Glycosylation protein therapeutics

Due to the structural complexity of therapeutic proteins, their recombinant forms are usually produced in mammalian cell culture. When glyco-sylation is not present or is not essential for biological activity, therapeutic proteins can be produced in bacteria (e.g. E. coli) or yeast (e.g. Sacchar-omyces cerevisiae). However, some studies propose the use of these systems for glycosylated proteins as well. 

Gumming, D.A., Glycosylation of recombinant protein therapeutics Control and functional implications. Glycobiology, 1991, 1, 115-130. 

Werner R, Kopp K, Schlueter, M (2007) Glycosylation of therapeutic proteins in different production systems. Acta Paediatr Suppl 96(455) 17-22. 

All these approaches complement each other and it is envisaged that, either alone or in combination, they will continue to enable the generation of glycosylated proteins with predesigned modifications and increasing complexity for the elucidation of the molecular basis of protein glycosylation. This realization will certainly contribute to the development of novel and improved glycoprotein-derived therapeutics in the next few years. 

Glycosylation Engineering Alternate Expression Hosts For Recombinant Protein Therapeutic Production... 

It is desirable to perfect eukaryotic transfection for a number of reasons. Some proteins with therapeutic value have sugar residues attached to them. Such proteins are known as glycosylated proteins. As is the case for insuhn production, it would be beneficial to use cell culture-based processes to produce specific glycosylated proteins with therapeutic potential. However, glycosylated proteins are not... 

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