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- Title
Down-regulated expression of plant-specific glycoepitopes in alfalfa.
- Authors
Sourrouille, Christophe; Marquet‐Blouin, Estelle; D'Aoust, Marc‐André; Kiefer‐Meyer, Marie‐Christine; Seveno, Martial; Pagny‐Salehabadi, Sophie; Bardor, Muriel; Durambur, Gaelle; Lerouge, Patrice; Vezina, Louis; Gomord, Véronique
- Abstract
Compared with other plant expression systems used for pharmaceutical protein production, alfalfa offers the advantage of very homogeneous N-glycosylation. Therefore, this plant was selected for further attempts at glycoengineering. Two main approaches were developed in order to humanize N-glycosylation in alfalfa. The first was a knock-down of two plant-specific N-glycan maturation enzymes, β1,2-xylosyltransferase and α1,3-fucosyltransferases, using sense, antisense and RNA interference strategies. In a second approach, with the ultimate goal of rebuilding the whole human sialylation pathway, human β1,4-galactosyltransferase was expressed in alfalfa in a native form or in fusion with a targeting domain from N-acetylglucosaminyltransferase I, a glycosyltransferase located in the early Golgi apparatus in Nicotiana tabacum. Both knock-down and knock-in strategies strongly, but not completely, inhibited the biosynthesis of α1,3-fucose- and β1,2-xylose-containing glycoepitopes in transgenic alfalfa. However, recombinant human β1,4-galactosyltransferase activity in transgenic alfalfa completely prevented the accumulation of the Lewis a glycoepitope on complex N-glycans.
- Subjects
ALFALFA; FORAGE plants; PROTEINS; PROTOPLASM; NUCLEIC acids; RNA; TOBACCO; BIOCHEMICAL engineering; GOLGI apparatus; BIOSYNTHESIS
- Publication
Plant Biotechnology Journal, 2008, Vol 6, Issue 7, p702
- ISSN
1467-7644
- Publication type
Article
- DOI
10.1111/j.1467-7652.2008.00353.x