Highly sialylated recombinant human erythropoietin production in large-scale perfusion bioreactor utilizing CHO-gmt4 (JW152) with restored GnT I function (pages 100–109)
John S. Y. Goh, Yingwei Liu, Haifeng Liu, Kah Fai Chan, Corrine Wan, Gavin Teo, Xiangshan Zhou, Fusheng Xie, Peiqing Zhang, Dr. Yuanxing Zhang and Dr. Zhiwei Song
Article first published online: 10 DEC 2013 | DOI: 10.1002/biot.201300301
Mammalian cells produce recombinant therapeutic glycoproteins with heterogeneous glycosylation. However, it is desirable for glycoproteins to be better sialylated for improved circulatory half-life and efficacy. CHO-gmt4 cells lacking N-acetylglucosaminyltransferase I (GnT I) have been shown to produce highly sialylated erythropoietin (EPO) when GnT I is functionally restored. We have generated an EPO-producing CHO cell line derived from CHO-gmt4. Analyses of the resulting EPO produced in an existing bioprocess demonstrate that the CHO-gmt4D cell line has the industrial potential for producing highly sialylated recombinant EPO and other recombinant glycoprotein therapeutics.