Evidence map›Paper›PMID 21317243›Full record

ArticleGlycobiology2011

N-glycosylation engineering of plants for the biosynthesis of glycoproteins with bisected and branched complex N-glycans.

Alexandra Castilho, Pia Gattinger, Josephine Grass, Jakub Jez, Martin Pabst, Friedrich Altmann, Markus Gorfer, Richard Strasser, Herta Steinkellner

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
15.3field-weighted citation impact, top 1% 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

73 citing papers in PubMed, 137 citations in OpenAlex.

  1. Mass Spectrometric Analysis ofMolecules (Basel, Switzerland) · 2026
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  10. Trafficking and localization of Golgi-residentFrontiers in plant science · 2025
    Review
  11. Identification and comparison ofFood chemistry: X · 2025
    Article
  12. Introduction of a human- and keyboard-friendly N-glycan nomenclature.Beilstein journal of organic chemistry · 2024
    Article
  13. Green Biologics: Harnessing the Power of Plants to Produce Pharmaceuticals.International journal of molecular sciences · 2023
    Review
  14. Molecular Farming of Pembrolizumab and Nivolumab.International journal of molecular sciences · 2023
    Review
  15. Review
  16. Article
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  18. Plant-based biopharmaceutical engineering.Nature reviews bioengineering · 2023
    Review
  19. Article
  20. Review

13 more citing papers are in PubMed but not listed here.

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.

Alexandra CastilhoDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Pia Gattinger
Josephine Grass
Jakub Jez
Martin Pabst
Friedrich Altmann
Markus Gorfer
Richard Strasser
Herta Steinkellner
BOKU University · AT

Funding

Austrian Science Fund FWF L 575Austrian Science Fund FWF P 20817
6 · The paper itself

Abstract

Glycoengineering is increasingly being recognized as a powerful tool to generate recombinant glycoproteins with a customized N-glycosylation pattern. Here, we demonstrate the modulation of the plant glycosylation pathway toward the formation of human-type bisected and branched complex N-glycans. Glycoengineered Nicotiana benthamiana lacking plant-specific N-glycosylation (i.e. β1,2-xylose and core α1,3-fucose) was used to transiently express human erythropoietin (hEPO) and human transferrin (hTF) together with modified versions of human β1,4-mannosyl-β1,4-N-acetylglucosaminyltransferase (GnTIII), α1,3-mannosyl-β1,4-N-acetylglucosaminyltransferase (GnTIV) and α1,6-mannosyl-β1,6-N-acetylglucosaminyltransferase (GnTV). hEPO was expressed as a fusion to the IgG-Fc domain (EPO-Fc) and purified via protein A affinity chromatography. Recombinant hTF was isolated from the intracellular fluid of infiltrated plant leaves. Mass spectrometry-based N-glycan analysis of hEPO and hTF revealed the quantitative formation of bisected (GnGnbi) and tri- as well as tetraantennary complex N-glycans (Gn[GnGn], [GnGn]Gn and [GnGn][GnGn]). Co-expression of GnTIII together with GnTIV and GnTV resulted in the efficient generation of bisected tetraantennary complex N-glycans. Our results show the generation of recombinant proteins with human-type N-glycosylation at great uniformity. The strategy described here provides a robust and straightforward method for producing mammalian-type N-linked glycans of defined structures on recombinant glycoproteins, which can advance glycoprotein research and accelerate the development of protein-based therapeutics.

Indexed as

ErythropoietinGlycosylationHumansNicotianaPlant LeavesPolysaccharidesProtein EngineeringRecombinant ProteinsTransferrinEPO protein, humanErythropoietinPolysaccharidesRecombinant ProteinsTransferrin

Identifiers

PMID21317243
PMCPMC3091529
OpenAlexW2132435508

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.