Evidence map›Paper›PMID 24289031›Full record

ArticleVeterinary research2013

Novel expression of Haemonchus contortus vaccine candidate aminopeptidase H11 using the free-living nematode Caenorhabditis elegans.

Brett Roberts, Aristotelis Antonopoulos, Stuart M Haslam, Alison J Dicker, Tom N McNeilly, Stephanie L Johnston, Anne Dell, David P Knox, Collette Britton

Open access · goldAbstract read
In one paragraph

Article in Veterinary research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
5.5field-weighted citation impact, top 4% 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

27 citing papers in PubMed, 65 citations in OpenAlex.

  1. Deciphering theBiomolecules · 2025
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  8. Review
  9. Analysis of Caenorhabditis Protein Glycosylation.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  10. The Proteome and Lipidome of Extracellular Vesicles fromInternational journal of molecular sciences · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. N-glycome and N-glycoproteome of a hematophagous parasitic nematodeComputational and structural biotechnology journal · 2021
    Article
  18. Review
  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

9 authors at 3 institutions in 1 country.

Brett RobertsInstitute of Infection, Immunity and Inflammation, College of Medical, Veterinary and Life Sciences, University of Glasgow, Bearsden Road, Glasgow G61 1QH, UK. Collette.Britton@glasgow.ac.uk.
Aristotelis Antonopoulos
Stuart M Haslam
Alison J Dicker
Tom N McNeilly
Stephanie L Johnston
Anne Dell
David P Knox
Collette Britton
Imperial College London · GBMoredun Research Institute · GBUniversity of Glasgow · GB

Funding

Biotechnology and Biological Sciences Research Council B19088Biotechnology and Biological Sciences Research Council BB/F002033/1Biotechnology and Biological Sciences Research Council BB/F008309/1Biotechnology and Biological Sciences Research Council BBF0083091Biotechnology and Biological Sciences Research Council F002033
6 · The paper itself

Abstract

With the problem of parasitic nematode drug resistance increasing, vaccine development offers an alternative sustainable control approach. For some parasitic nematodes, native extracts enriched for specific proteins are highly protective. However, recombinant forms of these proteins have failed to replicate this protection. This is thought to be due to differences in glycosylation and/or conformation between native and recombinant proteins. We have exploited the free-living nematode Caenorhabditis elegans to examine its suitability as an alternative system for recombinant expression of parasitic nematode vaccine candidates. We focussed on Haemonchus contortus aminopeptidase H11 glycoprotein, which is enriched in a gut membrane fraction capable of inducing significant protection against this important ovine gastrointestinal nematode. We show that H. contortus H11 expressed in C. elegans is enzymatically active and MALDI mass spectrometry identifies similar di- and tri-fucosylated structures to those on native H11, with fucose at the 3- and/or 6-positions of the proximal GlcNAc. Some glycan structural differences were observed, such as lack of LDNF. Serum antibody to native H11 binds to C. elegans recombinant H11 and most of the antibody to rH11 or native H11 is directed to glycan moieties. Despite these similarities, no reduction in worm burden or faecal egg count was observed following immunisation of sheep with C. elegans-expressed recombinant H11 protein. The findings suggest that the di- and tri-fucosylated N-glycans expressed on rH11 do not contribute to the protective effect of H11 and that additional components present in native H11-enriched extract are likely required for enhancing the antibody response necessary for protection.

Indexed as

AminopeptidasesAnimalsAnimals, Genetically ModifiedCaenorhabditis elegansHaemonchiasisHaemonchusHelminth ProteinsMolecular Sequence DataRecombinant ProteinsSequence AlignmentSequence Analysis, ProteinSheepSheep DiseasesSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryVaccinesAminopeptidasesHelminth ProteinsRecombinant ProteinsVaccines

Identifiers

PMID24289031
PMCPMC4176091
OpenAlexW2162009890

What OpenQuestion holds

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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.