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.
Cooperation within Wageningen UR
Cooperation outside Wageningen UR
- University of Utrecht, The Netherlands
- University of Amsterdam, The Netherlands
- Fraunhofer- IME, Germany
- Bayer Bioscience, Belgium
- ICON genetics, Germany
- Greenovation Biotech, Germany
- University of Surrey, United Kingdom
- University of Natural Resources Austria and Applied Life Sciences (BOKU)
- Dow Agroscience (DAS), US/Germany
- Zürcher Hochschule, Switserland
- VTT, Finland
- RWTH Aachen, Germany
- St George’s Hospital Medical School (SGHMS), United Kingdom
- Forschungszentrum Jülich,Germany
- Kühner AG, Switzerland
Experts
Reports en publications
- Henquet, M., et al (2009). Differential effects of human and plant N-acetylglucosaminyltransferase I (GnTI) in plants. Transgenic Res. 2009
- Zhang, M., Henquet, M., et al (2009). LEW3, encoding a putative alpha-1,2-mannosyltransferase (ALG11) in N-linked glycoprotein, plays vital roles in cell-wall biosynthesis and the abiotic stress response in Arabidopsis thaliana. Plant J. 2009
- Henquet, M., et al. (2010) Characterization of the single-chain Fv-Fc antibody MBP10 produced in Arabidopsis alg3 mutant seeds. Transgenic Research.
- Rouwendal, G.J., et al. (2009) Synthesis of Lewis X epitopes on plant N-glycans. Carbohydr Res. 344(12): p. 1487-93.
- Bosch, H.J.; Schots, A. (2010) Plant glycans: friend or foe in vaccine development? Expert Review Vaccines 9 (8). - p. 835 - 842.
- Berends, E.; Scholtmeijer, K.; Wösten, H.A.B.; Bosch, H.J.; Lugones, L.G. (2009) The use of mushroom-forming fungi for the production of N-glycosylated therapeutic proteins. Trends in Microbiology 17 (10). - p. 439 - 443.
- M, Eigenhuijsen J, Hesselink T, Spiegel H, Schreuder M, van Duijn E, Cordewener J, Depicker A, van der Krol A, Bosch D (2011) Characterization of the single-chain Fv-Fc antibody MBP10 produced in Arabidopsis alg3 mutant seeds. Henquet. Transgenic Res; 20(5):1033-42.
Press
Websites