Evidence map›Paper›PMID 22791304›Full record

ArticlePlant physiology2012

Toward stable genetic engineering of human O-glycosylation in plants.

Zhang Yang, Eric P Bennett, Bodil Jørgensen, Damian P Drew, Emma Arigi, Ulla Mandel, Peter Ulvskov, Steven B Levery, Henrik Clausen, Bent L Petersen

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
5.1field-weighted citation impact, top 5% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

15 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Arabidopsis ROCK1 transports UDP-GlcNAc/UDP-GalNAc and regulates ER protein quality control and cytokinin activity.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Review
  12. Article
  13. Engineering of sialylated mucin-type O-glycosylation in plants.The Journal of biological chemistry · 2012
    Article
  14. Article
  15. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors at 2 institutions in 1 country.

Zhang YangDepartment of Molecular Biology and Genetics, Faculty of Science and Technology, Aarhus University, Flakkebjerg, 4200 Slagelse, Denmark.
Eric P Bennett
Bodil Jørgensen
Damian P Drew
Emma Arigi
Ulla Mandel
Peter Ulvskov
Steven B Levery
Henrik Clausen
Bent L Petersen
Aarhus University · DKUniversity of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

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.

Indexed as

AcetylgalactosamineArabidopsisBacterial ProteinsCell Culture TechniquesCulture MediaGenetic EngineeringGlycosylationHumansHydroxylationLuminescent ProteinsMucin-1NicotianaPlant CellsPlant ProteinsPlants, Genetically ModifiedProlineAcetylgalactosamineBacterial ProteinsCulture MediaLuminescent ProteinsMucin-1Plant ProteinsProlineRecombinant Proteinsyellow fluorescent protein, Bacteria

Identifiers

PMID22791304
PMCPMC3440218
OpenAlexW2089287684

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.