Evidence map›Paper›PMID 36245278›Full record

ArticleThe EMBO journal2022

An apical membrane complex for triggering rhoptry exocytosis and invasion in Toxoplasma.

Daniela Sparvoli, Jason Delabre, Diana Marcela Penarete-Vargas, Shrawan Kumar Mageswaran, Lev M Tsypin, Justine Heckendorn, Liam Theveny, Marjorie Maynadier, Marta Mendonça Cova, Laurence Berry-Sterkers and 7 more

Open access · hybridAbstract read
In one paragraph

Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.8field-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

24 citing papers in PubMed, 38 citations in OpenAlex.

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  14. SPARK regulates AGC kinases central to thebioRxiv : the preprint server for biology · 2024
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  15. The emerging role ofFrontiers in immunology · 2024
    Review
  16. Article
  17. The Immunoprotective Effect of ROP27 Protein ofAnimals : an open access journal from MDPI · 2023
    Article
  18. Article
  19. Article
  20. mBio · 2023
    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

17 authors at 3 institutions in 2 countries.

Daniela Sparvoli *Laboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.ORCID 0000-0002-5992-3753
Jason Delabre *Laboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
Diana Marcela Penarete-Vargas *Laboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
Shrawan Kumar Mageswaran *Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Lev M TsypinDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL, USA.ORCID 0000-0002-0642-8468
Justine HeckendornLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
Liam ThevenyDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Marjorie MaynadierLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.ORCID 0000-0002-1825-3095
Marta Mendonça CovaLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.ORCID 0000-0001-6727-248X
Laurence Berry-SterkersLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
Amandine GuérinDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Jean-François DubremetzLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.
Serge UrbachIGF, Université de Montpellier, CNRS, INSERM, Montpellier, France.ORCID 0000-0001-8663-2006
Boris StriepenDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0002-7426-432X
Aaron P TurkewitzDepartment of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL, USA.
Yi-Wei ChangDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID 0000-0003-2391-473X
Maryse LebrunLaboratory of Pathogen Host Interactions, UMR 5235 CNRS, Université de Montpellier, Montpellier, France.ORCID 0000-0002-6292-8408
Centre National de la Recherche Scientifique · FRUniversity of Pennsylvania · USUniversity of Chicago · US

Funding

Genetic Analysis of CryptosporidiumR01AI112427 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI STRIEPEN, BORIS · 2014 to 2023
$4.2M
Sortilin-dependent traffic to dense core secretory granules - Resubmission 01R01GM105783 · NIGMS · UNIVERSITY OF CHICAGO · PI TURKEWITZ, AARON P · 2014 to 2022
$2.7M
Genetic Analysis of CryptosporidiumR37AI112427 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI BORIS STRIEPEN · 2024 to 2026
$1.5M
European Research Council 833309NIAID NIH HHS R01 AI112427NIAID NIH HHS R37 AI112427NIGMS NIH HHS R01 GM105783
6 · The paper itself

Abstract

Apicomplexan parasites possess secretory organelles called rhoptries that undergo regulated exocytosis upon contact with the host. This process is essential for the parasitic lifestyle of these pathogens and relies on an exocytic machinery sharing structural features and molecular components with free-living ciliates. However, how the parasites coordinate exocytosis with host interaction is unknown. Here, we performed a Tetrahymena-based transcriptomic screen to uncover novel exocytic factors in Ciliata and conserved in Apicomplexa. We identified membrane-bound proteins, named CRMPs, forming part of a large complex essential for rhoptry secretion and invasion in Toxoplasma. Using cutting-edge imaging tools, including expansion microscopy and cryo-electron tomography, we show that, unlike previously described rhoptry exocytic factors, TgCRMPs are not required for the assembly of the rhoptry secretion machinery and only transiently associate with the exocytic site-prior to the invasion. CRMPs and their partners contain putative host cell-binding domains, and CRMPa shares similarities with GPCR proteins. Collectively our data imply that the CRMP complex acts as a host-molecular sensor to ensure that rhoptry exocytosis occurs when the parasite contacts the host cell.

Indexed as

ToxoplasmaExocytosisHost-Parasite InteractionsMembrane ProteinsOrganellesProtozoan ProteinsMembrane ProteinsProtozoan ProteinsapicomplexaciliatesCRMPrhoptrysecretion

Identifiers

PMID36245278
PMCPMC9670195
OpenAlexW4306391381

What OpenQuestion holds

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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.