Evidence map›Paper›PMID 24753388›Full record

ArticleBiotechnology journal2014

Minimizing fucosylation in insect cell-derived glycoproteins reduces binding to IgE antibodies from the sera of patients with allergy.

Dieter Palmberger, Kazem Ashjaei, Stephanie Strell, Karin Hoffmann-Sommergruber, Reingard Grabherr

Open access · greenAbstract read
In one paragraph

Article in Biotechnology journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.4field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 24 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  5. Review
  6. Article
  7. Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021
    Article
  8. Cell-Free Glycoengineering of the Recombinant SARS-CoV-2 Spike Glycoprotein.Frontiers in bioengineering and biotechnology · 2021
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Humanizing glycosylation pathways in eukaryotic expression systems.World journal of microbiology & biotechnology · 2017
    Review
  14. Review
  15. Article
  16. Advances in the development of influenza virus vaccines.Nature reviews. Drug discovery · 2015
    Review
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

5 authors at 2 institutions in 1 country.

Dieter PalmbergerVienna Institute of BioTechnology - VIBT, University of Natural Resources and Life Sciences, Vienna, Austria.
Kazem Ashjaei
Stephanie Strell
Karin Hoffmann-Sommergruber
Reingard Grabherr
BOKU University · ATMedical University of Vienna · AT

Funding

Austrian Science Fund FWF F 4603Austrian Science Fund FWF P 25092
6 · The paper itself

Abstract

The baculovirus/insect cell system has proven to be a very powerful tool for the expression of several therapeutics. Nevertheless, these products sometimes suffer from reduced biological activity and unwanted side effects. Several studies have demonstrated that glycosylation can greatly influence the structure, function, half-life, antigenicity and immunogenicity of various glycoproteins. Yet, the glycosylation pattern of insect cell-derived products is not favorable for many applications. Especially, the presence of core α1,3-linked fucose bears the risk of causing immediate hypersensitivity reactions in patients with allergy. In this study, we evaluated the impact of fucose residues on the allergenic potential of an insect cell-expressed vaccine candidate. In order to block the GDP-L-fucose de novo synthesis pathway, we integrated the Pseudomonas aeruginosa GDP-6-deoxy-D-lyxo-4-hexulose reductase (RMD) gene into a baculovirus backbone. This virus was then used for the expression of soluble influenza A virus hemagglutinin (HA). Expression studies showed that the co-expression of RMD did not influence the overall level of recombinant protein secretion. We confirmed the result of our strategy by analyzing PNGase A-released N-glycans using MALDI-TOF-MS. In order to evaluate the biological impact of defucosylation of influenza HA we tested the binding activity of IgE derived from the sera of patients with allergy to the purified antigen. The non-fucosylated HA showed a 10-fold decrease in IgE binding levels as compared to wildtype variants.

Indexed as

AnimalsAntibodiesAntigensBacterial ProteinsBaculoviridaeFucoseGlycoproteinsGlycosylationHemagglutininsHumansHypersensitivityImmune SeraImmunoglobulin EInfluenza A virusInfluenza VaccinesInsectaAntibodiesAntigensBacterial ProteinsFucoseGDP-6-deoxy-D-lyxo-4-hexulose reductaseGlycoproteinsHemagglutininsImmune SeraImmunoglobulin EInfluenza VaccinesOxidoreductases Acting on Aldehyde or Oxo Group DonorsRecombinant ProteinsBaculovirusFucoseGlycosylationInsect cellsVaccines

Identifiers

PMID24753388
PMCPMC4739504
OpenAlexW2004010477

What OpenQuestion holds

Textmetadata
LicenceTDM
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.