R
Renaud Léonard
Researcher at University of Natural Resources and Life Sciences, Vienna
Publications - 25
Citations - 1663
Renaud Léonard is an academic researcher from University of Natural Resources and Life Sciences, Vienna. The author has contributed to research in topics: Glycan & Arabidopsis thaliana. The author has an hindex of 19, co-authored 22 publications receiving 1541 citations.
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Journal ArticleDOI
In Planta Protein Sialylation through Overexpression of the Respective Mammalian Pathway
Alexandra Castilho,Richard Strasser,Johannes Stadlmann,Josephine Grass,Jakub Jez,Pia Gattinger,Renate Kunert,Heribert Quendler,Martin Pabst,Renaud Léonard,Friedrich Altmann,Herta Steinkellner +11 more
TL;DR: In vivo protein sialylation in plants is reported, which has been shown to be well suited for the efficient generation of complex mammalian glycoproteins and may serve as a general model for the manipulation of complex traits into plants.
Journal ArticleDOI
A Unique β1,3-Galactosyltransferase Is Indispensable for the Biosynthesis of N-Glycans Containing Lewis a Structures in Arabidopsis thaliana
Richard Strasser,Jayakumar Singh Bondili,Ulrike Vavra,Jennifer Schoberer,Barbara Svoboda,Josef Glössl,Renaud Léonard,Johannes Stadlmann,Friedrich Altmann,Herta Steinkellner,Lukas Mach +10 more
TL;DR: Results demonstrate that GALT1 is both sufficient and essential for the addition of β1,3-linked galactose residues to N-glycans and thus is required for the biosynthesis of Lewis a structures in Arabidopsis.
Journal ArticleDOI
The Drosophila fused lobes Gene Encodes an N-Acetylglucosaminidase Involved in N-Glycan Processing
Renaud Léonard,Dubravko Rendić,Catherine Rabouille,Iain B. H. Wilson,Thomas Preat,Friedrich Altmann +5 more
TL;DR: In this paper, a β-N-acetylglucosaminidase with a potential transmembrane domain was cloned and expressed in Pichia pastoris, which exhibited a substrate specificity similar to that previously described for a hexosamidase activity from Sf-9 cells, i.e., it hydrolyzed exclusively the GlcNAc residue attached to the α 1,3-linked mannose of the core pentasaccharide of N-glycans.
TheDrosophila fused lobesGene Encodes an N-Acetylglucosaminidase Involved in N-Glycan Processing *
TL;DR: The fdl gene encodes a novel hexosaminidase responsible for the occurrence of paucimannosidic N-glycans in Drosophila, and the ratio of structures with terminal GlcNAc over those without was drastically increased in the fdl-deficient flies.
Journal ArticleDOI
Two novel types of O-glycans on the mugwort pollen allergen Art v 1 and their role in antibody binding.
Renaud Léonard,Bent O. Petersen,Martin Himly,Waltraud Kaar,Nicole Wopfner,Daniel Kolarich,Ronald van Ree,Christof Ebner,Jens Ø. Duus,Fatima Ferreira,Friedrich Altmann +10 more
TL;DR: Although the authors could not observe antibody binding by the polysaccharide, the single hydroxyproline-linked β-arabinose residues appeared to react with the antibodies and constitute a new, potentially cross-reactive, carbohydrate determinant in plant proteins.