Evidence map›Paper›PMID 21998582›Full record

ArticlePLoS pathogens2011

Evolutionarily divergent, unstable filamentous actin is essential for gliding motility in apicomplexan parasites.

Kristen M Skillman, Karthikeyan Diraviyam, Asis Khan, Keliang Tang, David Sept, L David Sibley

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

60 citing papers in PubMed, 112 citations in OpenAlex.

  1. Article
  2. Study of Unconventional Cytoskeleton Components Regulating Actin Contraction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Refractile bodies ofFrontiers in cellular and infection microbiology · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Unusual dynamics of the divergent malaria parasiteProceedings of the National Academy of Sciences of the United States of America · 2019
    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

6 authors at 2 institutions in 1 country.

Kristen M SkillmanDepartment of Molecular Microbiology, Washington University School of Medicine, St. Louis, Missouri, USA.
Karthikeyan Diraviyam
Asis Khan
Keliang Tang
David Sept
L David Sibley
Washington University in St. Louis · USUniversity of Michigan–Ann Arbor · US

Funding

Infectious Diseases/Basic Microbial Pathogenic MechanismsT32AI007172 · NIAID · WASHINGTON UNIVERSITY · PI Daniel E. Goldberg, JENNIFER A PHILIPS · 1985 to 2026
$13.0M
PROTEIN SECRETION &INTRACELLULAR SURVIVAL BY TOXOPLASMAR01AI034036 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 1993 to 2019
$7.9M
Targeting the Actin Cytoskeleton in ParasitesR01AI073155 · NIAID · WASHINGTON UNIVERSITY · PI SIBLEY, L. DAVID · 2007 to 2011
$1.7M
NIAID NIH HHS AI073155NIAID NIH HHS R01 AI034036NIAID NIH HHS R01 AI073155NIAID NIH HHS T32 AI007172NIAID NIH HHS T32-AI007172
6 · The paper itself

Abstract

Apicomplexan parasites rely on a novel form of actin-based motility called gliding, which depends on parasite actin polymerization, to migrate through their hosts and invade cells. However, parasite actins are divergent both in sequence and function and only form short, unstable filaments in contrast to the stability of conventional actin filaments. The molecular basis for parasite actin filament instability and its relationship to gliding motility remain unresolved. We demonstrate that recombinant Toxoplasma (TgACTI) and Plasmodium (PfACTI and PfACTII) actins polymerized into very short filaments in vitro but were induced to form long, stable filaments by addition of equimolar levels of phalloidin. Parasite actins contain a conserved phalloidin-binding site as determined by molecular modeling and computational docking, yet vary in several residues that are predicted to impact filament stability. In particular, two residues were identified that form intermolecular contacts between different protomers in conventional actin filaments and these residues showed non-conservative differences in apicomplexan parasites. Substitution of divergent residues found in TgACTI with those from mammalian actin resulted in formation of longer, more stable filaments in vitro. Expression of these stabilized actins in T. gondii increased sensitivity to the actin-stabilizing compound jasplakinolide and disrupted normal gliding motility in the absence of treatment. These results identify the molecular basis for short, dynamic filaments in apicomplexan parasites and demonstrate that inherent instability of parasite actin filaments is a critical adaptation for gliding motility.

Indexed as

Cell MovementEvolution, MolecularActin CytoskeletonActinsAmino Acid SubstitutionAnimalsBinding SitesDepsipeptidesGene Expression RegulationModels, MolecularParasitesPhalloidinePhylogenyPlasmidsPlasmodiumProtein MultimerizationActinsDepsipeptidesjasplakinolidePhalloidineProtozoan Proteins

Identifiers

PMID21998582
PMCPMC3188518
OpenAlexW1985611492

What OpenQuestion holds

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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.