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N-linked oligosaccharide processing is not necessary for glycoprotein secretion in plants
Authors:Patrice Lerouge,Anne-Catherine Fitchette-Lainé  ,Aï  cha Chekkafi,Vé  ronique Avidgor, Loï  c Faye
Affiliation:Centre Régional Universitaire de Spectroscopie, CNRS-URA 464, and;Laboratoire des Transports Intracellulaires, CNRS-URA 203, European Institute for Peptide Research (IFRMP no. 23), Universitéde Rouen, 76821 Mont Saint Aignan, France
Abstract:
The role of N-glycans in the secretion of glycoproteins by suspension-cultured sycamore cells was studied. The transport of glycoproteins to the extracellular compartment was investigated in the presence of a glycan-processing inhibitor, castanospermine. Castanospermine has been selected because it inhibits homogeneously glycan maturation in sycamore cells and leads to the accumulation of a single immature N-glycan. The structure of this glycan has been identified as Glc3Man7GlcNAc2 by labeling experiments, affinity chromatography on concanavalin A-Sepharose and proton NMR. In contrast with previous results showing that N-glycosylation is a pre-requisite for secretion of N-linked glycoproteins, this secretion is not affected by the presence of castanospermine. As a consequence, the presence of this unprocessed glycan is sufficient for an efficient secretion of glycoproteins in the extracellular compartment of suspension-cultured sycamore cells.
Keywords:
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