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Monaco L, Marc A, Eon-Duval A, et al. Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ. Cytotechnology. 1996;22(1):197-203doi: 10.1007/BF00353939.
Monaco, L., Marc, A., Eon-Duval, A., Acerbis, G., Distefano, G., Lamotte, D., Engasser, J. M., Soria, M., & Jenkins, N. (1996). Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ. Cytotechnology, 22(1), 197-203. https://doi.org/10.1007/BF00353939
Monaco, L, et al. "Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ." Cytotechnology vol. 22,1 (1996): 197-203. doi: https://doi.org/10.1007/BF00353939
Monaco L, Marc A, Eon-Duval A, Acerbis G, Distefano G, Lamotte D, Engasser JM, Soria M, Jenkins N. Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ. Cytotechnology. 1996 Jan;22(1):197-203. doi: 10.1007/BF00353939. PMID: 22358930.
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Cytotechnology. 1996 Jan;22(1):197-203. doi: 10.1007/BF00353939.

Genetic engineering of α2,6-sialyltransferase in recombinant CHO cells and its effects on the sialylation of recombinant interferon-γ.

Cytotechnology

L Monaco, A Marc, A Eon-Duval, G Acerbis, G Distefano, D Lamotte, J M Engasser, M Soria, N Jenkins

Affiliations

  1. Department of Biological & Technological Research, San Raffaele Scientific Institute, Milan, Italy.

PMID: 22358930 DOI: 10.1007/BF00353939

Abstract

The CHO cell line has achieved considerable commercial importance as a vehicle for the production of human therapeutic proteins, but is known to lack a functional copy of the gene coding for α2,6-sialyltransferase (EC 2.4.99.1). The cDNA for rat α2,6-ST was expressed in a recombinant CHO cell line making interferon-γ, using a novel in vitro amplification vector. The enzyme was expressed efficiently, and resulted in up to 60% of the total sialic acids on interferon-γ being linked in the α2,6-conformation. This sialic acid linkage distribution was more akin to that seen in natural human glycoproteins. In the most successful cell clones, expression of α2,6-sialyltransferase improved the overall level of sialylation by up to 56%, and had no adverse effects on cell growth, IFN-γ productivity or other aspects of IFN-γ glycosylation. These experiments demonstrate how the glycosylation machinery of rodent cells can be genetically manipulated to replicate human tissues.

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