Abstract
Glycosylation affects many general functional factors of a glycoprotein, such as stability, inhibition of proteolysis, solubility, aggregation, as well as other attributes critical to its use as a biotherapeutic. Therefore our understanding of the glycosylation pathway, factors that affect it, and our ability to manipulate glycosylation are essential in producing superior biotherapeutics. The complex synthetic pathway of N-linked glycosylation occurs in both the endoplasmic reticulum and Golgi and involves a large number of precursors and enzymes, leading to a large array of possible glycan structures. Thus, variability in glycosylation may be influenced by numerous factors that affect this pathway, such as host cell type, nutrient levels and supplements, dissolved oxygen, pH, temperature, and by-product accumulation, and thus must be closely monitored. Better analytical techniques have allowed linking specific glycan structures to functionality of glycoproteins, which have led to efforts to modify glycosylation through genetic engineering, sequence-interfering RNA (siRNA), glycosylation inhibitors or chemoenzymatic modification.
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Spearman, M., Butler, M. (2015). Glycosylation in Cell Culture. In: Al-Rubeai, M. (eds) Animal Cell Culture. Cell Engineering, vol 9. Springer, Cham. https://doi.org/10.1007/978-3-319-10320-4_9
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