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Updated: Apr 18, 2026

Protein Engineering by Yeast Surface Display
Published on: November 29, 2024
Engineering yeast for producing human glycoproteins: where are we now?
Bram Laukens1, Charlotte De Visscher, Nico Callewaert
1Unit for Medical Biotechnology, Inflammation Research Centre (IRC), VIB-UGent, Technologiepark 927, B-9052 Ghent-Zwijnaarde, Belgium.
None:
Yeast has advanced as an alternative for mammalian cell culture for the production of recombinant therapeutic glycoproteins. Engineered yeast strains not only allow to mimic the human N-glycosylation pathway but also specific types of human O-glycosylation. This is of great value for therapeutic protein production and indispensable to determine the structure-function relationships of glycans on recombinant proteins. However, as the technology matures, some limitations have come up that may hamper biomedical applications and must be considered to exploit the full potential of the unprecedented glycan homogeneity obtained on relevant biopharmaceuticals. In this special report, we focus on the recent developments in N- and O-glycosylation engineering in yeasts of industrial importance, to produce recombinant therapeutics with customized glycans.
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