Evidence map›Paper›PMID 22733825›Full record

ArticleThe Journal of biological chemistry2012

Galactosylated fucose epitopes in nematodes: increased expression in a Caenorhabditis mutant associated with altered lectin sensitivity and occurrence in parasitic species.

Shi Yan, Silvia Bleuler-Martinez, David Fernando Plaza, Markus Künzler, Markus Aebi, Anja Joachim, Ebrahim Razzazi-Fazeli, Verena Jantsch, Rudolf Geyer, Iain B H Wilson and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

28 citing papers in PubMed, 54 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Towards understanding the extensive diversity of protein N-glycan structures in eukaryotes.Biological reviews of the Cambridge Philosophical Society · 2022
    Review
  5. Nanoparticles To Study Lectins inBiomacromolecules · 2021
    Article
  6. Review
  7. N-glycomic Complexity in Anatomical Simplicity:Frontiers in molecular biosciences · 2019
    Review
  8. Article
  9. The Journal of biological chemistry · 2017
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Review
  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

11 authors at 5 institutions in 3 countries.

Shi YanDepartment für Chemie, Universität für Bodenkultur, A-1190 Wien, Austria.
Silvia Bleuler-Martinez
David Fernando Plaza
Markus Künzler
Markus Aebi
Anja Joachim
Ebrahim Razzazi-Fazeli
Verena Jantsch
Rudolf Geyer
Iain B H Wilson
Katharina Paschinger
ETH Zurich · CHBOKU University · ATUniversity of Veterinary Medicine Vienna · ATMax Perutz Labs · ATUniversity of Giessen · DE

Funding

Austrian Science Fund FWF P 21946
6 · The paper itself

Abstract

The modification of α1,6-linked fucose residues attached to the proximal (reducing-terminal) core N-acetylglucosamine residue of N-glycans by β1,4-linked galactose ("GalFuc" epitope) is a feature of a number of invertebrate species including the model nematode Caenorhabditis elegans. A pre-requisite for both core α1,6-fucosylation and β1,4-galactosylation is the presence of a nonreducing terminal N-acetylglucosamine; however, this residue is normally absent from the final glycan structure in invertebrates due to the action of specific hexosaminidases. Previously, we have identified two hexosaminidases (HEX-2 and HEX-3) in C. elegans, which process N-glycans. In the present study, we have prepared a hex-2;hex-3 double mutant, which possesses a radically altered N-glycomic profile. Whereas in the double mutant core α1,3-fucosylation of the proximal N-acetylglucosamine was abolished, the degree of galactosylation of core α1,6-fucose increased, and a novel Galα1,2Fucα1,3 moiety attached to the distal core N-acetylglucosamine residue was detected. Both galactosylated fucose moieties were also found in two parasitic nematodes, Ascaris suum and Oesophagostomum dentatum. As core modifications of N-glycans are known targets for fungal nematotoxic lectins, the sensitivity of the C. elegans double hexosaminidase mutant was assessed. Although this mutant displayed hypersensitivity to the GalFuc-binding lectin CGL2 and the N-acetylglucosamine-binding lectin XCL, the mutant was resistant to CCL2, which binds core α1,3-fucose. Thus, the use of C. elegans mutants aids the identification of novel N-glycan modifications and the definition of in vivo specificities of nematotoxic lectins with potential as anthelmintic agents.

Indexed as

AcetylglucosamineAnimalsAnthelminticsAscaris suumCaenorhabditis elegansCaenorhabditis elegans ProteinsDrug DesignEpitopesFucoseGalectin 2GlycosylationHexosaminidasesMutationOesophagostomumPolysaccharidesAcetylglucosamineAnthelminticsCaenorhabditis elegans ProteinsEpitopesFucoseGalectin 2HexosaminidasesPolysaccharides

Identifiers

PMID22733825
PMCPMC3436517
OpenAlexW2016862743

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.