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 euk...
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Published in | Applied microbiology and biotechnology Vol. 87; no. 5; pp. 1617 - 1631 |
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Main Authors | , , |
Format | Journal Article |
Language | English |
Published |
Berlin/Heidelberg
Berlin/Heidelberg : Springer-Verlag
01.08.2010
Springer-Verlag Springer Springer Nature B.V |
Subjects | |
Online Access | Get full text |
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Summary: | 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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Bibliography: | http://dx.doi.org/10.1007/s00253-010-2721-1 ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1 ObjectType-Article-1 ObjectType-Feature-2 |
ISSN: | 0175-7598 1432-0614 |
DOI: | 10.1007/s00253-010-2721-1 |