Open AccessComparative analysis of the site‐specific N‐glycosylation of human lactoferrin produced in maize and tobacco plants
Author(s) -
SamynPetit Bénédicte,
Wajda Dubos JeanPierre,
Chirat Frédéric,
Coddeville Bernadette,
Demaizieres Grégory,
Farrer Sybille,
Slomianny MarieChristine,
Theisen Manfred,
Delannoy Philippe
Publication year - 2003
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.1432-1033.2003.03706.x
Subject(s) - lactoferrin , glycosylation , chemistry , microbiology and biotechnology , biochemistry , biology
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 β1,2‐xylose and α1,3‐linked fucose at the proximal N ‐acetylglucosamine. However, tobacco Lf shows a significant amount of processed N‐glycans with one or two β1,2GlcNAc linked to the trimannose core, which are weakly expressed in maize Lf. Finally, no Lewis a epitope was observed on tobacco Lf.