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Humanization of yeast to produce complex terminally sialylated glycoproteins |
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| Authors: | Hamilton Stephen R Davidson Robert C Sethuraman Natarajan Nett Juergen H Jiang Youwei Rios Sandra Bobrowicz Piotr Stadheim Terrance A Li Huijuan Choi Byung-Kwon Hopkins Daniel Wischnewski Harry Roser Jessica Mitchell Teresa Strawbridge Rendall R Hoopes Jack Wildt Stefan Gerngross Tillman U |
| Institution: | GlycoFi Inc., 21 Lafayette Street, Suite 200, Lebanon, NH 03766, USA. |
| 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. |
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