Evidence map›Paper›PMID 21589904›Full record

ArticlePLoS pathogens2011

A family of helminth molecules that modulate innate cell responses via molecular mimicry of host antimicrobial peptides.

Mark W Robinson, Sheila Donnelly, Andrew T Hutchinson, Joyce To, Nicole L Taylor, Raymond S Norton, Matthew A Perugini, John P Dalton

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 71 papers.

0numbers the graph read from it
0cells of the map it votes in
71citing papers in PubMed
8.6field-weighted citation impact, top 2% 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

71 citing papers in PubMed, 145 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Cecropin anisaxin-2S hasFrontiers in immunology · 2025
    Article
  5. Review
  6. Article
  7. Pathogens (Basel, Switzerland) · 2024
    Article
  8. Article
  9. Trematode Genomics and Proteomics.Advances in experimental medicine and biology · 2024
    Article
  10. Review
  11. Article
  12. Antigens from the HelminthInternational journal of molecular sciences · 2023
    Article
  13. Type I Cystatin Derived fromPathogens (Basel, Switzerland) · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. The Zoonotic Helminth ParasiteAnimals : an open access journal from MDPI · 2021
    Article
  19. Article
  20. Article

11 more citing papers are in PubMed but not listed here.

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

8 authors at 4 institutions in 2 countries.

Mark W RobinsonInfection, Immunity and Innovation (i3) Institute, University of Technology Sydney (UTS), Ultimo, Sydney, Australia. mark.robinson@uts.edu.au
Sheila Donnelly
Andrew T Hutchinson
Joyce To
Nicole L Taylor
Raymond S Norton
Matthew A Perugini
John P Dalton
University of Technology Sydney · AUUniversity of Melbourne · AUMcGill University · CAMonash University · AU

Funding

Canadian Institutes of Health Research
6 · The paper itself

Abstract

Over the last decade a significant number of studies have highlighted the central role of host antimicrobial (or defence) peptides in modulating the response of innate immune cells to pathogen-associated ligands. In humans, the most widely studied antimicrobial peptide is LL-37, a 37-residue peptide containing an amphipathic helix that is released via proteolytic cleavage of the precursor protein CAP18. Owing to its ability to protect against lethal endotoxaemia and clinically-relevant bacterial infections, LL-37 and its derivatives are seen as attractive candidates for anti-sepsis therapies. We have identified a novel family of molecules secreted by parasitic helminths (helminth defence molecules; HDMs) that exhibit similar biochemical and functional characteristics to human defence peptides, particularly CAP18. The HDM secreted by Fasciola hepatica (FhHDM-1) adopts a predominantly α-helical structure in solution. Processing of FhHDM-1 by F. hepatica cathepsin L1 releases a 34-residue C-terminal fragment containing a conserved amphipathic helix. This is analogous to the proteolytic processing of CAP18 to release LL-37, which modulates innate cell activation by classical toll-like receptor (TLR) ligands such as lipopolysaccharide (LPS). We show that full-length recombinant FhHDM-1 and a peptide analogue of the amphipathic C-terminus bind directly to LPS in a concentration-dependent manner, reducing its interaction with both LPS-binding protein (LBP) and the surface of macrophages. Furthermore, FhHDM-1 and the amphipathic C-terminal peptide protect mice against LPS-induced inflammation by significantly reducing the release of inflammatory mediators from macrophages. We propose that HDMs, by mimicking the function of host defence peptides, represent a novel family of innate cell modulators with therapeutic potential in anti-sepsis treatments and prevention of inflammation.

Indexed as

Molecular MimicryAcute-Phase ProteinsAmino Acid SequenceAnimalsAnti-Infective AgentsAntimicrobial Cationic PeptidesCarrier ProteinsCathelicidinsEndotoxemiaFasciola hepaticaFascioliasisHelminth ProteinsHumansImmunity, InnateInflammationLipopolysaccharide-Binding ProteinAcute-Phase ProteinsAnti-Infective AgentsAntimicrobial Cationic PeptidesCarrier ProteinsCathelicidinsHelminth ProteinsLipopolysaccharide-Binding ProteinLipopolysaccharidesMembrane GlycoproteinsRecombinant ProteinsToll-Like Receptors

Identifiers

PMID21589904
PMCPMC3093369
OpenAlexW2031757574

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.