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https://hdl.handle.net/2440/95813
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dc.contributor.author | Yang, Z. | - |
dc.contributor.author | Bennett, E. | - |
dc.contributor.author | Jørgensen, B. | - |
dc.contributor.author | Drew, D. | - |
dc.contributor.author | Arigi, E. | - |
dc.contributor.author | Mandel, U. | - |
dc.contributor.author | Ulvskov, P. | - |
dc.contributor.author | Levery, S. | - |
dc.contributor.author | Clausen, H. | - |
dc.contributor.author | Petersen, B. | - |
dc.date.issued | 2012 | - |
dc.identifier.citation | Plant Physiology, 2012; 160(1):450-463 | - |
dc.identifier.issn | 0032-0889 | - |
dc.identifier.issn | 1532-2548 | - |
dc.identifier.uri | http://hdl.handle.net/2440/95813 | - |
dc.description.abstract | Glycosylation is the most abundant and complex posttranslational modification to be considered for recombinant production of therapeutic proteins. Mucin-type (N-acetylgalactosamine [GalNAc]-type) O-glycosylation is found in eumetazoan cells but absent in plants and yeast, making these cell types an obvious choice for de novo engineering of this O-glycosylation pathway. We previously showed that transient implementation of O-glycosylation capacity in plants requires introduction of the synthesis of the donor substrate UDP-GalNAc and one or more polypeptide GalNAc-transferases for incorporating GalNAc residues into proteins. Here, we have stably engineered O-glycosylation capacity in two plant cell systems, soil-grown Arabidopsis (Arabidopsis thaliana) and tobacco (Nicotiana tabacum) Bright Yellow-2 suspension culture cells. Efficient GalNAc O-glycosylation of two stably coexpressed substrate O-glycoproteins was obtained, but a high degree of proline hydroxylation and hydroxyproline-linked arabinosides, on a mucin (MUC1)-derived substrate, was also observed. Addition of the prolyl 4-hydroxylase inhibitor 2,2-dipyridyl, however, effectively suppressed proline hydroxylation and arabinosylation of MUC1 in Bright Yellow-2 cells. In summary, stably engineered mammalian type O-glycosylation was established in transgenic plants, demonstrating that plants may serve as host cells for the production of recombinant O-glycoproteins. However, the present stable implementation further strengthens the notion that elimination of endogenous posttranslational modifications may be needed for the production of protein therapeutics. | - |
dc.description.statementofresponsibility | Zhang Yang, Eric P. Bennett, Bodil Jørgensen, Damian P. Drew, Emma Arigi, Ulla Mandel, Peter Ulvskov, Steven B. Levery, Henrik Clausen, and Bent L. Petersen | - |
dc.language.iso | en | - |
dc.publisher | American Society of Plant Biologists | - |
dc.rights | © 2012 American Society of Plant Biologists. All Rights Reserved. | - |
dc.source.uri | http://dx.doi.org/10.1104/pp.112.198200 | - |
dc.subject | Acetylgalactosamine | - |
dc.title | Toward stable genetic engineering of human O-glycosylation in plants | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1104/pp.112.198200 | - |
pubs.publication-status | Published | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest 3 |
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