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Plant Physiol, October 1999, Vol. 121, pp. 333-344

Biosynthesis and Immunolocalization of Lewis a-Containing N-Glycans in the Plant Cell1

Anne-Catherine Fitchette, Marion Cabanes-Macheteau, Laure Marvin, Barry Martin, Béatrice Satiat-Jeunemaitre, Véronique Gomord, Kim Crooks, Patrice Lerouge, Loïc Faye,* and Chris Hawes

Laboratoire des Transports Intracellulaires, Centre National de la Recherche Scientifique ESA 6037, European Institute for Peptide Research (IFRMP 23), Université de Rouen, Faculté des Sciences, 76821 Mont Saint Aignan cédex, France (A.-C.F., M.C.-M., V.G., P.L., L.F.); Spectrométrie de Masse Bioorganique, Centre National de la Recherche Scientifique ESA 6014, IFRMP 23, Université de Rouen, Faculté des Sciences, 76821 Mont Saint Aignan cédex, France (L.M.); Research School of Biological and Molecular Sciences, Oxford Brookes University, Gipsy Lane, Headington, Oxford OX3 0BP, United Kingdom (B.M., K.C., C.H.); and Institut des Sciences Végétales, Centre National de la Recherche Scientifique UPR 40, 91198 Gif-sur-Yvette, France (B.S.-J.)

We recently demonstrated the presence of a new asparagine-linked complex glycan on plant glycoproteins that harbors the Lewis a (Lea), or Galbeta (1-3)[Fucalpha (1-4)]GlcNAc, epitope, which in mammalian cells plays an important role in cell-to-cell recognition. Here we show that the monoclonal antibody JIM 84, which is widely used as a Golgi marker in light and electron microscopy of plant cells, is specific for the Lea antigen. This antigen is present on glycoproteins of a number of flowering and non-flowering plants, but is less apparent in the Cruciferae, the family that includes Arabidopsis. Lea-containing oligosaccharides are found in the Golgi apparatus, and our immunocytochemical experiments suggest that it is synthesized in the trans-most part of the Golgi apparatus. Lea epitopes are abundantly present on extracellular glycoproteins, either soluble or membrane bound, but are never observed on vacuolar glycoproteins. Double-labeling experiments suggest that vacuolar glycoproteins do not bypass the late Golgi compartments where Lea is built, and that the absence of the Lea epitope from vacuolar glycoproteins is probably the result of its degradation by glycosidases en route to or after arrival in the vacuole.

1 This work has been conducted in the French network "GT-rec" supported by MENRT (ACC SV 14, no. 9514111), Centre National de la Recherche Scientifique (Program PCV). This work was also supported by the University of Rouen, the Région Haute-Normandie and by a British council/Centre National de la Recherche Scientifique Alliance grant to C.H., B.S.-J., and L.F.

* Corresponding author; e-mail lfaye{at}crihan.fr; fax 33-2-35-14-67-87.

© 1999 American Society of Plant Physiologists


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