Evidence map›Paper›PMID 23875042›Full record

ArticlePLoS neglected tropical diseases2013

Cathelicidin-like helminth defence molecules (HDMs): absence of cytotoxic, anti-microbial and anti-protozoan activities imply a specific adaptation to immune modulation.

Karine Thivierge, Sophie Cotton, Deborah A Schaefer, Michael W Riggs, Joyce To, Maria E Lund, Mark W Robinson, John P Dalton, Sheila M Donnelly

Open access · goldAbstract read
In one paragraph

Article in PLoS neglected tropical diseases, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
3.5field-weighted citation impact, top 8% 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, 39 citations in OpenAlex.

  1. Article
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  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Frontiers in immunology · 2020
    Review
  10. Infection by the Helminth ParasiteMolecular & cellular proteomics : MCP · 2018
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Insight into the molecular basis of Schistosoma haematobium-induced bladder cancer through urine proteomics.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016
    Article
  17. Article
  18. 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

9 authors at 3 institutions in 4 countries.

Karine ThiviergeInstitute of Parasitology, McGill University, Sainte-Anne-de-Bellevue, Quebec, Canada.
Sophie Cotton
Deborah A Schaefer
Michael W Riggs
Joyce To
Maria E Lund
Mark W Robinson
John P Dalton
Sheila M Donnelly
University of Technology Sydney · AUMcGill University · CAUniversity of Arizona · US

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Host defence peptides (HDPs) are expressed throughout the animal and plant kingdoms. They have multifunctional roles in the defence against infectious agents of mammals, possessing both bactericidal and immune-modulatory activities. We have identified a novel family of molecules secreted by helminth parasites (helminth defence molecules; HDMs) that exhibit similar structural and biochemical characteristics to the HDPs. Here, we have analyzed the functional activities of four HDMs derived from Schistosoma mansoni and Fasciola hepatica and compared them to human, mouse, bovine and sheep HDPs. Unlike the mammalian HDPs the helminth-derived HDMs show no antimicrobial activity and are non-cytotoxic to mammalian cells (macrophages and red blood cells). However, both the mammalian- and helminth-derived peptides suppress the activation of macrophages by microbial stimuli and alter the response of B cells to cytokine stimulation. Therefore, we hypothesise that HDMs represent a novel family of HDPs that evolved to regulate the immune responses of their mammalian hosts by retaining potent immune modulatory properties without causing deleterious cytotoxic effects.

Indexed as

Host-Pathogen InteractionsAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBacteriaCathelicidinsCattleCells, CulturedCytotoxinsErythrocytesFasciola hepaticaHelminth ProteinsHumansImmunologic FactorsMacrophage ActivationMacrophagesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesCathelicidinsCytotoxinsHelminth ProteinsImmunologic Factors

Identifiers

PMID23875042
PMCPMC3708846
OpenAlexW2056628838

What OpenQuestion holds

Textmetadata
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.