Journal
FEBS LETTERS
Volume 472, Issue 1, Pages 105-108Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(00)01443-5
Keywords
beta 1,2-xylosyltransferase; glycosyltransferase; N-glycan; Arabdiposis thaliana
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The transfer of xylose from UDP-xylose to the core beta-linked mannose of N-linked oligosaccharides by beta 1,2-xylosyl-transferase (XylT) is a widespread feature of plant glycoproteins which renders them immunogenic and allergenic in man. Here, we report the isolation of the Arabidopsis thaliana XylT gene, which contains two introns and encodes a 60.2 kDa protein with a predicted type II transmembrane protein topology typical for Golgi glycosyltransferases, Upon expression of A. thaliana XylT cDNA in the baculovirus/insect cell system, a recombinant protein was produced that exhibited XylT activity in vitro. Furthermore, the recombinant enzyme displayed XylT activity in vivo in the insect cells, as judged by the acquired cross-reaction of cellular glycoproteins with antibodies against the beta 1,2-xylose epitope, The cloned XylT cDNA as well as the recombinant enzyme are essential tools to study the role of beta 1,2-xylose in the immunogenicity and allergenicity of plant glycoproteins at the molecular level. (C) 2000 Federation of European Biochemical Societies.
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