The Journal of Experimental Medicine
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Published online June 11, 2007
doi:10.1084/jem.20062405
The Journal of Experimental Medicine, Vol. 204, No. 6, 1281-1287
The Rockefeller University Press, 0022-1007 $30.00
© 2007 Cyrklaff et al.
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BRIEF DEFINITIVE REPORT

 Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites

Marek Cyrklaff1, Mikhail Kudryashev2, Andrew Leis1, Kevin Leonard3, Wolfgang Baumeister1, Robert Menard4, Markus Meissner2, and Friedrich Frischknecht2

1 Department of Molecular Structural Biology, Max Planck Institute for Biochemistry, 82152, Martinsried, Germany
2 Department of Parasitology, Hygiene Institute, University of Heidelberg Medical School, 69120 Heidelberg, Germany
3 European Molecular Biology Laboratory-European Bioinformatics Institute, Wellcome Trust Genome Campus, Cambridge CB10 1SD, UK
4 Malaria Biology and Genetics Unit, Institut Pasteur, 75015 Paris, France

CORRESPONDENCE Marek Cyrklaff: cyrklaff{at}biochem.mpg.de OR Friedrich Frischknecht: freddy.frischknecht{at}med.uni-heidelberg.de

Microtubules are dynamic cytoskeletal structures important for cell division, polarity, and motility and are therefore major targets for anticancer and antiparasite drugs. In the invasive forms of apicomplexan parasites, which are highly polarized and often motile cells, exceptionally stable subpellicular microtubules determine the shape of the parasite, and serve as tracks for vesicle transport. We used cryoelectron tomography to image cytoplasmic structures in three dimensions within intact, rapidly frozen Plasmodium sporozoites. This approach revealed microtubule walls that are extended at the luminal side by an additional 3 nm compared to microtubules of mammalian cells. Fourier analysis revealed an 8-nm longitudinal periodicity of the luminal constituent, suggesting the presence of a molecule interacting with tubulin dimers. In silico generation and analysis of microtubule models confirmed this unexpected topology. Microtubules from extracted sporozoites and Toxoplasma gondii tachyzoites showed a similar density distribution, suggesting that the putative protein is conserved among Apicomplexa and serves to stabilize microtubules.


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