| Literature DB >> 16960007 |
Stephen R Hamilton1, Robert C Davidson, Natarajan Sethuraman, Juergen H Nett, Youwei Jiang, Sandra Rios, Piotr Bobrowicz, Terrance A Stadheim, Huijuan Li, Byung-Kwon Choi, Daniel Hopkins, Harry Wischnewski, Jessica Roser, Teresa Mitchell, Rendall R Strawbridge, Jack Hoopes, Stefan Wildt, Tillman U Gerngross.
Abstract
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.Entities:
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Year: 2006 PMID： 16960007 DOI： 10.1126/science.1130256
Source DB: PubMed Journal: Science ISSN： 0036-8075 Impact factor: 47.728