Evidence map›Paper›PMID 22184099›Full record

Trial reportMolecular & cellular proteomics : MCP2012

Changes in antigen-specific IgG1 Fc N-glycosylation upon influenza and tetanus vaccination.

Maurice H J Selman, Sanne E de Jong, Darius Soonawala, Frank P Kroon, Ayola Akim Adegnika, André M Deelder, Cornelis H Hokke, Maria Yazdanbakhsh, Manfred Wuhrer

Open access · hybridAbstract readClinical TrialControlled Clinical Trial
In one paragraph

Trial report in Molecular & cellular proteomics : MCP, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

88 citing papers in PubMed, 142 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Immunomodulation of Antibody Glycosylation through the Placental Transfer.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Review

28 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

9 authors at 3 institutions in 3 countries.

Maurice H J SelmanDepartment of Parasitology, Leiden University Medical Center, Leiden, the Netherlands.
Sanne E de Jong
Darius Soonawala
Frank P Kroon
Ayola Akim Adegnika
André M Deelder
Cornelis H Hokke
Maria Yazdanbakhsh
Manfred Wuhrer
Leiden University · NLLeiden University Medical Center · NLAlbert Schweitzer Hospital · GA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antibody effector functions have been shown to be influenced by the structure of the Fc N-glycans. Here we studied the changes in plasma or serum IgG Fc N-glycosylation upon vaccination of 10 Caucasian adults and 10 African children. Serum/plasma IgG was purified by affinity chromatography prior to and at two time points after vaccination. Fc N-glycosylation profiles of individual IgG subclasses were determined for both total IgG and affinity-purified anti-vaccine IgG using a recently developed fast nanoliquid chromatography-electrospray ionization MS (LC-ESI-MS) method. While vaccination had no effect on the glycosylation of total IgG, anti-vaccine IgG showed increased levels of galactosylation and sialylation upon active immunization. Interestingly, the number of sialic acids per galactose increased during the vaccination time course, suggesting a distinct regulation of galactosylation and sialylation. In addition we observed a decrease in the level of IgG1 bisecting N-acetylglucosamine whereas no significant changes were observed for the level of fucosylation. Our data indicate that dependent on the vaccination time point the infectious agent will encounter IgGs with different glycosylation profiles, which are expected to influence the antibody effector functions relevant in immunity.

Indexed as

AdultAntigensAntigens, BacterialAntigens, ViralChildFemaleGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GInfluenza, HumanMaleMiddle AgedTetanusVaccinationAntigensAntigens, BacterialAntigens, ViralImmunoglobulin Fc FragmentsImmunoglobulin G

Identifiers

PMID22184099
PMCPMC3322571
OpenAlexW2136564498

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.