Today a team of scientists at GlycoFi, Inc. and Dartmouth College report the successful reengineering of the glycosylation pathway in the yeast Pichia pastoris. Published in the latest issue of Science, these results constitute the first fungal organism able to secrete a human glycoprotein with complex human glycosylation.
"The vast majority of therapeutic proteins are glycosylated and most require complex, human-like glycosylation to ensure therapeutic efficacy," said GlycoFi's Stephen Hamilton, Ph.D., lead author of the publication. "Mammalian cell lines can replicate human-like glycoprotein processing to a large extent, and so have traditionally been used to produce most protein therapeutics. However, mammalian cell culture systems have significant drawbacks including low protein yields, long fermentation times, production of a mixture of protein glycoforms, and ongoing viral contamination issues."
"Being able to produce human glycoproteins with homogenous N-glycan structures in a fungal host allows us to take advantage of the inherent commercial advantages of yeast and other fungal production systems," says Dr. Tillman Gerngross, GlycoFi chief scientific officer and associate professor of biochemical engineering at Dartmouth College. "Moreover, the ability to produce a homogeneous glycoprotein in yeast offers the biopharmaceutical industry a new tool for further understanding the structure-function relationships of glycoproteins and for potentially crea
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28-Aug-2003