Glycoconjugates such as glycoproteins and glycolipids containing N-glycoylneuraminic acid (Neu5Gc) are extremely antigenic in chickens and high titers of antibodies specifically directed against the carbohydrate have been expressed in the serum of these animals and their eggs. It has been suspected that a similar immunogenic response may be elicited in humans if they are exposed to glycoconjugates bearing Neu5Gc. In the present work, we attempted to employ co-expression strategy of CMP-sialic acid transporter (CMP-SAT) that is antiporter and transports cytosolic CMP-sialic acid into the Golgi lumen. Therefore, co-expression of CMP-SAT can increase transportation of CMP-N-acetylneuraminic acid (CMP-Neu5Ac) to the Golgi compartment and this could also lead to reduction of turnover rate of CMP-Neu5Ac to CMP-Neu5Gc in cytosol that is mediated by hydroxylase. We employed rhDNase as a model human glycoprotein in Chinese hamster ovary (CHO) cells because this protein has comparatively high levels of Neu5Gc in its N-glycans.

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