Evidence map›Paper›PMID 26618514›Full record

ArticleClinical and experimental immunology2016

Sialylation of anti-histone immunoglobulin G autoantibodies determines their capabilities to participate in the clearance of late apoptotic cells.

I Magorivska, L E Muñoz, C Janko, T Dumych, J Rech, G Schett, F Nimmerjahn, R Bilyy, M Herrmann

Open access · greenAbstract read
In one paragraph

Article in Clinical and experimental immunology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.8field-weighted citation impact, top 15% 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

15 citing papers in PubMed, 33 citations in OpenAlex.

  1. IgG N-glycosylation in autoimmune diseases.Frontiers in immunology · 2026
    Review
  2. Article
  3. Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Recombinant Proteins and Monoclonal Antibodies.Advances in biochemical engineering/biotechnology · 2021
    Review
  9. Glycosylation in Autoimmune Diseases.Advances in experimental medicine and biology · 2021
    Article
  10. Immunoglobulin G Glycosylation in Diseases.Experientia supplementum (2012) · 2021
    Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. 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

9 authors at 2 institutions in 2 countries.

I MagorivskaDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
L E MuñozDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
C JankoDepartment of Otorhinolaryngology, Head and Neck Surgery, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
T DumychInstitute of Cell Biology, National Academy of Sciences of Ukraine, Lviv, Ukraine.
J RechDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
G SchettDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
F NimmerjahnChair of Genetic, Department of Biology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
R BilyyDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
M HerrmannDepartment of Internal Medicine 3 Rheumatology and Immunology, Friedrich-Alexander University Erlangen-Nürnberg, Erlangen, Germany.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DEInstitute of Cell Biology · UA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Fc portion of immunoglobulin (Ig)G harbours a single glycosylation site. Glycan sialylation is critical for structure and for certain effector functions of IgG. Anti-histone IgG of patients with systemic lupus erythematosus is reportedly responsible for the recruitment of polymorphonuclear cells (PMN) to the clearance of apoptotic cells. Autoantibodies decorating secondary necrotic cells (SNEC) induce proinflammatory responses after activation of blood-borne phagocytes. Analysing the sialylation status of affinity-purified anti-histone IgG in patients with systemic lupus erythematosus (SLE), we demonstrated that the anti-histone IgG was contained preferentially in the non-sialylated fraction. In functional ex-vivo phagocytosis studies, non-sialylated anti-SNEC IgG directed SNEC preferentially into PMN but did not change their cytokine secretion profiles. In contrast, sialylated IgG reduced the phagocytosis by monocytes of SNEC. Moreover, the sialylated anti-SNEC IgG was not simply anti-inflammatory, but switched the cytokine secretion profiles from interleukin (IL)-6/IL-8 to tumour necrosis factor (TNF)-α/IL-1β. Here we describe how different sialylation statuses of IgG autoantibodies contribute to the complex inflammatory network that regulates chronic inflammation.

Indexed as

PhagocytosisAdultAgedAged, 80 and overApoptosisAutoantibodiesCase-Control StudiesGene Expression RegulationGlycosylationHistonesHumansImmunoglobulin Fc FragmentsImmunoglobulin GInterleukin-1betaInterleukin-6Interleukin-8AutoantibodiesHistonesIL6 protein, humanImmunoglobulin Fc FragmentsImmunoglobulin GInterleukin-1betaInterleukin-6Interleukin-8Sialic AcidsTumor Necrosis Factor-alphaautoantibodiesIgGlectinsialylationSLE

Identifiers

PMID26618514
PMCPMC4778101
OpenAlexW2189323649

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.