Silencing β1,2-xylosyltransferase in Transgenic Tomato Fruits Reveals xylose as Constitutive Component of Ige-Binding Epitopes.

Complex plant N-glycans containing β1,2-xylose and core α1,3-fucose are regarded as the major class of the so-called "carbohydrate cross-reactive determinants" reactive with IgE antibodies in sera of many allergic patients, but their clinical relevance is still under debate. 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 N-glycans of glycoproteins, respectively. To test the clinical relevance of β1,2-xylose-containing epitopes, expression of the tomato β1,2-xylosyltransferase was down-regulated by RNA interference (RNAi) in transgenic plants.

The second face of a known player: Arabidopsis silencing suppressor AtXRN4 acts organ-specifically.

Plant viruses exploit the symplastic transport pathway provided by plasmodesmata by encoding for specialized movement proteins, which interact with host factors to enable viral intracellular and intercellular spread. Stable expression of the Potato leaf roll virus movement protein MP17 in Arabidopsis results in a carbohydrate export block and stunted growth. To identify host factors essential for viral infection, we screened a progeny population of EMS (ethyl methanesulfonate)-mutagenized Arabidopsis expressing a MP17:GFP fusion for suppressor mutants with restored wild type-like phenotype.