Engineering of glycosylation in yeast and other fungi: current state and perspectives

Appl Microbiol Biotechnol. 2010 Aug;87(5):1617-31. doi: 10.1007/s00253-010-2721-1. Epub 2010 Jun 29.


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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Fungal Proteins / genetics*
  • Fungal Proteins / metabolism*
  • Fungi / enzymology
  • Fungi / genetics*
  • Fungi / metabolism*
  • Glycosylation*
  • Metabolic Networks and Pathways / genetics*
  • Protein Engineering*
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism


  • Fungal Proteins
  • Recombinant Proteins