Evidence map›Paper›PMID 22966004›Full record

ArticleThe Journal of experimental medicine2012

Schistosome-derived omega-1 drives Th2 polarization by suppressing protein synthesis following internalization by the mannose receptor.

Bart Everts, Leonie Hussaarts, Nicole N Driessen, Moniek H J Meevissen, Gabriele Schramm, Alwin J van der Ham, Barbara van der Hoeven, Thomas Scholzen, Sven Burgdorf, Markus Mohrs and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of experimental medicine, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 153 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
153citing papers in PubMed, 1 pooled it
15.1field-weighted citation impact, top 1% 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

153 citing papers in PubMed, 1 synthesis or guideline pooled it, 231 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Chemical inhibition of α-mannosidase inFrontiers in parasitology · 2026
    Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Innate Immune Response to Helminth Infections.Advances in experimental medicine and biology · 2025
    Review
  15. Review
  16. Clinical & translational immunology · 2024
    Review
  17. Article
  18. Article
  19. Review
  20. High-mannose glycans fromFrontiers in immunology · 2024
    Article

93 more citing papers are in PubMed but not listed here.

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

15 authors at 4 institutions in 3 countries.

Bart EvertsDepartment of Parasitology, Leiden University Medical Center, 2333 ZA Leiden, Netherlands.
Leonie Hussaarts
Nicole N Driessen
Moniek H J Meevissen
Gabriele Schramm
Alwin J van der Ham
Barbara van der Hoeven
Thomas Scholzen
Sven Burgdorf
Markus Mohrs
Edward J Pearce
Cornelis H Hokke
Helmut Haas
Hermelijn H Smits
Maria Yazdanbakhsh
Leiden University Medical Center · NLResearch Center Borstel - Leibniz Lung Center · DETrudeau Institute · USWashington University in St. Louis · US

Funding

Dendritic Cell Function in SchistosomiasisR01AI053825 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI PEARCE, EDWARD J. · 2002 to 2010
$3.4M
NIAID NIH HHS AI53825NIAID NIH HHS R01 AI053825
6 · The paper itself

Abstract

Omega-1, a glycosylated T2 ribonuclease (RNase) secreted by Schistosoma mansoni eggs and abundantly present in soluble egg antigen, has recently been shown to condition dendritic cells (DCs) to prime Th2 responses. However, the molecular mechanisms underlying this effect remain unknown. We show in this study by site-directed mutagenesis of omega-1 that both the glycosylation and the RNase activity are essential to condition DCs for Th2 polarization. Mechanistically, we demonstrate that omega-1 is bound and internalized via its glycans by the mannose receptor (MR) and subsequently impairs protein synthesis by degrading both ribosomal and messenger RNA. These experiments reveal an unrecognized pathway involving MR and interference with protein synthesis that conditions DCs for Th2 priming.

Indexed as

Protein BiosynthesisAmino Acid SequenceAnimalsCell LineCells, CulturedDendritic CellsEndoribonucleasesGlycosylationHumansLectins, C-TypeMannose-Binding LectinsMannose ReceptorMiceMolecular Sequence DataOvumReceptors, Cell SurfaceEndoribonucleasesLectins, C-TypeMannose-Binding LectinsMannose ReceptorReceptors, Cell Surfaceribonuclease T(2)RNA, MessengerRNA, Ribosomal

Identifiers

PMID22966004
PMCPMC3457738
OpenAlexW2158574746

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.