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Comparative analysis of the site-specific N-glycosylation of human lactoferrin produced in maize and tobacco plants


Comparative analysis of the site-specific N-glycosylation of human lactoferrin produced in maize and tobacco plants



European Journal of Biochemistry 270(15): 3235-3242



ISSN/ISBN: 0014-2956

PMID: 12869199

DOI: 10.1046/j.1432-1033.2003.03706.x

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 beta1,2-xylose and alpha1,3-linked fucose at the proximal N-acetylglucosamine. However, tobacco Lf shows a significant amount of processed N-glycans with one or two beta1,2GlcNAc linked to the trimannose core, which are weakly expressed in maize Lf. Finally, no Lewisa epitope was observed on tobacco Lf.

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Accession: 003684772

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