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DOI: 10.1126/science.1130256
OpenAccess: Closed
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Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins

Stephen R. Hamilton,Robert C. Davidson,Natarajan Sethuraman,Juergen H. Nett,Yi Jiang,Sandra Rios,Piotr Bobrowicz,Terrance A. Stadheim,Huijuan Li,Byungcho Choi,Daniel Hopkins,Harry Wischnewski,Jessica Roser,Teresa Mitchell,Rendall R. Strawbridge,Jack Hoopes,Stefan Wildt,Tillman U. Gerngross

Yeast
Glycoprotein
Pichia pastoris
2006
Yeast is a widely used recombinant protein expression system. We expanded its utility by engineering the yeast Pichia pastoris to secrete human glycoproteins with fully complex terminally sialylated N-glycans. After the knockout of four genes to eliminate yeast-specific glycosylation, we introduced 14 heterologous genes, allowing us to replicate the sequential steps of human glycosylation. The reported cell lines produce complex glycoproteins with greater than 90% terminal sialylation. Finally, to demonstrate the utility of these yeast strains, functional recombinant erythropoietin was produced.
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    Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins” is a paper by Stephen R. Hamilton Robert C. Davidson Natarajan Sethuraman Juergen H. Nett Yi Jiang Sandra Rios Piotr Bobrowicz Terrance A. Stadheim Huijuan Li Byungcho Choi Daniel Hopkins Harry Wischnewski Jessica Roser Teresa Mitchell Rendall R. Strawbridge Jack Hoopes Stefan Wildt Tillman U. Gerngross published in 2006. It has an Open Access status of “closed”. You can read and download a PDF Full Text of this paper here.