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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Bibliographic Details
Published inApplied microbiology and biotechnology Vol. 87; no. 5; pp. 1617 - 1631
Main Authors De Pourcq, Karen, De Schutter, Kristof, Callewaert, Nico
Format Journal Article
LanguageEnglish
Published Berlin/Heidelberg Berlin/Heidelberg : Springer-Verlag 01.08.2010
Springer-Verlag
Springer
Springer Nature B.V
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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.
Bibliography:http://dx.doi.org/10.1007/s00253-010-2721-1
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ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-010-2721-1