Evidence map›Paper›PMID 26868756›Full record

ArticlePlant biotechnology journal2016

The production of human glucocerebrosidase in glyco-engineered Nicotiana benthamiana plants.

Juthamard Limkul, Sayoko Iizuka, Yohei Sato, Ryo Misaki, Takao Ohashi, Toya Ohashi, Kazuhito Fujiyama

Open access · goldAbstract read
In one paragraph

Article in Plant biotechnology journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.5field-weighted citation impact, top 4% 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

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
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  3. Review
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  8. Review
  9. Analysis ofPlant biotechnology (Tokyo, Japan) · 2021
    Article
  10. Review
  11. Article
  12. Inactivation ofFrontiers in plant science · 2021
    Article
  13. Glyco-Engineering of Plant-Based Expression Systems.Advances in biochemical engineering/biotechnology · 2021
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The Production of Human β-Glucocerebrosidase inInternational journal of molecular sciences · 2018
    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

7 authors at 3 institutions in 1 country.

Juthamard LimkulInternational Center for Biotechnology, Osaka University, Suita-shi, Osaka, Japan.
Sayoko IizukaDivision of Gene Therapy, Research Center for Medical Sciences, The Jikei University School of Medicine, Minato-ku, Tokyo, Japan.
Yohei SatoDivision of Gene Therapy, Research Center for Medical Sciences, The Jikei University School of Medicine, Minato-ku, Tokyo, Japan.
Ryo MisakiInternational Center for Biotechnology, Osaka University, Suita-shi, Osaka, Japan.
Takao OhashiInternational Center for Biotechnology, Osaka University, Suita-shi, Osaka, Japan.
Toya OhashiDivision of Gene Therapy, Research Center for Medical Sciences, The Jikei University School of Medicine, Minato-ku, Tokyo, Japan.
Kazuhito FujiyamaInternational Center for Biotechnology, Osaka University, Suita-shi, Osaka, Japan.
Jikei University School of Medicine · JPOsaka International University · JPOsaka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

For the production of therapeutic proteins in plants, the presence of β1,2-xylose and core α1,3-fucose on plants' N-glycan structures has been debated for their antigenic activity. In this study, RNA interference (RNAi) technology was used to down-regulate the endogenous N-acetylglucosaminyltransferase I (GNTI) expression in Nicotiana benthamiana. One glyco-engineered line (NbGNTI-RNAi) showed a strong reduction of plant-specific N-glycans, with the result that as much as 90.9% of the total N-glycans were of high-mannose type. Therefore, this NbGNTI-RNAi would be a promising system for the production of therapeutic glycoproteins in plants. The NbGNTI-RNAi plant was cross-pollinated with transgenic N. benthamiana expressing human glucocerebrosidase (GC). The recombinant GC, which has been used for enzyme replacement therapy in patients with Gaucher's disease, requires terminal mannose for its therapeutic efficacy. The N-glycan structures that were presented on all of the four occupied N-glycosylation sites of recombinant GC in NbGNTI-RNAi plants (GC(gnt1) ) showed that the majority (ranging from 73.3% up to 85.5%) of the N-glycans had mannose-type structures lacking potential immunogenic β1,2-xylose and α1,3-fucose epitopes. Moreover, GC(gnt1) could be taken up into the macrophage cells via mannose receptors, and distributed and taken up into the liver and spleen, the target organs in the treatment of Gaucher's disease. Notably, the NbGNTI-RNAi line, producing GC, was stable and the NbGNTI-RNAi plants were viable and did not show any obvious phenotype. Therefore, it would provide a robust tool for the production of GC with customized N-glycan structures.

Indexed as

AnimalsGlucosylceramidaseGlycosylationHumansLectins, C-TypeMacrophagesMannose-Binding LectinsMannose ReceptorMice, Inbred C57BLN-AcetylglucosaminyltransferasesNicotianaPlants, Genetically ModifiedPollinationPolysaccharidesReceptors, Cell SurfaceRecombinant Proteinsalpha-1,3-mannosyl-glycoprotein beta-1,2-N-acetylglucosaminyltransferase IGlucosylceramidaseLectins, C-TypeMannose-Binding LectinsMannose ReceptorN-AcetylglucosaminyltransferasesPolysaccharidesReceptors, Cell SurfaceRecombinant Proteinsglyco-engineered planthuman glucocerebrosidaseN-acetylglucosaminyltransferase INicotiana benthamianaplant-made pharmaceuticals

Identifiers

PMID26868756
PMCPMC5067671
OpenAlexW2336833988

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.