Engineering of glycosylation in yeast and other fungi: current state and perspectives.
With the increasing demand for recombinant proteins and glycoproteins, research on hosts for producing these proteins is focusing increasingly on more cost-effective expression systems. Yeasts and other fungi are promising alternatives because they provide easy and cheap systems that can perform eukaryotic post-translational modifications. Unfortunately, yeasts and other fungi modify their glycoproteins with heterogeneous high-mannose glycan structures, which is often detrimental to a therapeutic protein's pharmacokinetic behavior and can reduce the efficiency of downstream processing. This problem can be solved by engineering the glycosylation pathways to produce homogeneous and, if so desired, human-like glycan structures. In this review, we provide an overview of the most significant recently reported approaches for engineering the glycosylation pathways in yeasts and fungi.
De Pourcq
Karen
K
Unit for Molecular Glycobiology, Department for Molecular Biomedical Research, VIB-Ghent University, Technologiepark 927, 9052, Ghent-Zwijnaarde, Belgium.
De Schutter
Kristof
K
Callewaert
Nico
N
D005656:Fungal Proteins / Q000235:genetics* / Q000378:metabolism*; D005658:Fungi / Q000201:enzymology / Q000235:genetics* / Q000378:metabolism*; D006031:Glycosylation; D053858:Metabolic Networks and Pathways / Q000235:genetics*; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism
D005656:Fungal Proteins; D011994:Recombinant Proteins