Team:Marburg/Human Practice/Talk of Peter Hermentin
From 2013.igem.org
Talk of Peter Hermentin
The accurate effectiveness of an antibody depends on its glycosylation pattern whereupon the core region may appear similar to:
N: N-Acetyl-D-glucosamine
[Fuc]:Fucose
As a general problem regarding the antibody production in non-mammals like plants and especially microalgae Mr Hermentin advised us of different glycosyltransferases used in this species that create glycosylation patterns that are not biocompatible to humans. [[File:Dr. Peter Hermentin.jpg|thumbs|right] To accomplish his lecture, he presented a possibility to avoid this problem in our organism Phaeodactylum tricornutum. Interestingly, PHAECTORY provides all enzymes required for N-Glycan biosynthesis in its ER and Golgi complex. Additionally, P. tricornutum is capable to build high-mannose structures. Unfortunately, the organism uses two glycosyltransferases, α(1,3)-Fucosyltransferase and β(1,2)-Xyloysltransferase, that are not compatible to humans. This means that the production of therapeutic antibodies in P. tricornutum for human application demands the knockout of these two genes.
For further information check out these two articles:
[1] Baiet B, Burel C, Saint-Jean B, Louvet R, Menu-Bouaouiche L, Kiefer-Meyer MC, et al. N-glycans of Phaeodactylum tricornutum diatom and functional characterization of its N-acetylglucosaminyltransferase I enzyme. J Biol Chem. 2011, 286(8), 6152-64.
[2] Bowler C, Allen AE, Badger JH, Grimwood J, Jabbari K, Kuo A, et al. The Phaeodactylum genome reveals the evolutionary history of diatom genomes. Nature. 2008, 456(7219), 239-44.