Evidence map›Paper›PMID 26457892›Full record

ArticlePloS one2015

Comparison of Fc N-Glycosylation of Pharmaceutical Products of Intravenous Immunoglobulin G.

Willem Jan R Fokkink, David Falck, Tom C M Santbergen, Ruth Huizinga, Manfred Wuhrer, Bart C Jacobs

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. 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
1.4field-weighted citation impact, top 19% 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. Review
  2. Harnessing IgG Fc glycosylation for clinical benefit.Current opinion in immunology · 2022
    Review
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. IVIg-induced plasmablasts in patients with Guillain-Barré syndrome.Annals of clinical and translational neurology · 2019
    Article
  9. Review
  10. Article
  11. 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

6 authors at 2 institutions in 1 country.

Willem Jan R FokkinkDepartment of Immunology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands; Department of Neurology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands.
David FalckCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands.
Tom C M SantbergenDepartment of Immunology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands.
Ruth HuizingaDepartment of Immunology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands.
Manfred WuhrerCenter for Proteomics and Metabolomics, Leiden University Medical Center, Leiden, The Netherlands; Division of BioAnalytical Chemistry, Department of Chemistry and Pharmaceutical Sciences, Division of BioAnalytical Chemistry, VU University, Amsterdam, The Netherlands.
Bart C JacobsDepartment of Immunology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands; Department of Neurology, Erasmus MC, University Medical Center Rotterdam, Rotterdam, The Netherlands.
Erasmus MC · NLLeiden University Medical Center · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intravenous immunoglobulin (IVIg) products from different pharmaceutical companies vary in composition, in part because of the selected blood donors and production process. N-glycosylation of the Fc-portion of IgG varies between blood donors and may influence both the side-effects and therapeutic effectiveness of IVIg. At present, the variation in Fc N-glycosylation between IVIg products has not been defined. Utilizing mass spectrometry, we performed relative quantitation of the Fc N-glycosylation of IgG, assessing a total of 154 unique lot numbers of IVIg. Seven products showed comparable Fc N-glycosylation, with only one product differing from the others in all glycosylation features (galactosylation, sialylation, fucosylation and bisecting N-acetylglucosamine). However, the mean difference did not exceed 3%. Within product variation was present to a minor degree, but largely indistinguishable from analytical variation. In conclusion, we expect that the minor variation in Fc N-glycosylation between IVIg products has a small effect, if any, on the biological activity.

Indexed as

FemaleGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulins, IntravenousMaleImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulins, Intravenous

Identifiers

PMID26457892
PMCPMC4601728
OpenAlexW2258228646

What OpenQuestion holds

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LicenceCC BY
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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.