Evidence map›Paper›PMID 24453943›Full record

ArticlePLoS biology2014

Electron tomography and simulation of baculovirus actin comet tails support a tethered filament model of pathogen propulsion.

Jan Mueller, Julia Pfanzelter, Christoph Winkler, Akihiro Narita, Christophe Le Clainche, Maria Nemethova, Marie-France Carlier, Yuichiro Maeda, Matthew D Welch, Taro Ohkawa and 3 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.6field-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

27 citing papers in PubMed, 54 citations in OpenAlex.

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  2. Pathogen-Mediated Cell Fusion and Actin Cytoskeleton.Advances in experimental medicine and biology · 2026
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  9. Three-dimensional organization of the cytoskeleton: A cryo-electron tomography perspective.Protein science : a publication of the Protein Society · 2020
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  10. High Rac1 activity is functionally translated into cytosolic structures with unique nanoscale cytoskeletal architecture.Proceedings of the National Academy of Sciences of the United States of America · 2019
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 7 institutions in 4 countries.

Jan MuellerInstitute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.
Julia PfanzelterInstitute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.
Christoph WinklerRICAM, Austrian Academy of Sciences, Vienna, Austria ; Faculty of Mathematics, University of Vienna, Austria.
Akihiro NaritaNagoya University, Graduate School of Sciences, Structural Biology Research Center and Division of Biological Sciences, Nagoya, Japan ; Nagoya University JST PRESTO, 4-1-8 Honcho Kawaguchi, Saitama, Japan.
Christophe Le ClaincheLaboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
Maria NemethovaInstitute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.
Marie-France CarlierLaboratoire d'Enzymologie et Biochimie Structurales, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France.
Yuichiro MaedaNagoya University, Graduate School of Sciences, Structural Biology Research Center and Division of Biological Sciences, Nagoya, Japan.
Matthew D WelchDepartment of Molecular and Cell Biology, University of California, Berkeley, California, United States of America.
Taro OhkawaDepartment of Molecular and Cell Biology, University of California, Berkeley, California, United States of America.
Christian SchmeiserRICAM, Austrian Academy of Sciences, Vienna, Austria ; Faculty of Mathematics, University of Vienna, Austria.
Guenter P ReschCampus Science Support Facilities GmbH, Vienna, Austria.
J Victor SmallInstitute of Molecular Biotechnology, Austrian Academy of Sciences, Vienna, Austria.
Austrian Academy of Sciences · ATInstitute of Molecular Biotechnology · ATLaboratoire d'Enzymologie et Biochimie Structurales · FRNagoya University · JPUniversity of California, Berkeley · USUniversity of Vienna · ATCampus Science Support Facilities · AT

Funding

Austrian Science Fund FWF I 516Austrian Science Fund FWF P 21292
6 · The paper itself

Abstract

Several pathogens induce propulsive actin comet tails in cells they invade to disseminate their infection. They achieve this by recruiting factors for actin nucleation, the Arp2/3 complex, and polymerization regulators from the host cytoplasm. Owing to limited information on the structural organization of actin comets and in particular the spatial arrangement of filaments engaged in propulsion, the underlying mechanism of pathogen movement is currently speculative and controversial. Using electron tomography we have resolved the three-dimensional architecture of actin comet tails propelling baculovirus, the smallest pathogen yet known to hijack the actin motile machinery. Comet tail geometry was also mimicked in mixtures of virus capsids with purified actin and a minimal inventory of actin regulators. We demonstrate that propulsion is based on the assembly of a fishbone-like array of actin filaments organized in subsets linked by branch junctions, with an average of four filaments pushing the virus at any one time. Using an energy-minimizing function we have simulated the structure of actin comet tails as well as the tracks adopted by baculovirus in infected cells in vivo. The results from the simulations rule out gel squeezing models of propulsion and support those in which actin filaments are continuously tethered during branch nucleation and polymerization. Since Listeria monocytogenes, Shigella flexneri, and Vaccinia virus among other pathogens use the same common toolbox of components as baculovirus to move, we suggest they share the same principles of actin organization and mode of propulsion.

Indexed as

Models, StatisticalActin CytoskeletonActin-Related Protein 2-3 ComplexAnimalsBaculoviridaeComet AssayElectron Microscope TomographyGene ExpressionGenes, ReporterGoldfishGreen Fluorescent ProteinsHeLa CellsHumansLuminescent ProteinsMelanoma, ExperimentalRed Fluorescent ProteinActin-Related Protein 2-3 ComplexGreen Fluorescent ProteinsLuminescent ProteinsRed Fluorescent Protein

Identifiers

PMID24453943
PMCPMC3891563
OpenAlexW2018399608

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.