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Microheterogeneity of the oligosaccharides carried by the recombinant bovine lactoferrin expressed in Mamestra brassicae cells |
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| Authors: | Lopez Michel; Coddeville Bernadette; Langridge James; Plancke Yves; Sautiere Pierre; Chaabihi Hassan; Chirat Frederic; Harduin-Lepers Anne; Cerutti Martine; Verbert Andre; Delannoy Philippe |
| Institution: | 1Laboratoire de Chimie Biologique, Unité Mixte de Recherche du CNRS n° 111, Université des Sciences et Technologies de Lille F-59655 Villeneuve d'Ascq, France 2Société Protéine-Performance, Route d'Alès, F-30380 Saint Christol-les-Alès, France 3Micromass UK Limited, 3 Tudor Road, Altrincham, Cheshire, WA14 5RZ, United Kingdom 4Laboratoire de Chimie des Biomolécules Unité de Recherche Associée du CNRS n° 1309, Institut Pasteur de Lille, 1 Rue du Professeur Calmette, F-59019 Lille, France 5Station de Pathologie Comparée INRA/Unité de Recherche Associée du CNRS n° 2209, Route d'Alès, F-30380 Saint Christol-les-Alès, France |
| Abstract: | The development of therapeutic glycoprotein production usingthe baculovirus expression system depends on the ability ofinsect cell lines to reproduce site specific mammalian-likeN-glycans. A combination of 1H-NMR and mass spectrometry techniques(MALD-MS, ES-MS, and CID-MS-MS) allowed us to elucidate theN-linked oligosaccharides microheterogeneity on three differentN-glycosylation sites, Asn233, Asn476, and Asn545, of a baculovirus-expressedrecombinant bovine lactoferrin produced in Mamestra brassicae.Two families of N-glycan structures have been found: first,oligomannosidic glycans (Man95GlcNAC2) and secondly, short truncatedpartially fucosylated glycans (Man3–2Fuc0–1]GlcNAc2).These results indicate that Mamestra brassicae cell line isnot able to synthesize complex N-glycans, even if an |
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