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.
journal_name
Cytotechnologyjournal_title
Cytotechnologyauthors
Monaco L,Marc A,Eon-Duval A,Acerbis G,Distefano G,Lamotte D,Engasser JM,Soria M,Jenkins Ndoi
10.1007/BF00353939subject
Has Abstractpub_date
1996-01-01 00:00:00pages
197-203issue
1-3eissn
0920-9069issn
1573-0778journal_volume
22pub_type
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