Generation of Arabidopsis thaliana plants with complex N-glycans lacking β1,2-linked xylose and core α1,3-linked fucose

被引:241
作者
Strasser, R
Altmann, F
Mach, L
Glössl, J
Steinkellner, H
机构
[1] Univ Bodenkultur Wien, Inst Angew Genet & Zellbiol, A-1190 Vienna, Austria
[2] Univ Bodenkultur Wien, Inst Chem, A-1190 Vienna, Austria
基金
美国国家科学基金会; 奥地利科学基金会;
关键词
beta 1,2-xylosyltransferase; core alpha 1,3-fucosyltransferase; glycosyltransferase; N-glycan; Arabidopsis thaliana;
D O I
10.1016/S0014-5793(04)00150-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:132 / 136
页数:5
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