Comparative analysis of the site-specific N-glycosylation of human lactoferrin produced in maize and tobacco plants.
Samyn-Petit, Benedicte 1; Dubos, Jean-Pierre Wajda 2; Chirat, Frederic 1; Coddeville, Bernadette 1; Demaizieres, Gregory 2; Farrer, Sybille 2; Slomianny, Marie-Christine 1; Theisen, Manfred 2; Delannoy, Philippe 1
[Article] European Journal of Biochemistry. 270(15):3235-3242, August 2003.

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We have compared the site-by-site N-glycosylation status of human lactoferrin (Lf) produced in maize, a monocotyledon, and in tobacco, used as a model dicotyledon. Maize and tobacco plants were stably transformed and recombinant Lf was purified from both seeds and leaves. N-glycopeptides were generated by trypsin digestion of recombinant Lf and purified by reverse-phase HPLC. The N-glycosylation pattern of each site was determined by mass spectrometry. Our results indicated that the N-glycosylation patterns of recombinant Lf produced in maize and tobacco share common structural features. In particular, both N-glycosylation sites of each recombinant Lf are mainly substituted by typical plant paucimannose-type N-glycans, with [beta]1,2-xylose and [alpha]1,3-linked fucose at the proximal N-acetylglucosamine. However, tobacco Lf shows a significant amount of processed N-glycans with one or two [beta]1,2GlcNAc linked to the trimannose core, which are weakly expressed in maize Lf. Finally, no Lewisa epitope was observed on tobacco Lf.

(C) 2003 Blackwell Science Ltd.