Evidence map›Paper›PMID 27421111›Full record

ArticlePlant biotechnology journal2017

Reduced paucimannosidic N-glycan formation by suppression of a specific β-hexosaminidase from Nicotiana benthamiana.

Yun-Ji Shin, Alexandra Castilho, Martina Dicker, Flavio Sádio, Ulrike Vavra, Clemens Grünwald-Gruber, Tae-Ho Kwon, Friedrich Altmann, Herta Steinkellner, Richard Strasser

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
5.4field-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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Engineering the mossFrontiers in plant science · 2025
    Article
  8. Article
  9. Recombinant neutralizing secretory IgA antibodies for preventing mucosal acquisition and transmission of SARS-CoV-2.Molecular therapy : the journal of the American Society of Gene Therapy · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  16. Review
  17. Review
  18. Engineering theFrontiers in plant science · 2022
    Article
  19. Review
  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

10 authors at 2 institutions in 2 countries.

Yun-Ji ShinDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Alexandra CastilhoDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Martina DickerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Flavio SádioDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Ulrike VavraDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Clemens Grünwald-GruberDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Tae-Ho KwonNBM Inc., Wanju-gun, Jeollabuk-do, Korea.
Friedrich AltmannDepartment of Chemistry, University of Natural Resources and Life Sciences, Vienna, Austria.
Herta SteinkellnerDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
Richard StrasserDepartment of Applied Genetics and Cell Biology, University of Natural Resources and Life Sciences, Vienna, Austria.
BOKU University · ATThe English Linguistics Society of Korea · KR

Funding

Austrian Science Fund FWF TRP 242
6 · The paper itself

Abstract

Plants are attractive hosts for the production of recombinant glycoproteins for therapeutic use. Recent advances in glyco-engineering facilitate the elimination of nonmammalian-type glycosylation and introduction of missing pathways for customized N-glycan formation. However, some therapeutically relevant recombinant glycoproteins exhibit unwanted truncated (paucimannosidic) N-glycans that lack GlcNAc residues at the nonreducing terminal end. These paucimannosidic N-glycans increase product heterogeneity and may affect the biological function of the recombinant drugs. Here, we identified two enzymes, β-hexosaminidases (HEXOs) that account for the formation of paucimannosidic N-glycans in Nicotiana benthamiana, a widely used expression host for recombinant proteins. Subcellular localization studies showed that HEXO1 is a vacuolar protein and HEXO3 is mainly located at the plasma membrane in N. benthamiana leaf epidermal cells. Both enzymes are functional and can complement the corresponding HEXO-deficient Arabidopsis thaliana mutants. In planta expression of HEXO3 demonstrated that core α1,3-fucose enhances the trimming of GlcNAc residues from the Fc domain of human IgG. Finally, using RNA interference, we show that suppression of HEXO3 expression can be applied to increase the amounts of complex N-glycans on plant-produced human α1-antitrypsin.

Indexed as

ArabidopsisBase Sequencebeta-N-AcetylhexosaminidasesCell MembraneGenes, PlantGlycosylationNicotianaPlant LeavesPlant ProteinsPlants, Genetically ModifiedPolysaccharidesRecombinant ProteinsVacuolesbeta-N-AcetylhexosaminidasesPlant ProteinsPolysaccharidesRecombinant Proteinsglyco-engineeringN-glycosylationNicotiana benthamianaplant-made pharmaceuticalsα1-antitrypsin

Identifiers

PMID27421111
PMCPMC5259580
OpenAlexW2464790038

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.