Evidence map›Paper›PMID 35154135›Full record

ArticleFrontiers in immunology2022

Enhanced Immunomodulatory Effect of Intravenous Immunoglobulin by Fc Galactosylation and Nonfucosylation.

Yusuke Mimura, Yuka Mimura-Kimura, Radka Saldova, Pauline M Rudd, Roy Jefferis

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in Frontiers in immunology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

19 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. 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
  4. Exploring glycoform-dependent dynamic modulations in human immunoglobulin G via computational and experimental approaches.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Serum immunoglobulin and the threshold of Fc receptor-mediated immune activation.Biochimica et biophysica acta. General subjects · 2023
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Extracellular vesicles ofFrontiers in immunology · 2023
    Article
  17. Article
  18. Article
  19. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 4 institutions in 4 countries.

Yusuke MimuraDepartment of Clinical Research, National Hospital Organization Yamaguchi Ube Medical Center, Ube, Japan.
Yuka Mimura-KimuraDepartment of Clinical Research, National Hospital Organization Yamaguchi Ube Medical Center, Ube, Japan.
Radka SaldovaNIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Dublin, Ireland.
Pauline M RuddNIBRT GlycoScience Group, National Institute for Bioprocessing Research and Training, Dublin, Ireland.
Roy JefferisInstitute of Immunology and Immunotherapy, College of Medical and Dental Sciences, University of Birmingham, Birmingham, United Kingdom.
National Sanyo Hospital · JPAgency for Science, Technology and Research · SGNational Institute for Bioprocessing Research and Training · IEUniversity of Birmingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Intravenous immunoglobulin (IVIG) is used as an immunomodulatory agent in the treatment of various autoimmune/inflammatory diseases although its mechanism of action remains elusive. Recently, nonfucosylated IgG has been shown to be preferentially bound to Fcγ receptor IIIa (FcγRIIIa) on circulating natural killer cells; therefore, we hypothesized that nonfucosylated IVIG may modulate immune responses through FcγRIIIa blockade. Here, homogeneous fucosylated or nonfucosylated glycoforms of normal polyclonal IgG bearing sialylated, galactosylated or nongalactosylated Fc oligosaccharides were generated by chemoenzymatic glycoengineering to investigate whether the IgG glycoforms can inhibit antibody-dependent cellular cytotoxicity (ADCC). Among the six IgG glycoforms, galactosylated, nonfucosylated IgG [(G2)

Indexed as

AnimalsAntibody-Dependent Cell CytotoxicityArthritisFucoseGlycosylationHumansImmunoglobulins, IntravenousMicePilot ProjectsReceptors, IgGRituximabFCGR3A protein, humanFucoseImmunoglobulins, IntravenousReceptors, IgGRituximabantibody-dependent cellular cytotoxicityautoimmune diseaseFcγ receptorglycoengineeringintravenous immunoglobulinnatural killer celloligosaccharide

Identifiers

PMID35154135
PMCPMC8831331
OpenAlexW4210522976

What OpenQuestion 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 OpenQuestion graph.