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

Moreau, C., Bhargav, S. P., Kumar, H., Quadt, K., Piirainen, H., Strauss, L., et al. (2017). A unique profilin-actin interface is important for malaria parasite motility. PLoS Pathogens, 13(5): e1006412, pp. 1-26. doi:10.1371/journal.ppat.1006412.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-002D-792A-2 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-002E-5E69-C
Genre: Journal Article

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 Creators:
Moreau, Catherine, Author
Bhargav, Saligram P., Author
Kumar, Hirdesh, Author
Quadt, Katherina1, Author           
Piirainen, Henni, Author
Strauss, Léanne, Author
Kehrer, Jessica, Author
Streichfuss, Martin1, 2, Author           
Spatz, Joachim P.1, 2, Author           
Wade, Rebecca, Author
Kursula, Inari, Author
Frischknecht, Friedrich, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2017-01-252017-05-162017-05-26
 Publication Status: Published online
 Pages: 26
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1371/journal.ppat.1006412
URI: https://www.ncbi.nlm.nih.gov/pubmed/28552953
URI: https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5464670/
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Title: PLoS Pathogens
  Other : PLoS Pathog.
Source Genre: Journal
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Publ. Info: San Francisco, CA : Public Library of Science
Pages: - Volume / Issue: 13 (5) Sequence Number: e1006412 Start / End Page: 1 - 26 Identifier: ISSN: 1553-7366
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000018830