Evidence map›Paper›PMID 16319175›Full record

ArticleMolecular biology of the cell2006

Unusual kinetic and structural properties control rapid assembly and turnover of actin in the parasite Toxoplasma gondii.

Nivedita Sahoo, Wandy Beatty, John Heuser, David Sept, L David Sibley

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.

0numbers the graph read from it
0cells of the map it votes in
63citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

63 citing papers in PubMed, 122 citations in OpenAlex.

  1. Architecture of theProceedings of the National Academy of Sciences of the United States of America · 2024
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  7. bioRxiv : the preprint server for biology · 2023
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  10. Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019
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  12. Structural and mechanistic insights into the function of the unconventional class XIV myosin MyoA fromProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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  16. Review
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3 more citing papers are in PubMed but not listed here.

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 at 1 institution in 1 country.

Nivedita SahooDepartment of Molecular Microbiology, Center for Infectious Diseases, Washington University School of Medicine, St. Louis, MO 63110, USA.
Wandy Beatty
John Heuser
David Sept
L David Sibley
Washington University in St. Louis · US

Funding

PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
Protein interactions underlying actin-based motilityR01GM067246 · NIGMS · WASHINGTON UNIVERSITY · PI SEPT, DAVID S. · 2002 to 2006
$1.3M
NIAID NIH HHS R01 AI034036NIGMS NIH HHS GM-067246NIGMS NIH HHS R01 GM067246
6 · The paper itself

Abstract

Toxoplasma is a protozoan parasite in the phylum Apicomplexa, which contains a number of medically important parasites that rely on a highly unusual form of motility termed gliding to actively penetrate their host cells. Parasite actin filaments regulate gliding motility, yet paradoxically filamentous actin is rarely detected in these parasites. To investigate the kinetics of this unusual parasite actin, we expressed TgACT1 in baculovirus and purified it to homogeneity. Biochemical analysis showed that Toxoplasma actin (TgACT1) rapidly polymerized into filaments at a critical concentration that was 3-4-fold lower than conventional actins, yet it failed to copolymerize with mammalian actin. Electron microscopic analysis revealed that TgACT1 filaments were 10 times shorter and less stable than rabbit actin. Phylogenetic comparison of actins revealed a limited number of apicomplexan-specific residues that likely govern the unusual behavior of parasite actin. Molecular modeling identified several key alterations that affect interactions between monomers and that are predicted to destabilize filaments. Our findings suggest that conserved molecular differences in parasite actin favor rapid cycles of assembly and disassembly that govern the unusual form of gliding motility utilized by apicomplexans.

Indexed as

Actin CytoskeletonActinsAnimalsBaculoviridaeCells, CulturedCloning, MolecularDepsipeptidesKineticsModels, MolecularPhylogenyProtein Structure, TertiaryProtozoan ProteinsRabbitsToxoplasmaActinsDepsipeptidesjasplakinolideProtozoan Proteins

Identifiers

PMID16319175
PMCPMC1356598
OpenAlexW2020819397

What OpenQuestion holds

Textmetadata
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.