Evidence map›Paper›PMID 17995454›Full record

ArticleBiology of the cell2008

A transient forward-targeting element for microneme-regulated secretion in Toxoplasma gondii.

Susannah D Brydges, Jill M Harper, Fabiola Parussini, Isabelle Coppens, Vern B Carruthers

Abstract read
In one paragraph

Article in Biology of the cell, 2008. 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
–field-weighted citation impact
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.

  1. Molecular therapy. Oncology · 2025
    Article
  2. Article
  3. Article
  4. A cathepsin C-like protease post-translationally modifiesbioRxiv : the preprint server for biology · 2023
    Article
  5. An image-based high-content screening for compounds targetingFrontiers in cellular and infection microbiology · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Frontiers in microbiology · 2017
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Cathepsin proteases in Toxoplasma gondii.Advances in experimental medicine and biology · 2011
    Review
  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

5 authors.

Susannah D BrydgesW. Harry Feinstone Department of Molecular Microbiology and Immunology, Johns Hopkins Bloomberg School of Public Health, Baltimore, MD 21205, USA.
Jill M Harper
Fabiola Parussini
Isabelle Coppens
Vern B Carruthers

Funding

MICRONEME FUNCTION IN TOXOPLASMAR01AI046675 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI CARRUTHERS, VERNON BRUCE · 2000 to 2021
$6.5M
Targeting of host vesicles to the vacuole of Toxoplasma and lipid cargo sortingR01AI060767 · NIAID · JOHNS HOPKINS UNIVERSITY · PI COPPENS, ISABELLE · 2004 to 2020
$5.1M
NIAID NIH HHS AI-046675NIAID NIH HHS AI-060767NIAID NIH HHS R01 AI046675NIAID NIH HHS R01 AI060767
6 · The paper itself

Abstract

background informationAccurate sorting of proteins to the three types of secretory granules in Toxoplasma gondii is crucial for successful cell invasion by this obligate intracellular parasite. As in other eukaryotic systems, propeptide sequences are a common yet poorly understood feature of proteins destined for regulated secretion, which for Toxoplasma occurs through two distinct invasion organelles, rhoptries and micronemes. Microneme discharge during parasite apical attachment plays a pivotal role in cell invasion by delivering adhesive proteins for host receptor engagement.

resultsWe show here that the small micronemal proprotein MIC5 (microneme protein-5) undergoes proteolytic maturation at a site beyond the Golgi, and only the processed form of MIC5 is secreted via the micronemes. Proper cleavage of the MIC5 propeptide relies on an arginine residue in the P1' position, although P1' mutants are still cleaved to a lesser extent at an alternative site downstream of the primary site. Nonetheless, this aberrantly cleaved species still correctly traffics to the micronemes, indicating that correct cleavage is not necessary for micronemal targeting. In contrast, a deletion mutant lacking the propeptide was retained within the secretory system, principally in the ER (endoplasmic reticulum). The MIC5 propeptide also supported correct trafficking when exchanged for the M2AP propeptide, which was recently shown to also be required for micronemal trafficking of the TgMIC2 (T. gondii MIC2)-M2AP complex [Harper, Huynh, Coppens, Parussini, Moreno and Carruthers (2006) Mol. Biol. Cell 17, 4551-4563].

conclusionOur results illuminate common and unique features of micronemal propeptides in their role as trafficking facilitators.

Indexed as

Amino Acid SequenceAnimalsAnimals, Genetically ModifiedChelating AgentsEgtazic AcidGolgi ApparatusHumansMicroscopy, ElectronMolecular Sequence DataOrganellesPlasmidsProtein FoldingProtein Processing, Post-TranslationalProtein TransportProtozoan ProteinsSecretory Vesicles1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl esterChelating AgentsEgtazic AcidProtozoan Proteins

Identifiers

PMID17995454
PMCPMC2663041

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.