Evidence map›Paper›PMID 26814575›Full record

ArticleeLife2016

Guanylate binding proteins directly attack Toxoplasma gondii via supramolecular complexes.

Elisabeth Kravets, Daniel Degrandi, Qijun Ma, Thomas-Otavio Peulen, Verena Klümpers, Suren Felekyan, Ralf Kühnemuth, Stefanie Weidtkamp-Peters, Claus Am Seidel, Klaus Pfeffer

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
12.6field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 132 citations in OpenAlex.

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  14. Frontiers in immunology · 2025
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  19. To kill a tachyzoite: assault and battery.Trends in parasitology · 2024
    Article
  20. Interferon-Science (New York, N.Y.) · 2024
    Review

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

10 authors at 1 institution in 1 country.

Elisabeth KravetsInstitute of Medical Microbiology and Hospital Hygiene, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.
Daniel DegrandiInstitute of Medical Microbiology and Hospital Hygiene, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.
Qijun MaInstitute for Molecular Physical Chemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Thomas-Otavio PeulenInstitute for Molecular Physical Chemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Verena KlümpersInstitute of Medical Microbiology and Hospital Hygiene, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.
Suren FelekyanInstitute for Molecular Physical Chemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Ralf KühnemuthInstitute for Molecular Physical Chemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Stefanie Weidtkamp-PetersCenter of Advanced Imaging, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.
Claus Am SeidelInstitute for Molecular Physical Chemistry, Heinrich-Heine-University Düsseldorf, Düsseldorf, Germany.ORCID http://orcid.org/0000-0002-5171-149X
Klaus PfefferInstitute of Medical Microbiology and Hospital Hygiene, Heinrich-Heine University Düsseldorf, Düsseldorf, Germany.
Heinrich Heine University Düsseldorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

GBPs are essential for immunity against intracellular pathogens, especially for Toxoplasma gondii control. Here, the molecular interactions of murine GBPs (mGBP1/2/3/5/6), homo- and hetero-multimerization properties of mGBP2 and its function in parasite killing were investigated by mutational, Multiparameter Fluorescence Image Spectroscopy, and live cell microscopy methodologies. Control of T. gondii replication by mGBP2 requires GTP hydrolysis and isoprenylation thus, enabling reversible oligomerization in vesicle-like structures. mGBP2 undergoes structural transitions between monomeric, dimeric and oligomeric states visualized by quantitative FRET analysis. mGBPs reside in at least two discrete subcellular reservoirs and attack the parasitophorous vacuole membrane (PVM) as orchestrated, supramolecular complexes forming large, densely packed multimers comprising up to several thousand monomers. This dramatic mGBP enrichment results in the loss of PVM integrity, followed by a direct assault of mGBP2 upon the plasma membrane of the parasite. These discoveries provide vital dynamic and molecular perceptions into cell-autonomous immunity.

Indexed as

AnimalsCell MembraneCell SurvivalFluorescence Resonance Energy TransferGTP-Binding ProteinsMiceMicroscopyOptical ImagingProtein MultimerizationSpectrometry, X-Ray EmissionToxoplasmaVacuolesGbp2 protein, mouseGTP-Binding Proteinsbiophysicscell-autonomous immunityFörster resonance energy transferguanylate-binding proteinshost-pathogen interactioninfectious diseasemicrobiologymousemultiparameter fluorescence image spectroscopystructural biology

Identifiers

PMID26814575
PMCPMC4786432
OpenAlexW2310060842

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.