Evidence map›Paper›PMID 37421619›Full record

ArticleCell reports2023

Mixed IgG Fc immune complexes exhibit blended binding profiles and refine FcR affinity estimates.

Zhixin Cyrillus Tan, Anja Lux, Markus Biburger, Prabha Varghese, Stephen Lees, Falk Nimmerjahn, Aaron S Meyer

Abstract read
In one paragraph

Article in Cell reports, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
–field-weighted citation impact
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

10 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  8. Review
  9. Article
  10. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Zhixin Cyrillus TanBioinformatics Interdepartmental Program, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA.
Anja LuxDivision of Genetics, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Markus BiburgerDivision of Genetics, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Prabha VargheseDivision of Genetics, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Stephen LeesDepartment of Bioengineering, UCLA, Los Angeles, CA 90095, USA.
Falk NimmerjahnDivision of Genetics, Department of Biology, Friedrich-Alexander-Universität Erlangen-Nürnberg, 91058 Erlangen, Germany.
Aaron S MeyerBioinformatics Interdepartmental Program, University of California, Los Angeles (UCLA), Los Angeles, CA 90095, USA; Department of Bioengineering, UCLA, Los Angeles, CA 90095, USA; Jonsson Comprehensive Cancer Center, UCLA, Los Angeles, CA 90095, USA; Eli and Edythe Broad Center of Regenerative Medicine and Stem Cell Research, UCLA, Los Angeles, CA 90095, USA. Electronic address: ameyer@asmlab.org.

Funding

Mapping the effector response space of antibody combinationsU01AI148119 · NIAID · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI MEYER, AARON SAMUEL, NIMMERJAHN, FALK · 2020 to 2024
$1.6M
NIAID NIH HHS U01 AI148119
6 · The paper itself

Abstract

Immunoglobulin G (IgG) antibodies coordinate immune effector responses by interacting with effector cells via fragment crystallizable γ (Fcγ) receptors. The IgG Fc domain directs effector responses through subclass and glycosylation variation. Although each Fc variant has been extensively characterized in isolation, during immune responses, IgG is almost always produced in Fc mixtures. How this influences effector responses has not been examined. Here, we measure Fcγ receptor binding to mixed Fc immune complexes. Binding of these mixtures falls along a continuum between pure cases and quantitatively matches a mechanistic model, except for several low-affinity interactions mostly involving IgG2. We find that the binding model provides refined estimates of their affinities. Finally, we demonstrate that the model predicts effector cell-elicited platelet depletion in humanized mice. Contrary to previous views, IgG2 exhibits appreciable binding through avidity, though it is insufficient to induce effector responses. Overall, this work demonstrates a quantitative framework for modeling mixed IgG Fc-effector cell regulation.

Indexed as

Antigen-Antibody ComplexReceptors, IgGAnimalsGlycosylationImmunoglobulin Fc FragmentsImmunoglobulin GMiceReceptors, FcAntigen-Antibody ComplexImmunoglobulin Fc FragmentsImmunoglobulin GReceptors, FcReceptors, IgGaffinityantibodiesavidityCP: Immunologyeffector functionFcγimmunologyreceptors

Identifiers

PMID37421619
PMCPMC10404157

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.