Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins

@article{Hamilton2006HumanizationOY,
  title={Humanization of Yeast to Produce Complex Terminally Sialylated Glycoproteins},
  author={Stephen R. Hamilton and Robert C. Davidson and Natarajan Sethuraman and Juergen H Nett and Youwei Jiang and Sandra E R{\'i}os and Piotr Bobrowicz and Terrance A. Stadheim and Huijuan Li and Byung-Kwon Choi and Daniel Hopkins and Harry Wischnewski and Jessica Roser and Teresa I Mitchell and Rendall R. Strawbridge and Jack Hoopes and Stefan Wildt and Tillman U. Gerngross},
  journal={Science},
  year={2006},
  volume={313},
  pages={1441 - 1443}
}
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… Expand
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