Evidence map›Paper›PMID 25900423›Full record

ArticlePlant physiology and biochemistry : PPB2015

Characterization of plants expressing the human β1,4-galactosyltrasferase gene.

Jeannine Schneider, Alexandra Castilho, Martin Pabst, Friedrich Altmann, Clemens Gruber, Richard Strasser, Pia Gattinger, Georg J Seifert, Herta Steinkellner

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology and biochemistry : PPB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.3field-weighted citation impact, top 10% 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

22 citing papers in PubMed, 42 citations in OpenAlex.

  1. Review
  2. Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Production andFrontiers in plant science · 2023
    Article
  8. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  9. Review
  10. Article
  11. Review
  12. Unexpected Arabinosylation after Humanization of Plant ProteinFrontiers in bioengineering and biotechnology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Expression Profiling and Glycan Engineering of IgG Subclass 1-4 inFrontiers in bioengineering and biotechnology · 2020
    Article
  18. Review
  19. Frontiers in bioengineering and biotechnology · 2019
    Article
  20. 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

9 authors at 1 institution in 1 country.

Jeannine SchneiderDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Alexandra CastilhoDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Martin PabstDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Clemens GruberDepartment of Chemistry, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Pia GattingerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Georg J SeifertDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria.
Herta SteinkellnerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Muthgasse 18, 1190 Vienna, Austria. Electronic address: herta.steinkellner@boku.ac.at.
BOKU University · AT

Funding

Austrian Science Fund FWF I 1182Austrian Science Fund FWF L 575Austrian Science Fund FWF P 21782
6 · The paper itself

Abstract

Modification of the plant N-glycosylation pathway towards human type structures is an important strategy to implement plants as expression systems for therapeutic proteins. Nevertheless, relatively little is known about the overall impact of non-plant glycosylation enzymes in stable transformed plants. Here, we analyzed transgenic lines (Nicotiana benthamiana and Arabidopsis thaliana) that stably express a modified version of human β1,4-galactosyltransferase ((ST)GalT). While some transgenic plants grew normally, other lines exhibited a severe phenotype associated with stunted growth and developmental retardation. The severity of the phenotype correlated with both increased (ST)GalT mRNA and protein levels but no differences were observed between N-glycosylation profiles of plants with and without the phenotype. In contrast to non-transgenic plants, all (ST)GalT expressing plants synthesized significant amounts of incompletely processed (largely depleted of core fucose) N-glycans with up to 40% terminally galactosylated structures. While transgenic plants showed no differences in nucleotide sugar composition and cell wall monosaccharide content, alterations in the reactivity of cell wall carbohydrate epitopes associated with arabinogalactan-proteins and pectic homogalacturonan were detected in (ST)GalT expressing plants. Notably, plants with phenotypic alterations showed increased levels of hydrogen peroxide, most probably a consequence of hypersensitive reactions. Our data demonstrate that unfavorable phenotypical modifications may occur upon stable in planta expression of non-native glycosyltransferases. Such important issues need to be taken into consideration in respect to stable glycan engineering in plants.

Indexed as

PhenotypePlants, Genetically ModifiedArabidopsisCell WallEpitopesGalactosyltransferasesGenetic EngineeringGlycosylationHumansHydrogen PeroxideMucoproteinsN-Acetyllactosamine SynthaseNicotianaPectinsPlant LeavesPlant Proteinsarabinogalactan proteinsEpitopesGalactosyltransferasesHydrogen PeroxideMucoproteinsN-Acetyllactosamine SynthaseN-acetyllactosaminide alpha-1,3-galactosyltransferasePectinsPlant Proteinspolygalacturonic acidPolysaccharidesRNA, MessengerDevelopmental phenotypeGlyco-engineeringNicotiana benthamianaTransgenic plantsβ1,4-Galactosylation

Identifiers

PMID25900423
PMCPMC4451504
OpenAlexW2039409183

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.