Evidence map›Paper›PMID 21372247›Full record

ArticleMolecular & cellular proteomics : MCP2011

Targeted glycoproteomic analysis reveals that kappa-5 is a major, uniquely glycosylated component of Schistosoma mansoni egg antigens.

Moniek H J Meevissen, Crina I A Balog, Carolien A M Koeleman, Michael J Doenhoff, Gabriele Schramm, Helmut Haas, André M Deelder, Manfred Wuhrer, Cornelis H Hokke

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

26 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
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  4. Article
  5. Article
  6. Review
  7. Schistosome immunomodulators.PLoS pathogens · 2021
    Review
  8. β-Hexosaminidases Along the Secretory Pathway ofFrontiers in plant science · 2021
    Article
  9. Article
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  11. Article
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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 3 institutions in 3 countries.

Moniek H J MeevissenDepartment of Parasitology, Leiden University Medical Center, 2333 ZA Leiden, the Netherlands.
Crina I A Balog
Carolien A M Koeleman
Michael J Doenhoff
Gabriele Schramm
Helmut Haas
André M Deelder
Manfred Wuhrer
Cornelis H Hokke
Leiden University Medical Center · NLResearch Center Borstel - Leibniz Lung Center · DEUniversity of Nottingham · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycans present on glycoproteins from the eggs of the parasite Schistosoma mansoni are mediators of various immune responses of the human host, including T-cell modulation and granuloma formation, and they are the target of glycan-specific antibodies. Here we have analyzed the glycosylation of kappa-5, a major glycoprotein antigen from S. mansoni eggs using a targeted approach of lectin purification followed by mass spectrometry of glycopeptides as well as released glycans. We demonstrate that kappa-5 has four fully occupied N-glycosylation sites carrying unique triantennary glycans composed of a difucosylated and xylosylated core region, and immunogenic GalNAcβ1-4GlcNAc (LDN) termini. Furthermore, we show that the kappa-5 specific IgE antibodies in sera of S. mansoni-infected individuals are directed against the core region of the kappa-5 glycans. Whereas two previously analyzed immunomodulatory egg glycoproteins, IPSE/alpha-1 and omega-1, both express diantennary N-glycans with a difucosylated core and one or two Galβ1-4(Fucα1-3)GlcNAc (Lewis X) antennae, the kappa-5 glycosylation appears unique among the major soluble egg antigens of S. mansoni. The distinct structural and antigenic properties of kappa-5 glycans suggest a specific role for kappa-5 in schistosome egg immunogenicity.

Indexed as

Amino Acid MotifsAnimalsAntibodies, HelminthAntigens, HelminthEgg ProteinsGlycoproteinsGlycoside HydrolasesGlycosylationHelminth ProteinsHost-Parasite InteractionsHumansImmunoglobulin ELactosePeptide FragmentsPolysaccharidesSchistosoma mansoniAntibodies, HelminthAntigens, HelminthEgg ProteinsGlycoproteinsGlycoside HydrolasesHelminth ProteinsImmunoglobulin ELactoseN-acetylgalactosaminyl-1-4-N-acetylglucosaminePeptide FragmentsPolysaccharides

Identifiers

PMID21372247
PMCPMC3098592
OpenAlexW2115270104

What OpenQuestion holds

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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.