Chinese hamster ovary (CHO) host cell engineering to increase sialylation of recombinant therapeutic proteins by modulating sialyltransferase expression.

@article{Lin2015ChineseHO,
  title={Chinese hamster ovary (CHO) host cell engineering to increase sialylation of recombinant therapeutic proteins by modulating sialyltransferase expression.},
  author={Nan Lin and Joaquina X Mascarenhas and Natalie R Sealover and Henry J George and Jeanne Kaye Brooks and Kevin J Kayser and Brian C Gau and I. Wayan W. Yasa and Parastoo Azadi and Stephanie Archer-Hartmann},
  journal={Biotechnology progress},
  year={2015},
  volume={31 2},
  pages={334-46}
}
N-Glycans of human proteins possess both α2,6- and α2,3-linked terminal sialic acid (SA). Recombinant glycoproteins produced in Chinese hamster overy (CHO) only have α2,3-linkage due to the absence of α2,6-sialyltransferase (St6gal1) expression. The Chinese hamster ST6GAL1 was successfully overexpressed using a plasmid expression vector in three recombinant immunoglobulin G (IgG)-producing CHO cell lines. The stably transfected cell lines were enriched for ST6GAL1 overexpression using FITC… CONTINUE READING
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The genomic Page 25 of 45 John Wiley & Sons Biotechnology Progress This article is protected by copyright

  • X. Xu, H. Nagarajan, +19 authors B. O. Palsson
  • All rights reserved
  • 2011

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