Evidence map›Paper›PMID 27492264›Full record

ArticlemAbs

The immunoglobulin G1 N-glycan composition affects binding to each low affinity Fc γ receptor.

Ganesh P Subedi, Adam W Barb

Open access · goldAbstract read
In one paragraph

Article in mAbs. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 105 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed, 2 pooled it
18.2field-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.

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

105 citing papers in PubMed, 2 syntheses or guidelines pooled it, 174 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Trial
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Antibody glycosylation in neuroimmune diseases.Journal of translational medicine · 2025
    Review
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Automated Assignment ofJournal of the American Society for Mass Spectrometry · 2024
    Article
  17. Article
  18. Review
  19. Article
  20. Article

45 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

2 authors at 1 institution in 1 country.

Ganesh P Subedia Roy J. Carver Department of Biochemistry , Biophysics and Molecular Biology, Iowa State University , Ames , IA , USA.
Adam W Barba Roy J. Carver Department of Biochemistry , Biophysics and Molecular Biology, Iowa State University , Ames , IA , USA.
Iowa State University · US

Funding

Mechanism and engineering of IgG-based monoclonal antibody/receptor interactionsR01GM115489 · NIGMS · UNIVERSITY OF GEORGIA · PI BARB, ADAM WESLEY · 2015 to 2019
$1.4M
NIGMS NIH HHS R01 GM115489
6 · The paper itself

Abstract

Immunoglobulin G1 (IgG1) is the most abundant circulating human antibody and also the scaffold for many therapeutic monoclonal antibodies (mAbs). The destruction of IgG-coated targets by cell-mediated pathways begins with an interaction between the IgG Fc region and multiple varieties of membrane-bound Fc γ receptors (FcγRs) on the surface of leukocytes. This interaction requires the presence of an asparagine-linked (N-)glycan on the Fc, and variations in the N-glycan composition can affect the affinity of CD16A binding (an FcγR). Contemporary efforts to glycoengineer mAbs focus on increasing CD16A affinity, and thus treatment efficacy, but it is unclear how these changes affect affinity for the other FcγRs. Here, we measure binding of the extracellular Fc-binding domains for human CD16A and B, CD32A, B and C, and CD64 to 6 well-defined IgG1 Fc glycoforms that cover ∼85% of the pool of human IgG1 Fc glycoforms. Core α1-6 fucosylation showed the greatest changes with CD16B (8.5-fold decrease), CD16A (3.9-fold decrease) and CD32B/C (1.8-fold decrease), but did not affect binding to CD32A. Adding galactose to the non-reducing termini of the complex-type, biantennary glycan increased affinity for all CD16s and 32s tested by 1.7-fold. Sialylation did not change the affinity of core-fucosylated Fc, but increased the affinity of afucosylated Fc slightly by an average of 1.16-fold for all CD16s and CD32s tested. The effects of fucose and galactose modification are additive, suggesting the contributions of these residues to Fc γ receptor affinity are independent.

Indexed as

AnimalsAntibody AffinityHumansImmunoglobulin GPolysaccharidesReceptors, IgGImmunoglobulin GPolysaccharidesReceptors, IgGCD16CD32CD64FcγRIFcγRIIFcγRIIIN-glycosylation

Identifiers

PMID27492264
PMCPMC5098437
OpenAlexW2478409189

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.