Evidence map›Paper›PMID 38141762›Full record

ArticleThe Journal of biological chemistry2024

Toxoplasma gondii mitochondrial association factor 1b interactome reveals novel binding partners including Ral GTPase accelerating protein α1.

Cameron J Powell, Meredith L Jenkins, Tara B Hill, Matthew L Blank, Leah F Cabo, Lexie R Thompson, John E Burke, Jon P Boyle, Martin J Boulanger

Open access · goldAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.6field-weighted citation impact, top 34% 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

3 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
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

9 authors at 3 institutions in 2 countries.

Cameron J PowellDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.
Meredith L JenkinsDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.
Tara B HillDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.
Matthew L BlankDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Leah F CaboDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Lexie R ThompsonDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada.
John E BurkeDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada; Department of Biochemistry and Molecular Biology, The University of British Columbia, Vancouver, British Columbia, Canada.
Jon P BoyleDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania, USA.
Martin J BoulangerDepartment of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada. Electronic address: mboulang@uvic.ca.
University of Victoria · CAUniversity of Pittsburgh · USUniversity of British Columbia · CA

Funding

Comparative and functional genomics of Toxoplasma and Hammondia hammondiR01AI116855 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BOYLE, JON P · 2015 to 2024
$3.2M
Effector diversification and Toxoplasma virulenceR01AI114655 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BOYLE, JON P · 2015 to 2019
$1.9M
CIHRNIAID NIH HHS R01 AI114655NIAID NIH HHS R01 AI116855
6 · The paper itself

Abstract

The intracellular parasite, Toxoplasma gondii, has developed sophisticated molecular strategies to subvert host processes and promote growth and survival. During infection, T. gondii replicates in a parasitophorous vacuole (PV) and modulates host functions through a network of secreted proteins. Of these, Mitochondrial Association Factor 1b (MAF1b) recruits host mitochondria to the PV, a process that confers an in vivo growth advantage, though the precise mechanisms remain enigmatic. To address this knowledge gap, we mapped the MAF1b interactome in human fibroblasts using a commercial Yeast-2-hybrid (Y2H) screen, which revealed several previously unidentified binding partners including the GAP domain of Ral GTPase Accelerating Protein α1 (RalGAPα1(GAP)). Recombinantly produced MAF1b and RalGAPα1(GAP) formed as a stable binary complex as shown by size exclusion chromatography with a K

Indexed as

GTPase-Activating ProteinsMitochondriaProtein Interaction MapsProtozoan ProteinsToxoplasmaBinding SitesCalorimetryChromatography, GelFibroblastsHumansHydrogen Deuterium Exchange-Mass SpectrometryNerve Tissue ProteinsTwo-Hybrid System TechniquesGTPase-Activating ProteinsNerve Tissue ProteinsProtozoan ProteinsRALGAPA1 protein, humanGTPase activating protein (GAP)host mitochondrial associationhost-pathogen interactionhydrogen-deuterium exchangehydrogen exchange mass spectrometryisothermal titration calorimetry (ITC)molecular modellingRalGAPα1Toxoplasma gondii

Identifiers

PMID38141762
PMCPMC10821591
OpenAlexW4390064567

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.