Evidence map›Paper›PMID 25740940›Full record

ArticleGlycobiology2015

Two types of galactosylated fucose motifs are present on N-glycans of Haemonchus contortus.

Katharina Paschinger, Iain B H Wilson

Open access · bronzeAbstract read
In one paragraph

Article in Glycobiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
3.7field-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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Review
  6. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  7. Article
  8. Review
  9. N-glycome and N-glycoproteome of a hematophagous parasitic nematodeComputational and structural biotechnology journal · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019
    Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Analysis of Invertebrate and Protist N-Glycans.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Katharina PaschingerDepartment für Chemie, Universität für Bodenkultur Wien, Wien 1190, Austria.
Iain B H WilsonDepartment für Chemie, Universität für Bodenkultur Wien, Wien 1190, Austria iain.wilson@boku.ac.at.
BOKU University · AT

Funding

Austrian Science Fund FWF P 21946Austrian Science Fund FWF P 23922
6 · The paper itself

Abstract

N-Glycans from the nematode Haemonchus contortus (barber pole worm), a parasite of sheep and cattle, were the first to be described to possess up to three fucose residues associated with the N,N'-diacetylchitobiosyl core, two being on the reducing-terminal proximal GlcNAc and one on the distal core GlcNAc residue. The assumption was that truncated glycans from this organism with three hexose residues have the composition Man3GlcNAc2Fuc1-3. In this study, we have performed HPLC and MALDI-TOF MS/MS in combination with selected digestions of N-glycans from Haemonchus. A dominant trifucosylated Hex3HexNAc2Fuc3 glycan was modified not only with α1,6-fucose but also with a proximal core α1,3-fucose and a galactosylated distal α1,3-fucose; thereby, only two of the hexose residues were mannose. Other N-glycans displayed galactosylation of the core α1,6-fucose, antennal fucosylation or modification with phosphorylcholine. Thus, the N-glycans of Haemonchus contain a number of potentially immunogenic glycan epitopes also found in other parasites and our proposed structures are in line with the previously defined specificity of nematode glycosyltransferases as we show that distal fucosylation and the presence of an α1,6-mannose are apparently mutually exclusive. These data are thereby of importance for engineering cell lines capable of mimicking Haemonchus-type N-glycans in the preparation of recombinant proteins as vaccine candidates.

Indexed as

AnimalsChromatography, High Pressure LiquidFucoseGalactoseGlycosylationHaemonchusPolysaccharidesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryFucoseGalactosePolysaccharidesmass spectrometrynematodeoligosaccharide

Identifiers

PMID25740940
PMCPMC4414472
OpenAlexW2142054120

What OpenQuestion holds

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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.