Journal
APPLIED MICROBIOLOGY AND BIOTECHNOLOGY
Volume 87, Issue 5, Pages 1617-1631Publisher
SPRINGER
DOI: 10.1007/s00253-010-2721-1
Keywords
N-glycosylation engineering; O-glycosylation engineering; Yeast; Fungi; Biopharmaceuticals; Recombinant proteins
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Funding
- Marie Curie Excellence Grant [MEXT-014292]
- Fund for Scientific Research-Flanders (FWO)
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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.
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