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 Jjournal_title
Plant biotechnology journalauthors
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 Vdoi
10.1111/j.1467-7652.2008.00353.xsubject
Has Abstractpub_date
2008-09-01 00:00:00pages
702-21issue
7eissn
1467-7644issn
1467-7652pii
PBI353journal_volume
6pub_type
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