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Engineering of yeast glycoprotein expression

Charlot De Wachter (UGent) , Linde Van Landuyt (UGent) and Nico Callewaert (UGent)
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Abstract
Yeasts are valuable hosts for recombinant protein production, as these unicellular eukaryotes are easy to handle, grow rapidly to a high cell density on costeffective defined media, often offer a high space-time yield, and are able to perform posttranslational modifications. However, a key difference between yeasts and mammalian cells involves the type of glycosylation structures, which hampers the use of yeasts for the production of many biopharmaceuticals. Glycosylation is not only important for the folding process of most recombinant proteins; it has a large impact on pharmacokinetics and pharmacodynamics of the therapeutic proteins as well. Yeasts' hypermannosylated glycosyl structures in some cases can evoke immune responses and lead to rapid clearance of the therapeutic protein from the blood. This chapter highlights the efforts made so far regarding the glycoengineering of N- and O-type glycosylation, removing or reducing yeast-specific glycans. In some cases, this is combined with the introduction of humanized glycosylation pathways. After many years of patient development to overcome remaining challenges, these efforts have now culminated in effective solutions that should allow yeasts to reclaim the primary position in biopharmaceutical manufacturing that they enjoyed in the early days of biotechnology.
Keywords
Fungi, N-glycosylation engineering, O-glycosylation engineering, Pichia pastoris, Recombinant protein expression, Saccharomyces cerevisiae, Yeast, PROTEIN-O-GLYCOSYLATION, LIPID-LINKED OLIGOSACCHARIDES, HUMAN SERUM-ALBUMIN, HOST-CELL LINE, DOL-P-MAN, PICHIA-PASTORIS, SACCHAROMYCES-CEREVISIAE, CANDIDA-ALBICANS, N-GLYCOSYLATION, ALG3 GENE

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MLA
De Wachter, Charlot, et al. “Engineering of Yeast Glycoprotein Expression.” ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY, edited by Erdmann Rapp and Udo Reichl, vol. 175, Springer, 2021, pp. 93–135, doi:10.1007/10_2018_69.
APA
De Wachter, C., Van Landuyt, L., & Callewaert, N. (2021). Engineering of yeast glycoprotein expression. ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY, 175, 93–135. https://doi.org/10.1007/10_2018_69
Chicago author-date
De Wachter, Charlot, Linde Van Landuyt, and Nico Callewaert. 2021. “Engineering of Yeast Glycoprotein Expression.” Edited by Erdmann Rapp and Udo Reichl. ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY 175: 93–135. https://doi.org/10.1007/10_2018_69.
Chicago author-date (all authors)
De Wachter, Charlot, Linde Van Landuyt, and Nico Callewaert. 2021. “Engineering of Yeast Glycoprotein Expression.” Ed by. Erdmann Rapp and Udo Reichl. ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY 175: 93–135. doi:10.1007/10_2018_69.
Vancouver
1.
De Wachter C, Van Landuyt L, Callewaert N. Engineering of yeast glycoprotein expression. Rapp E, Reichl U, editors. ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY. 2021;175:93–135.
IEEE
[1]
C. De Wachter, L. Van Landuyt, and N. Callewaert, “Engineering of yeast glycoprotein expression,” ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY, vol. 175, pp. 93–135, 2021.
@article{8599901,
  abstract     = {{Yeasts are valuable hosts for recombinant protein production, as these unicellular eukaryotes are easy to handle, grow rapidly to a high cell density on costeffective defined media, often offer a high space-time yield, and are able to perform posttranslational modifications. However, a key difference between yeasts and mammalian cells involves the type of glycosylation structures, which hampers the use of yeasts for the production of many biopharmaceuticals. Glycosylation is not only important for the folding process of most recombinant proteins; it has a large impact on pharmacokinetics and pharmacodynamics of the therapeutic proteins as well. Yeasts' hypermannosylated glycosyl structures in some cases can evoke immune responses and lead to rapid clearance of the therapeutic protein from the blood. This chapter highlights the efforts made so far regarding the glycoengineering of N- and O-type glycosylation, removing or reducing yeast-specific glycans. In some cases, this is combined with the introduction of humanized glycosylation pathways. After many years of patient development to overcome remaining challenges, these efforts have now culminated in effective solutions that should allow yeasts to reclaim the primary position in biopharmaceutical manufacturing that they enjoyed in the early days of biotechnology.}},
  author       = {{De Wachter, Charlot and Van Landuyt, Linde and Callewaert, Nico}},
  editor       = {{Rapp, Erdmann and Reichl, Udo}},
  isbn         = {{9783030695897}},
  issn         = {{0724-6145}},
  journal      = {{ADVANCES IN BIOCHEMICAL ENGINEERING-BIOTECHNOLOGY}},
  keywords     = {{Fungi,N-glycosylation engineering,O-glycosylation engineering,Pichia pastoris,Recombinant protein expression,Saccharomyces cerevisiae,Yeast,PROTEIN-O-GLYCOSYLATION,LIPID-LINKED OLIGOSACCHARIDES,HUMAN SERUM-ALBUMIN,HOST-CELL LINE,DOL-P-MAN,PICHIA-PASTORIS,SACCHAROMYCES-CEREVISIAE,CANDIDA-ALBICANS,N-GLYCOSYLATION,ALG3 GENE}},
  language     = {{eng}},
  pages        = {{93--135}},
  publisher    = {{Springer}},
  title        = {{Engineering of yeast glycoprotein expression}},
  url          = {{http://dx.doi.org/10.1007/10_2018_69}},
  volume       = {{175}},
  year         = {{2021}},
}

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