Staff Publications

Staff Publications

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    'Staff publications' is the digital repository of Wageningen University & Research

    'Staff publications' contains references to publications authored by Wageningen University staff from 1976 onward.

    Publications authored by the staff of the Research Institutes are available from 1995 onwards.

    Full text documents are added when available. The database is updated daily and currently holds about 240,000 items, of which 72,000 in open access.

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Record number 400695
Title Characterization of the single-chain Fv-Fc antibody MBP10 produced in Arabidopsis alg3 mutant seeds
Author(s) Henquet, M.G.L.; Eigenhuijsen, J.; Hesselink, T.; Spiegel, H.; Schreuder, M.E.L.; Duijn, E. van; Cordewener, J.H.G.; Depicker, A.; Krol, A.R. van der; Bosch, H.J.
Source Transgenic Research 20 (2011)5. - ISSN 0962-8819 - p. 1033 - 1042.
Department(s) Laboratory of Plant Physiology
PRI BIOS Applied Metabolic Systems
PRI BIOS Applied Genomics & Proteomics
Publication type Refereed Article in a scientific journal
Publication year 2011
Keyword(s) n-acetylglucosaminyltransferase-i - human beta-1,4-galactosyltransferase - monoclonal-antibody - mass-spectrometry - transgenic plants - linked glycans - glycosylation - cells - protein
Abstract ER resident glycoproteins, including ectopically expressed recombinant glycoproteins, carry so-called high-mannose type N-glycans, which can be at different stages of processing. The presence of heterogeneous high-mannose type glycans on ER-retained therapeutic proteins is undesirable for specific therapeutic applications. Previously, we described an Arabidopsis alg3-2 glycosylation mutant in which aberrant Man5GlcNAc2 mannose type N-glycans are transferred to proteins. Here we show that the alg3-2 mutation reduces the N-glycan heterogeneity on ER resident glycoproteins in seeds. We compared the properties of a scFv-Fc, with a KDEL ER retention tag (MBP10) that was expressed in seeds of wild type and alg3-2 plants. N-glycans on these antibodies from mutant seeds were predominantly of the intermediate Man5GlcNAc2 compared to Man8GlcNAc2 and Man7GlcNAc2 isoforms on MBP10 from wild-type seeds. The presence of aberrant N-glycans on MBP10 did not seem to affect MBP10 dimerisation nor binding of MBP10 to its antigen. In alg3-2 the fraction of underglycosylated MBP10 protein forms was higher than in wild type. Interestingly, the expression of MBP10 resulted also in underglycosylation of other, endogenous glycoproteins
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