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Gewählte Publikation:

Strasser, R; Altmann, F; Mach, L; Glössl, J; Steinkellner, H; .
(2004): Generation of Arabidopsis thaliana plants with complex N-glycans lacking beta1,2-linked xylose and core alpha1,3-linked fucose.
FEBS Lett. 2004; 561(1-3):132-136 FullText FullText_BOKU

Abstract:
The plant glycosyltransferases, beta1,2-xylosyltransferase (XylT) and core alpha1,3-fucosyltransferase (FucT), are responsible for the transfer of beta1,2-linked xylose and core alpha1,3-linked fucose residues to glycoprotein N-glycans. These glycan epitopes are not present in humans and thus may cause immunological responses, which represent a limitation for the therapeutic use of recombinant mammalian glycoproteins produced in transgenic plants. Here we report the genetic modification of the N-glycosylation pathway in Arabidopsis thaliana plants. Knockout plants were generated with complete deficiency of XylT and FucT. These plants lack antigenic protein-bound N-glycans and instead synthesise predominantly structures with two terminal betaN-acetylglucosamine residues (GlcNAc(2)Man(3)GlcNAc(2)). (C) 2004 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Autor*innen der BOKU Wien:
Altmann Friedrich
Glößl Josef
Mach Lukas
Steinkellner Herta
Strasser Richard
Find related publications in this database (using NML MeSH Indexing)
Acetylglucosamine;Arabidopsis/enzymology;Arabidopsis/genetics*;Blotting, Western;Fucose/analysis;Fucose/deficiency;Fucosyltransferases/analysis;Fucosyltransferases/deficiency*;Fucosyltransferases/genetics;Glycosylation;Mutation*;Pentosyltransferases/analysis;Pentosyltransferases/deficiency*;Pentosyltransferases/genetics;Polysaccharides/biosynthesis*;Polysaccharides/chemistry;Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization;Xylose/analysis;Xylose/deficiency;

Find related publications in this database (Keywords)
beta 1,2-xylosyltransferase
core alpha 1,3-fucosyltransferase
glycosyltransferase
N-glycan
Arabidopsis thaliana


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