Project

High quality therapeutic glycoproteins

Glycosylation is one of the major post translation modifications to proteins in mammals. During this enzymatic process, sugar chains are attached to newly developed proteins. These sugar chains are called glycans and play an important role in the stability, function, recognition and folding of proteins. Also many therapeutic proteins like vaccines, antibodies and enzymes require glycans to have full biological activity.

The use of plants or mushrooms systems for the production of pharmaceutical glycoproteins offers an attractive alternative to the current state-of-the-art in protein production. The differences in glycan structures added by plants or mushrooms, in comparison to those found in humans, pose obstacles for the use as a pharmaceutical production system.

Therefore, the aim is to study the N-glycosylation in these organisms in more detail. By introducing mammalian enzymes a more humanizing end-glycan profile is produced which enables production of high quality therapeutic proteins. In our research we use the plant species Arabidopsis thaliana, Nicotiana tabacum and Nicotiana benthamiana. Furthermore, by developing tools for glycoprofiling and for assessing proteins quality using state of the art “omics” technology we are able to measure the integrity of the produced proteins in more detail.

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