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Generation of Arabidopsis thaliana plants with complex N ‐glycans lacking β1,2‐linked xylose and core α1,3‐linked fucose
Author(s) -
Strasser R.,
Altmann F.,
Mach L.,
Glössl J.,
Steinkellner H.
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00150-4
Subject(s) - glycan , fucose , fucosyltransferase , glycosylation , arabidopsis thaliana , glycoprotein , glycosyltransferase , epitope , biochemistry , arabidopsis , xylose , n linked glycosylation , recombinant dna , fucosylation , chemistry , biology , microbiology and biotechnology , gene , genetics , antigen , mutant , fermentation
The plant glycosyltransferases, β1,2‐xylosyltransferase (XylT) and core α1,3‐fucosyltransferase (FucT), are responsible for the transfer of β1,2‐linked xylose and core α1,3‐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 β N ‐acetylglucosamine residues (GlcNAc 2 Man 3 GlcNAc 2 ).