Evidence map›Paper›PMID 28332009›Full record

ArticleTransgenic research2017

N-Glycosylation of an IgG antibody secreted by Nicotiana tabacum BY-2 cells can be modulated through co-expression of human β-1,4-galactosyltransferase.

Catherine Navarre, Nicolas Smargiasso, Laurent Duvivier, Joseph Nader, Johann Far, Edwin De Pauw, Marc Boutry

Abstract read
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In one paragraph

Article in Transgenic research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Plant-Based Systems for Producing Therapeutic Proteins: Current Status and Future Prospects.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
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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 2 institutions in 1 country.

Catherine NavarreInstitut des Sciences de la Vie, Université catholique de Louvain, 1348, Louvain-la-Neuve, Belgium. catherine.navarre@uclouvain.be.ORCID 0000-0002-8413-0878
Nicolas SmargiassoMass Spectrometry Laboratory, University of Liege, 4000, Liège, Belgium.
Laurent DuvivierInstitut des Sciences de la Vie, Université catholique de Louvain, 1348, Louvain-la-Neuve, Belgium.
Joseph NaderInstitut des Sciences de la Vie, Université catholique de Louvain, 1348, Louvain-la-Neuve, Belgium.
Johann FarMass Spectrometry Laboratory, University of Liege, 4000, Liège, Belgium.
Edwin De PauwMass Spectrometry Laboratory, University of Liege, 4000, Liège, Belgium.
Marc BoutryInstitut des Sciences de la Vie, Université catholique de Louvain, 1348, Louvain-la-Neuve, Belgium.
UCLouvain · BEUniversity of Liège · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nicotiana tabacum BY-2 suspension cells have several advantages that make them suitable for the production of full-size monoclonal antibodies which can be purified directly from the culture medium. Carbohydrate characterization of an antibody (Lo-BM2) expressed in N. tabacum BY-2 cells showed that the purified Lo-BM2 displays N-glycan homogeneity with a high proportion (>70%) of the complex GnGnXF glycoform. The stable co-expression of a human β-1,4-galactosyltransferase targeted to different Golgi sub-compartments altered Lo-BM2N-glycosylation and resulted in the production of an antibody that exhibited either hybrid structures containing a low abundance of the plant epitopes (α-1,3-fucose and β-1,2-xylose), or a large amount of galactose-extended N-glycan structures. These results demonstrate the suitability of stable N-glycoengineered N. tabacum BY-2 cell lines for the production of human-like antibodies.

Indexed as

Chromatography, AffinityGene Expression RegulationGlycosylationGolgi ApparatusHumansImmunoglobulin GN-Acetyllactosamine SynthaseNicotianaPlants, Genetically ModifiedRecombinant ProteinsImmunoglobulin GN-Acetyllactosamine SynthaseRecombinant ProteinsAntibodyN-GlycosylationPlant suspension cellsβ-1,4-Galactosyltransferase

Identifiers

PMID28332009
OpenAlexW2598317583

What OpenQuestion holds

Textmetadata
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.