigro, Chiara and Meuris, Leander and Callewaert, Nico},
  editor       = {Chen, Yvonne and Van Deventer, James A},
  issn         = {0958-1669},
  journal      = {CURRENT OPINION IN BIOTECHNOLOGY},
  keywords     = {HAMSTER OVARY CELLS,C VIRUS-VACCINE,N-GLYCAN,CHO-CELLS,ANTIINFLAMMATORY ACTIVITY,CHEMOENZYMATIC SYNTHESIS,NEUTRALIZING ANTIBODIES,FC-GALACTOSYLATION,CHEMICAL-SYNTHESIS,LYSOSOMAL-ENZYMES},
  language     = {eng},
  pages        = {17--28},
  title        = {Customized protein glycosylation to improve biopharmaceutical function and targeting},
  url          = {http://dx.doi.org/10.1016/j.copbio.2018.11.017},
  volume       = {60},
  year         = {2019},
}

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