Journal
SCIENCE
Volume 301, Issue 5637, Pages 1244-1246Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1088166
Keywords
-
Categories
Funding
- NIGMS NIH HHS [1R43GM66690-1] Funding Source: Medline
Ask authors/readers for more resources
We report the humanization of the glycosylation pathway in the yeast Pichia pastoris to secrete a human glycoprotein with uniform complex N-glycosylation. The process involved eliminating endogenous yeast glycosylation pathways, while properly localizing five active eukaryotic proteins, including mannosidases I and II, N-acetylglucosaminyl transferases I and II, and uridine 5'-diphosphate (UDP)-N-acetylglucosamine transporter. Targeted localization of the enzymes enabled the generation of a synthetic in vivo glycosylation pathway, which produced the complex human N-glycan N-acetylglucosamine(2)-mannose(3)-N-acetylglucosamine(2) (GlcNAc(2)Man(3)GlcNAc(2)). The ability to generate human glycoproteins with homogeneous N-glycan structures in a fungal host is a step toward producing therapeutic glycoproteins and could become a tool for elucidating the structure-function relation of glycoproteins.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available