Evidence map›Paper›PMID 31998308›Full record

ArticleFrontiers in immunology2019

Minimal B Cell Extrinsic IgG Glycan Modifications of Pro- and Anti-Inflammatory IgG Preparations

Anja Schaffert, Maja Hanić, Mislav Novokmet, Olga Zaytseva, Jasminka Krištić, Anja Lux, Lars Nitschke, Matthias Peipp, Marija Pezer, René Hennig and 3 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.4field-weighted citation impact, top 9% 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

20 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. 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
  3. Role of Antibody Glycosylation in Health, Disease, and Therapy.Handbook of experimental pharmacology · 2025
    Review
  4. Article
  5. Article
  6. Antigen specificity shapes antibody functions in tuberculosis.bioRxiv : the preprint server for biology · 2024
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Review
  13. Molecules (Basel, Switzerland) · 2022
    Article
  14. Review
  15. Review
  16. Sweet Rules: Linking Glycosylation to Antibody Function.Experientia supplementum (2012) · 2021
    Review
  17. Article
  18. Article
  19. Glycosylation and Aging.Advances in experimental medicine and biology · 2021
    Article
  20. 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

13 authors at 5 institutions in 3 countries.

Anja SchaffertDepartment of Biology, Institute of Genetics, University of Erlangen-Nuremberg, Erlangen, Germany.
Maja HanićGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
Mislav NovokmetGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
Olga ZaytsevaGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
Jasminka KrištićGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
Anja LuxDepartment of Biology, Institute of Genetics, University of Erlangen-Nuremberg, Erlangen, Germany.
Lars NitschkeDepartment of Biology, Institute of Genetics, University of Erlangen-Nuremberg, Erlangen, Germany.
Matthias PeippDepartment of Medicine II, Christian-Albrechts University Kiel and University Medical Center Schleswig-Holstein, Kiel, Germany.
Marija PezerGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
René HennigglyXera GmbH, Magdeburg, Germany.
Erdmann RappglyXera GmbH, Magdeburg, Germany.
Gordan LaucGlycoscience Research Laboratory, Genos Ltd., Zagreb, Croatia.
Falk NimmerjahnDepartment of Biology, Institute of Genetics, University of Erlangen-Nuremberg, Erlangen, Germany.
Science Research Laboratory · USFriedrich-Alexander-Universität Erlangen-Nürnberg · DEMax Planck Institute for Dynamics of Complex Technical Systems · DEGenos (Croatia) · HRKiel University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Select residues in the biantennary sugar moiety attached to the fragment crystallizable of immunoglobulin G (IgG) antibodies can modulate IgG effector functions. Thus, afucosylated IgG glycovariants have enhanced cytotoxic activity, whereas IgG glycovariants rich in terminal sialic acid residues can trigger anti-inflammatory effects. More recent evidence suggests that terminal α2,6 linked sialic acids can be attached to antibodies post IgG secretion. These findings raise concerns for the use of therapeutic antibodies as they may change their glycosylation status in the patient and hence affect their activity. To investigate to what extent B cell extrinsic sialylation processes modify therapeutic IgG preparations

Indexed as

AnimalsB-LymphocytesGlycosylationHumansImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulins, IntravenousInflammationMiceMice, Inbred C57BLPolysaccharidesSialic AcidsImmunoglobulin Fc FragmentsImmunoglobulin GImmunoglobulins, IntravenousPolysaccharidesSialic AcidsantibodyB cellsglycosylationIgGIVIgsialylation

Identifiers

PMID31998308
PMCPMC6970187
OpenAlexW2998940295

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.