Evidence map›Paper›PMID 28552953›Full record

ArticlePLoS pathogens2017

A unique profilin-actin interface is important for malaria parasite motility.

Catherine A Moreau, Saligram P Bhargav, Hirdesh Kumar, Katharina A Quadt, Henni Piirainen, Léanne Strauss, Jessica Kehrer, Martin Streichfuss, Joachim P Spatz, Rebecca C Wade and 2 more

Open access · goldAbstract read
In one paragraph

Article in PLoS pathogens, 2017. 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
4.8field-weighted citation impact, top 4% 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, 67 citations in OpenAlex.

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  19. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
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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

12 authors at 3 institutions in 3 countries.

Catherine A MoreauIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-3412-2981
Saligram P BhargavIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.
Hirdesh KumarIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-8488-3001
Katharina A QuadtIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-4134-3379
Henni PiirainenBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.
Léanne StraussIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.ORCID http://orcid.org/0000-0002-0680-593X
Jessica KehrerIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.ORCID http://orcid.org/0000-0001-5084-3485
Martin StreichfussIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.
Joachim P SpatzInstitute for Physical Chemistry, Biophysical Chemistry, Heidelberg University, Heidelberg, Germany.ORCID http://orcid.org/0000-0003-3419-9807
Rebecca C WadeMolecular and Cellular Modeling Group, Heidelberg Institute for Theoretical Studies (HITS), Heidelberg, Germany.ORCID http://orcid.org/0000-0001-5951-8670
Inari KursulaBiocenter Oulu and Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland.ORCID http://orcid.org/0000-0001-5236-7056
Friedrich FrischknechtIntegrative Parasitology, Center for Infectious Diseases, Heidelberg University Medical School, Heidelberg, Germany.
Heidelberg University · DEUniversity of Bergen · NOUniversity of Oulu · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Profilin is an actin monomer binding protein that provides ATP-actin for incorporation into actin filaments. In contrast to higher eukaryotic cells with their large filamentous actin structures, apicomplexan parasites typically contain only short and highly dynamic microfilaments. In apicomplexans, profilin appears to be the main monomer-sequestering protein. Compared to classical profilins, apicomplexan profilins contain an additional arm-like β-hairpin motif, which we show here to be critically involved in actin binding. Through comparative analysis using two profilin mutants, we reveal this motif to be implicated in gliding motility of Plasmodium berghei sporozoites, the rapidly migrating forms of a rodent malaria parasite transmitted by mosquitoes. Force measurements on migrating sporozoites and molecular dynamics simulations indicate that the interaction between actin and profilin fine-tunes gliding motility. Our data suggest that evolutionary pressure to achieve efficient high-speed gliding has resulted in a unique profilin-actin interface in these parasites.

Indexed as

ActinsAnimalsCell MovementFemaleHumansMalariaMice, Inbred C57BLPlasmodium bergheiProfilinsProtein BindingProtozoan ProteinsSporozoitesActinsProfilinsProtozoan Proteins

Identifiers

PMID28552953
PMCPMC5464670
OpenAlexW2617016583

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.