Evidence map›Paper›PMID 37558667›Full record

ArticleNature communications2023

Origin and arrangement of actin filaments for gliding motility in apicomplexan parasites revealed by cryo-electron tomography.

Matthew Martinez, Shrawan Kumar Mageswaran, Amandine Guérin, William David Chen, Cameron Parker Thompson, Sabine Chavin, Dominique Soldati-Favre, Boris Striepen, Yi-Wei Chang

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

23 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Study of Unconventional Cytoskeleton Components Regulating Actin Contraction.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  5. Atomic models of the Toxoplasma cell invasion machinery.Nature structural & molecular biology · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Cryo-ET reveals the in situ architecture of the polar tube invasion apparatus from microsporidian parasites.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Architecture of theProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Contribution of microscopy to a better understanding of the anatomy of pathogenic protists.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  18. Article
  19. Myosin F controls actin organization and dynamics inMolecular biology of the cell · 2024
    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

9 authors at 2 institutions in 2 countries.

Matthew Martinez *Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0003-2559-1794
Shrawan Kumar Mageswaran *Department of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-0803-7129
Amandine GuérinDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA.
William David ChenDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Cameron Parker ThompsonPennsylvania Muscle Institute, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA.
Sabine ChavinDepartment of Physics and Astronomy, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0009-0005-4020-5793
Dominique Soldati-FavreDepartment of Microbiology and Molecular Medicine, Faculty of Medicine, University of Geneva, Geneva, Switzerland.ORCID http://orcid.org/0000-0003-4156-2109
Boris StriepenDepartment of Pathobiology, School of Veterinary Medicine, University of Pennsylvania, Philadelphia, PA, USA.ORCID http://orcid.org/0000-0002-7426-432X
Yi-Wei ChangDepartment of Biochemistry and Biophysics, Perelman School of Medicine, University of Pennsylvania, Philadelphia, PA, USA. ywc@pennmedicine.upenn.edu.ORCID http://orcid.org/0000-0003-2391-473X
University of Pennsylvania · USUniversity of Geneva · CH

Funding

Genetic Analysis of CryptosporidiumR01AI112427 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI STRIEPEN, BORIS · 2014 to 2023
$4.2M
Sexual Development of CryptosporidiumR01AI127798 · NIAID · UNIVERSITY OF PENNSYLVANIA · PI STRIEPEN, BORIS · 2017 to 2025
$4.1M
NIAID NIH HHS R01 AI112427NIAID NIH HHS R01 AI127798
6 · The paper itself

Abstract

The phylum Apicomplexa comprises important eukaryotic parasites that invade host tissues and cells using a unique mechanism of gliding motility. Gliding is powered by actomyosin motors that translocate host-attached surface adhesins along the parasite cell body. Actin filaments (F-actin) generated by Formin1 play a central role in this critical parasitic activity. However, their subcellular origin, path and ultrastructural arrangement are poorly understood. Here we used cryo-electron tomography to image motile Cryptosporidium parvum sporozoites and reveal the cellular architecture of F-actin at nanometer-scale resolution. We demonstrate that F-actin nucleates at the apically positioned preconoidal rings and is channeled into the pellicular space between the parasite plasma membrane and the inner membrane complex in a conoid extrusion-dependent manner. Within the pellicular space, filaments on the inner membrane complex surface appear to guide the apico-basal flux of F-actin. F-actin concordantly accumulates at the basal end of the parasite. Finally, analyzing a Formin1-depleted Toxoplasma gondii mutant pinpoints the upper preconoidal ring as the conserved nucleation hub for F-actin in Cryptosporidium and Toxoplasma. Together, we provide an ultrastructural model for the life cycle of F-actin for apicomplexan gliding motility.

Indexed as

CryptosporidiosisCryptosporidiumParasitesToxoplasmaActin CytoskeletonActinsAnimalsElectron Microscope TomographyHumansProtozoan ProteinsActinsProtozoan Proteins

Identifiers

PMID37558667
PMCPMC10412601
OpenAlexW4385704116

What OpenQuestion holds

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LicenceCC BY
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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.