Down-regulated expression of plant-specific glycoepitopes in alfalfa.

Abstract:

SUMMARY: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, beta1,2-xylosyltransferase and alpha1,3-fucosyltransferases, using sense, antisense and RNA interference strategies. In a second approach, with the ultimate goal of rebuilding the whole human sialylation pathway, human beta1,4-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 alpha1,3-fucose- and beta1,2-xylose-containing glycoepitopes in transgenic alfalfa. However, recombinant human beta1,4-galactosyltransferase activity in transgenic alfalfa completely prevented the accumulation of the Lewis a glycoepitope on complex N-glycans.

journal_name

Plant Biotechnol J

authors

Sourrouille C,Marquet-Blouin E,D'Aoust MA,Kiefer-Meyer MC,Seveno M,Pagny-Salehabadi S,Bardor M,Durambur G,Lerouge P,Vezina L,Gomord V

doi

10.1111/j.1467-7652.2008.00353.x

subject

Has Abstract

pub_date

2008-09-01 00:00:00

pages

702-21

issue

7

eissn

1467-7644

issn

1467-7652

pii

PBI353

journal_volume

6

pub_type

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