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  Plasmodium sporozoite motility is modulated by the turnover of discrete adhesion sites

Münter, S., Sabass, B., Selhuber-Unkel, C., Kudryashev, M., Hegge, S., Engel, U., et al. (2009). Plasmodium sporozoite motility is modulated by the turnover of discrete adhesion sites. Cell Host & Microbe, 6(6), 551-562. doi:10.1016/j.chom.2009.11.007.

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 Creators:
Münter, Sylvia1, Author
Sabass, Benedikt2, Author
Selhuber-Unkel, Christine3, Author
Kudryashev, Misha1, Author                 
Hegge, Stephan1, Author
Engel, Ulrike2, Author
Spatz, Joachim P.3, 4, Author           
Matuschewski, Kai1, Author
Schwarz, Ulrich S.1, 5, Author
Frischknecht, Friedrich1, Author
Affiliations:
1Parasitology, Department of Infectious Diseases, University of Heidelberg Medical School, Heidelberg, Germany, ou_persistent22              
2Bioquant, Nikon Imaging Center, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              
3Dept. New Materials and Biosystems, Max Planck Institute for Intelligent Systems, Max Planck Society, ou_1497649              
4University of Heidelberg, Department of Biophysical Chemistry, Heisenbergstr. 3, 70569 Stuttgart, Germany, ou_persistent22              
5Institute of Zoology, Theoretical Biophysics Group, University of Karlsruhe, 76131 Karlsruhe, Germany, ou_persistent22              

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 Abstract: Sporozoites are the highly motile stages of the malaria parasite injected into the host's skin during a mosquito bite. In order to navigate inside of the host, sporozoites rely on actin-dependent gliding motility. Although the major components of the gliding machinery are known, the spatiotemporal dynamics of the proteins and the underlying mechanism powering forward locomotion remain unclear. Here, we show that sporozoite motility is characterized by a continuous sequence of stick-and-slip phases. Reflection interference contrast and traction force microscopy identified the repeated turnover of discrete adhesion sites as the underlying mechanism of this substrate-dependent type of motility. Transient forces correlated with the formation and rupture of distinct substrate contact sites and were dependent on actin dynamics. Further, we show that the essential sporozoite surface protein TRAP is critical for the regulated formation and rupture of adhesion sites but is dispensable for retrograde capping.

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Language(s): eng - English
 Dates: 2009-10-212009-08-112009-11-192009-12-17
 Publication Status: Issued
 Pages: 12
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/j.chom.2009.11.007
PMID: 20006843
 Degree: -

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Title: Cell Host & Microbe
Source Genre: Journal
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Publ. Info: Cambridge, MA 02139 : Elsevier Inc.
Pages: - Volume / Issue: 6 (6) Sequence Number: - Start / End Page: 551 - 562 Identifier: ISSN: 1931-3128
CoNE: https://pure.mpg.de/cone/journals/resource/1931-3128