Evidence map›Paper›PMID 28067475›Full record

ArticleCellular microbiology2017

The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.

Natalie J Spillman, Josh R Beck, Suresh M Ganesan, Jacquin C Niles, Daniel E Goldberg

Abstract read
In one paragraph

Article in Cellular microbiology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Biogenesis of CytochromesACS infectious diseases · 2025
    Article
  6. Article
  7. Biogenesis of cytochromesbioRxiv : the preprint server for biology · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. GeneTargeter: AutomatedThe CRISPR journal · 2022
    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.

Natalie J SpillmanDepartments of Medicine and Molecular Microbiology, Washington University School of Medicine, Saint Louis, Missouri, 63110, USA.ORCID 0000-0002-3454-1636
Josh R BeckDepartments of Medicine and Molecular Microbiology, Washington University School of Medicine, Saint Louis, Missouri, 63110, USA.
Suresh M GanesanDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA.
Jacquin C NilesDepartment of Biological Engineering, Massachusetts Institute of Technology, Cambridge, Massachusetts, 02139, USA.
Daniel E GoldbergDepartments of Medicine and Molecular Microbiology, Washington University School of Medicine, Saint Louis, Missouri, 63110, USA.

Funding

Infectious Diseases/Basic Microbial Pathogenic MechanismsT32AI007172 · NIAID · WASHINGTON UNIVERSITY · PI Daniel E. Goldberg, JENNIFER A PHILIPS · 1985 to 2026
$13.0M
Erythrocyte Subversion by Malaria Parasite Exported EffectorsK99HL133453 · NHLBI · WASHINGTON UNIVERSITY · PI BECK, JOSH RYAN · 2016 to 2017
$166k
Elucidating the role of heat shock protein 101 in malaria effector protein exportF32AI115965 · NIAID · WASHINGTON UNIVERSITY · PI BECK, JOSH RYAN · 2015 to 2016
$71k
Howard Hughes Medical InstituteNHLBI NIH HHS K99 HL133453NIAID NIH HHS F32 AI115965NIAID NIH HHS T32 AI007172
6 · The paper itself

Abstract

The malaria parasite exports numerous proteins into its host red blood cell (RBC). The trafficking of these exported effectors is complex. Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. Recently, it was suggested that the parasite TRiC chaperonin complex is exported, and that it is involved in trafficking of exported effectors. Using a parasite-specific antibody and epitope-tagged transgenic parasites we could observe no export of Plasmodium TRiC into the RBC. We tested the importance of the parasite TRiC by creating a regulatable knockdown line of the TRiC-θ subunit. Loss of the parasite TRiC-θ led to a severe growth defect in asexual development, but did not alter protein export into the RBC. These observations indicate that the TRiC proteins play a critical role in parasite biology, though their function, within the parasite, appears unrelated to protein trafficking in the RBC compartment.

Indexed as

Cell MembraneChaperoninsCytosolErythrocytesGene Expression RegulationHumansMalaria, FalciparumMultiprotein ComplexesPlasmodium falciparumProtein RefoldingProtein TransportVacuolesChaperoninsMultiprotein Complexeschaperoninmalariaprotein exportregulatable expressionT-complex proteinTRiC

Identifiers

PMID28067475
PMCPMC5429184

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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.