| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6492139 | Journal of Biotechnology | 2012 | 9 Pages |
Abstract
⺠We report the expression of recombinant human erythropoietin (rhEPO) in glycoengineered P. pastoris. ⺠We show that glycosylation fidelity is maintained in fermentation volumes spanning six orders of magnitude and that the protein can be purified to high homogeneity. ⺠In order to increase the half-life of rhEPO, the purified protein was coupled to polyethylene glycol (PEG) and then compared to the currently marketed erythropoiesis stimulating agent, Aranesp® (darbepoetin). ⺠Pharmacodynamics as well as pharmacokinetic activity of PEGylated rhEPO in animals was comparable to that of Aranesp®. ⺠Taken together, our results show that glycoengineered P. pastoris is a suitable production host for rhEPO, yielding an active biologic that is comparable to those produced in current mammalian host systems.
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Physical Sciences and Engineering
Chemical Engineering
Bioengineering
Authors
Juergen H. Nett, Sujatha Gomathinayagam, Stephen R. Hamilton, Bing Gong, Robert C. Davidson, Min Du, Daniel Hopkins, Teresa Mitchell, Muralidhar R. Mallem, Adam Nylen, Seemab S. Shaikh, Nathan Sharkey, Gavin C. Barnard, Victoria Copeland, Liming Liu,