Evidence map›Paper›PMID 38827747›Full record

ArticleFrontiers in immunology2024

IgG sialylation occurs in B cells pre antibody secretion.

Anja Werner, Maja Hanić, Olga O Zaitseva, Gordan Lauc, Anja Lux, Lars Nitschke, Falk Nimmerjahn

Abstract read
In one paragraph

Article in Frontiers in immunology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. 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
  5. 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

7 authors.

Anja WernerDepartment of Biology, Division of Genetics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Maja HanićGenos Ltd, Glycoscience Research Laboratory, Zagreb, Croatia.
Olga O ZaitsevaGenos Ltd, Glycoscience Research Laboratory, Zagreb, Croatia.
Gordan LaucGenos Ltd, Glycoscience Research Laboratory, Zagreb, Croatia.
Anja LuxDepartment of Biology, Division of Genetics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Lars NitschkeDepartment of Biology, Division of Genetics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.
Falk NimmerjahnDepartment of Biology, Division of Genetics, Friedrich-Alexander-Universität Erlangen-Nürnberg, Erlangen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Sialic acids as terminal sugar residues on cell surface or secreted proteins have many functional roles. In particular, the presence or absence of α2,6-linked sialic acid residues at the immunoglobulin G (IgG) Fc fragment can switch IgG effector functions from pro- to anti-inflammatory activity. IgG glycosylation is considered to take place inside the plasma blast/plasma cell while the molecule travels through the endoplasmic reticulum and Golgi apparatus before being secreted. However, more recent studies have suggested that IgG sialylation may occur predominantly post-antibody secretion. To what extent this extracellular IgG sialylation process contributes to overall IgG sialylation remains unclear, however. By generating bone marrow chimeric mice with a B cell-specific deletion of ST6Gal1, the key enzyme required for IgG sialylation, we now show that sialylation of the IgG Fc fragment exclusively occurs within B cells pre-IgG secretion. We further demonstrate that B cells expressing ST6Gal1 have a developmental advantage over B cells lacking ST6Gal1 expression and thus dominate the plasma cell pool and the resulting serum IgG population in mouse models in which both ST6Gal1-sufficient and -deficient B cells are present.

Indexed as

B-LymphocytesImmunoglobulin GSialyltransferasesAnimalsAntibody Formationbeta-D-Galactoside alpha 2-6-SialyltransferaseGlycosylationImmunoglobulin Fc FragmentsMiceMice, Inbred C57BLMice, KnockoutPlasma Cellsbeta-D-Galactoside alpha 2-6-SialyltransferaseImmunoglobulin Fc FragmentsImmunoglobulin GSialyltransferasesautoantibodyB cellimmunoglobulin Gsialic acidsialylation

Identifiers

PMID38827747
PMCPMC11140079

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.