Nature Biotechnology22, 1409 - 1414 (2004)
Published online: 4 November 2004; | doi:10.1038/nbt1028
There is a Corrigenda (December 2004) associated with this Review.
Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
Tillman U Gerngross
Thayer School of Engineering, the Department of Biological Sciences and the Department of Chemistry, Dartmouth College, Hanover, New Hampshire 03755, USA and GlycoFi Inc., 21 Lafayette Street, Lebanon, New Hampshire 03766, USA.
Yeast and fungal protein expression systems are used for the production of many industrially relevant enzymes, and are widely used by the research community to produce proteins that cannot be actively expressed in Escherichia coli or require glycosylation for proper folding and biological activity. However, for the production of therapeutic glycoproteins intended for use in humans, yeasts have been less useful because of their inability to modify proteins with human glycosylation structures. Yeast glycosylation is of the high-mannose type, which confers a short in vivo half-life to the protein and may render it less efficacious or even immunogenic. Several ways of humanizing yeast-derived glycoproteins have been tried, including enzymatically modifying proteins in vitro and modulating host glycosylation pathways in vivo. Recent advances in the glycoengineering of yeasts and the expression of therapeutic glycoproteins in humanized yeasts have shown significant promise, and are challenging the current dominance of therapeutic protein production based on mammalian cell culture.
MORE ARTICLES LIKE THIS
These links to content published by NPG are automatically generated.
