Evidence map›Paper›PMID 9628889›Full record

ArticleThe Journal of cell biology1998

The protozoan parasite Toxoplasma gondii targets proteins to dense granules and the vacuolar space using both conserved and unusual mechanisms.

V Karsten, H Qi, C J Beckers, A Reddy, J F Dubremetz, P Webster, K A Joiner

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
8.0field-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

36 citing papers in PubMed, 122 citations in OpenAlex.

  1. Article
  2. Therapeutic Antitoxoplasmosis Potential ofJournal of tropical medicine · 2026
    Article
  3. bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
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  16. Article
  17. Article
  18. Article
  19. Cathepsin proteases in Toxoplasma gondii.Advances in experimental medicine and biology · 2011
    Review
  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

7 authors at 2 institutions in 2 countries.

V KarstenSection of Infectious Diseases, Department of Cell Biology, Yale University School of Medicine, New Haven, Connecticut 06520-8022, USA.
H Qi
C J Beckers
A Reddy
J F Dubremetz
P Webster
K A Joiner
Yale University · USInserm · FR

Funding

STRUCTURE AND FUNCTION OF THE T GONDII VACUOLE MEMBRANER01AI030060 · NIAID · YALE UNIVERSITY · PI JOINER, KEITH ALAN · 1990 to 2006
$2.7M
NIAID NIH HHS N01 AI030060NIAID NIH HHS R01 AI30060
6 · The paper itself

Abstract

All known proteins that accumulate in the vacuolar space surrounding the obligate intracellular protozoan parasite Toxoplasma gondii are derived from parasite dense granules. To determine if constitutive secretory vesicles could also mediate delivery to the vacuolar space, T. gondii was stably transfected with soluble Escherichia coli alkaline phosphatase and E. coli beta-lactamase. Surprisingly, both foreign secretory reporters were delivered quantitatively into parasite dense granules and efficiently secreted into the vacuolar space. Addition of a glycosylphosphatidylinositol membrane anchor rerouted alkaline phosphatase to the parasite surface. Alkaline phosphatase fused to the transmembrane domain and cytoplasmic tail from the endogenous dense granule protein GRA4 localized to dense granules. The protein was secreted into a tuboreticular network in the vacuolar space, in a fashion dependent upon the cytoplasmic tail, but not upon a tyrosine-based motif within the tail. Alkaline phosphatase fused to the vesicular stomatitis virus G protein transmembrane domain and cytoplasmic tail localized primarily to the Golgi, although staining of dense granules and the intravacuolar network was also detected; truncating the cytoplasmic tail decreased Golgi staining and increased delivery to dense granules but blocked delivery to the intravacuolar network. Targeting of secreted proteins to T. gondii dense granules and the plasma membrane uses general mechanisms identified in higher eukaryotic cells but is simplified and exaggerated in scope, while targeting of secreted proteins beyond the boundaries of the parasite involves unusual sorting events.

Indexed as

Membrane GlycoproteinsAlkaline PhosphataseAmino Acid SequenceAnimalsAnti-Bacterial Agentsbeta-LactamasesBinding SitesBrefeldin ACell MembraneChlorocebus aethiopsCyclopentanesCytoplasmEscherichia coliFluorescent Antibody Technique, IndirectGene ExpressionGlycosylphosphatidylinositolsAlkaline PhosphataseAnti-Bacterial Agentsbeta-LactamasesBrefeldin ACyclopentanesGlycosylphosphatidylinositolsG protein, vesicular stomatitis virusGRA4 protein, Toxoplasma gondiiMacrolidesMembrane GlycoproteinsProtein Synthesis InhibitorsProtozoan ProteinsViral Envelope Proteins

Identifiers

PMID9628889
PMCPMC2132784
OpenAlexW2142538346

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.