Evidence map›Paper›PMID 25004930›Full record

ArticleMolecular & cellular proteomics : MCP2014

Immunoglobulin G (IgG) Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes.

Albert Bondt, Yoann Rombouts, Maurice H J Selman, Paul J Hensbergen, Karli R Reiding, Johanna M W Hazes, Radboud J E M Dolhain, Manfred Wuhrer

Registry-linked trialOpen access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT03394092 (Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis), which is not on this map. Cited by 136 papers.

0numbers the graph read from it
0cells of the map it votes in
136citing papers in PubMed
15.0field-weighted citation impact, top 1% 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.

NCT03394092 completednot on this mapstarted 2018, after this paper: background citation

Changes in Glycopeptides of Serum Immunoglobulin G in Patients With Acute Myocardial Infarction and the Relationships Between Its Change and Prognosis

TypeobservationalSponsorThe First Affiliated Hospital of Dalian Medical UniversityRan2018 to 2019Enrolled100ConditionsAcute Coronary SyndromeArmsQuantitative measurements the changes of IgG glycosylation
3 · Its place in the literature

Who cites it

136 citing papers in PubMed, 258 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Immunoglobulin G in aging and cancer.Frontiers in immunology · 2026
    Review
  6. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
  7. Endothelial cells sialylate IgG within the FcRn-mediated recycling pathway.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Temporal and Sex-DependentInternational journal of molecular sciences · 2025
    Article
  14. Article
  15. Altered IgGBiomedicines · 2025
    Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article

76 more citing papers are in PubMed but not listed here.

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

8 authors at 3 institutions in 1 country.

Albert BondtFrom the ‡Department of Rheumatology, Erasmus University Medical Center, 3000 CA Rotterdam, The Netherlands; §Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;
Yoann Rombouts§Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands; ¶Department of Rheumatology, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;
Maurice H J Selman§Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;
Paul J Hensbergen§Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;
Karli R Reiding§Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands;
Johanna M W HazesFrom the ‡Department of Rheumatology, Erasmus University Medical Center, 3000 CA Rotterdam, The Netherlands;
Radboud J E M DolhainFrom the ‡Department of Rheumatology, Erasmus University Medical Center, 3000 CA Rotterdam, The Netherlands;
Manfred Wuhrer§Center for Proteomics and Metabolomics, Leiden University Medical Center, Albinusdreef 2, 2333 ZA Leiden, The Netherlands; ‖Division of BioAnalytical Chemistry, VU University Amsterdam, 1081 HV Amsterdam, The Netherlands; **Department of Molecular Cell Biology and Immunology, VU University Medical Center, 1007 MB Amsterdam, The Netherlands m.wuhrer@lumc.nl.
Leiden University Medical Center · NLErasmus MC · NLNetherlands Metabolomics Centre · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-linked glycosylation of the constant fragment (Fc) of immunoglobulin G has been shown to change during pathological and physiological events and to strongly influence antibody inflammatory properties. In contrast, little is known about Fab-linked N-glycosylation, carried by ∼ 20% of IgG. Here we present a high-throughput workflow to analyze Fab and Fc glycosylation of polyclonal IgG purified from 5 μl of serum. We were able to detect and quantify 37 different N-glycans by means of MALDI-TOF-MS analysis in reflectron positive mode using a novel linkage-specific derivatization of sialic acid. This method was applied to 174 samples of a pregnancy cohort to reveal Fab glycosylation features and their change with pregnancy. Data analysis revealed marked differences between Fab and Fc glycosylation, especially in the levels of galactosylation and sialylation, incidence of bisecting GlcNAc, and presence of high mannose structures, which were all higher in the Fab portion than the Fc, whereas Fc showed higher levels of fucosylation. Additionally, we observed several changes during pregnancy and after delivery. Fab N-glycan sialylation was increased and bisection was decreased relative to postpartum time points, and nearly complete galactosylation of Fab glycans was observed throughout. Fc glycosylation changes were similar to results described before, with increased galactosylation and sialylation and decreased bisection during pregnancy. We expect that the parallel analysis of IgG Fab and Fc, as set up in this paper, will be important for unraveling roles of these glycans in (auto)immunity, which may be mediated via recognition by human lectins or modulation of antigen binding.

Indexed as

FemaleGlycoproteinsGlycosylationHigh-Throughput Screening AssaysHumansImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GN-Acetylneuraminic AcidPolysaccharidesPostpartum PeriodPregnancySpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationGlycoproteinsglycosylated IgGImmunoglobulin Fab FragmentsImmunoglobulin Fc FragmentsImmunoglobulin GN-Acetylneuraminic AcidPolysaccharides

Identifiers

PMID25004930
PMCPMC4223489
OpenAlexW2146612842

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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.