Evidence map›Paper›PMID 21964353›Full record

ArticleMolecular & cellular proteomics : MCP2011

Life cycle stage-resolved proteomic analysis of the excretome/secretome from Strongyloides ratti--identification of stage-specific proteases.

Hanns Soblik, Abuelhassan Elshazly Younis, Makedonka Mitreva, Bernhard Y Renard, Marc Kirchner, Frank Geisinger, Hanno Steen, Norbert W Brattig

Open access · hybridAbstract read
In one paragraph

Article in Molecular & cellular proteomics : MCP, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
4.7field-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

54 citing papers in PubMed, 110 citations in OpenAlex.

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  7. Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
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  8. Invade or die: behaviours and biochemical mechanisms that drive skin penetration inPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024
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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 5 institutions in 3 countries.

Hanns SoblikBernhard Nocht Institute for Tropical Medicine, Hamburg, Germany.
Abuelhassan Elshazly Younis
Makedonka Mitreva
Bernhard Y Renard
Marc Kirchner
Frank Geisinger
Hanno Steen
Norbert W Brattig
Bernhard Nocht Institute for Tropical Medicine · DEBoston Children's Hospital · USAswan University · EGTranslationale Onkologie an der Universitätsmedizin der Johannes Gutenberg-Universität Mainz · DEWashington University in St. Louis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A wide range of biomolecules, including proteins, are excreted and secreted from helminths and contribute to the parasite's successful establishment, survival, and reproduction in an adverse habitat. Excretory and secretory proteins (ESP) are active at the interface between parasite and host and comprise potential targets for intervention. The intestinal nematode Strongyloides spp. exhibits an exceptional developmental plasticity in its life cycle characterized by parasitic and free-living generations. We investigated ESP from infective larvae, parasitic females, and free-living stages of the rat parasite Strongyloides ratti, which is genetically very similar to the human pathogen, Strongyloides stercoralis. Proteomic analysis of ESP revealed 586 proteins, with the largest number of stage-specific ESP found in infective larvae (196), followed by parasitic females (79) and free-living stages (35). One hundred and forty proteins were identified in all studied stages, including anti-oxidative enzymes, heat shock proteins, and carbohydrate-binding proteins. The stage-selective ESP of (1) infective larvae included an astacin metalloproteinase, the L3 Nie antigen, and a fatty acid retinoid-binding protein; (2) parasitic females included a prolyl oligopeptidase (prolyl serine carboxypeptidase), small heat shock proteins, and a secreted acidic protein; (3) free-living stages included a lysozyme family member, a carbohydrate-hydrolyzing enzyme, and saponin-like protein. We verified the differential expression of selected genes encoding ESP by qRT-PCR. ELISA analysis revealed the recognition of ESP by antibodies of S. ratti-infected rats. A prolyl oligopeptidase was identified as abundant parasitic female-specific ESP, and the effect of pyrrolidine-based prolyl oligopeptidase inhibitors showed concentration- and time-dependent inhibitory effects on female motility. The characterization of stage-related ESP from Strongyloides will help to further understand the interaction of this unique intestinal nematode with its host.

Indexed as

Amino Acid SequenceAnimalsBase SequenceCulture MediaFemaleGene Expression Regulation, DevelopmentalHelminth ProteinsImmune SeraIntestinesLarvaMaleMolecular Sequence DataPeptide HydrolasesProlyl OligopeptidasesProtease InhibitorsProtein Sorting SignalsCulture MediaHelminth ProteinsImmune SeraPeptide HydrolasesPREPL protein, humanProlyl OligopeptidasesProtease InhibitorsProtein Sorting SignalsSerine Endopeptidases

Identifiers

PMID21964353
PMCPMC3237078
OpenAlexW2142110535

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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.