Evidence map›Paper›PMID 23895670›Full record

ArticleJournal of proteome research2013

In-depth proteomic and glycomic analysis of the adult-stage Cooperia oncophora excretome/secretome.

Jimmy Borloo, Jessie De Graef, Iris Peelaers, D Linh Nguyen, Makedonka Mitreva, Bart Devreese, Cornelis H Hokke, Jozef Vercruysse, Edwin Claerebout, Peter Geldhof

Abstract read
In one paragraph

Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
4.7field-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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. A Revised Checklist ofHelminthologia · 2020
    Article
  6. Helminth Vaccines in Ruminants: From Development to Application.The Veterinary clinics of North America. Food animal practice · 2020
    Review
  7. Article
  8. Perusal of parasitic nematode 'omics in the post-genomic era.Molecular and biochemical parasitology · 2017
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Mucin-Type O-Glycosylation in Invertebrates.Molecules (Basel, Switzerland) · 2015
    Review
  14. 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

10 authors at 3 institutions in 3 countries.

Jimmy BorlooLaboratory of Parasitology, Faculty of Veterinary Medicine, Ghent University, Salisburylaan 133, Merelbeke B-9820, Belgium. jimmyborloo@hotmail.com
Jessie De Graef
Iris Peelaers
D Linh Nguyen
Makedonka Mitreva
Bart Devreese
Cornelis H Hokke
Jozef Vercruysse
Edwin Claerebout
Peter Geldhof
Ghent University · BELeiden University Medical Center · NLOffice of Infectious Diseases · US

Funding

COMPARATIVE GENOMICS OF PARASITIC NEMATODESR01AI081803 · NIAID · WASHINGTON UNIVERSITY · PI MITREVA, MAKEDONKA · 2009 to 2018
$3.1M
NIAID NIH HHS R01 AI081803
6 · The paper itself

Abstract

Cooperia oncophora is one of the most common intestinal parasitic nematodes in cattle worldwide. To date, C. oncophora infections are treated using broad-spectrum anthelmintics. However, during the past decade, reports of anthelmintic resistance in this parasite species have emerged worldwide, necessitating new avenues for its control, possibly through vaccination. In this frame, we analyzed the adult-stage C. oncophora excretome/secretome (ES), covering both the protein and glycan components, since this fraction constitutes the primary interface between parasite and host and may hold potential vaccine candidates. Two-dimensional gel electrophoretic separation of the ES material enabled the MALDI-TOF mass spectrometry (MS)-directed identification of 12 distinct proteins, grouped in three separate molecular weight fractions: (i) a high molecular weight fraction consisting of a double-domain activation-associated secreted protein (ASP), (ii) a midmolecular weight fraction predominantly containing a single-domain ASP, a thioredoxin peroxidase and innexin, and (iii) a low molecular weight protein pool essentially holding two distinct low molecular weight antigens. Further MS-driven glycan analysis mapped a variety of N-glycans to the midmolecular weight single-domain ASP, with Man6GlcNAc2 oligomannosyl glycans as the major species. The predominance of the nonglycosylated double-domain ASP in the high-molecular weight fraction renders it ideal for advancement toward vaccine trials and development.

Indexed as

Amino Acid SequenceAnimalsCarbohydrate ConformationCarbohydrate SequenceFemaleGlycoproteinsHelminth ProteinsLife Cycle StagesMaleMolecular Sequence DataPolysaccharidesProteomeProteomicsTrichostrongyloideaGlycoproteinsHelminth ProteinsPolysaccharidesProteome

Identifiers

PMID23895670
PMCPMC3883574
OpenAlexW2061350007

What OpenQuestion holds

Textmetadata
LicenceTDM
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.