XXXX supplementation enhance sialylation of recombinant Fc-fusion protein in CHO cell: an insight into the role of galactosylation in sialylation.

@entity20561 @entity3167 @entity413 @entity3649
UNASSIGNED: @entity3167 levels of therapeutic glycoprotein play an important role in plasma half-life. An undesirable decrease of @entity3167 content was observed when we increased Fc-fusion protein productivity fourfold in a GS-CHO cell line by bioprocess optimization. We investigated the potential mechanism for the @entity3167 content reduction. We found that limited @entity20561 precursor and the extracellular sialidase were not responsible for the reduction of the @entity3167 content after titer improvement. Oligosaccharide analysis revealed that the lack of protein galactosylation was the potential cause for the reduction of @entity3167 content. Thus we validated this notion by evaluated @entity3649 supplementation in 2  L bioreactors. Cell culture performance was not impacted by addition of up to 40  mM @entity3649 except for the @entity413 consumption rate. Addition of 20  mM @entity3649 to the bioreactor resulted in the increase of 44  % for total @entity3167 content and 20.3  % for sialylated glycans. These data were further validated when the process was run on 200  L scaled bioreactor. These data together show that the galactosylation plays an apparent role in sialylation in our current system.
