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PMID: 12151713 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

N-glycosylation potential of maize: the human lactoferrin used as a model.

Glycoconjugate journal ·Vol. 18 ·No. 7 ·2001-07-00 ·Pages 519-27

Samyn-Petit B, Gruber V, Flahaut C, Wajda-Dubos JP, Farrer S, Pons A, Desmaizieres G, Slomianny MC, Theisen M, Delannoy P

Abstract

In order to determine the N-glycosylation potential of maize, a monocotyledon expression system for the production of recombinant glycoproteins, human lactoferrin was used as a model. The human lactoferrin coding sequence was inserted into the pUC18 plasmid under control of the wheat glutenin promoter. Maize was stably transformed and recombinant lactoferrin was purified from the fourth generation seeds. Glycosylation was analysed by gas chromatography, lectin detection, glycosidase digestions and mass spectrometry. The results indicated that both N-glycosylation sites of recombinant lactoferrin are mainly substituted by typical plant paucimannose-type glycans, with beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine, and that complex-type glycans with Lewis(a) determinants are not present in maize recombinant lactoferrin.

MeSH Terms
Blotting, Western Glycosylation Humans Lactoferrin/metabolism Models, Chemical Recombinant Proteins/metabolism Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization Zea mays/metabolism
Chemicals
Recombinant Proteins Lactoferrin
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Samyn-Petit B
Meristem Therapeutics, 8 rue des Frères Lumière, 63100 Clermont-Ferrand, France.
Gruber V
Flahaut C
Wajda-Dubos J P
Farrer S
Pons A
Desmaizieres G
Slomianny M C
Theisen M
Delannoy P
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Article Info
Journal
Glycoconjugate journal
Abbr.
Glycoconj J
ISSN
0282-0080
DOI
10.1023/a:1019640312730
Published
2001-07-00
Pages
519-27
Language
English
Region
United States
NLM ID
8603310
Subset
IM
External Links
PubMed source DOI: 10.1023/a:1019640312730 View journal details
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