Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites
AuthorCyrklaff, M; Kudryashev, M; Leis, A; Leonard, K; Baumeister, W; Menard, R; Meissner, M; Frischknecht, F
Source TitleJournal of Experimental Medicine
PublisherROCKEFELLER UNIV PRESS
University of Melbourne Author/sLeis, Andrew
Document TypeJournal Article
CitationsCyrklaff, M., Kudryashev, M., Leis, A., Leonard, K., Baumeister, W., Menard, R., Meissner, M. & Frischknecht, F. (2007). Cryoelectron tomography reveals periodic material at the inner side of subpellicular microtubules in apicomplexan parasites. JOURNAL OF EXPERIMENTAL MEDICINE, 204 (6), pp.1281-1287. https://doi.org/10.1084/jem.20062405.
Access StatusOpen Access
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.
- Click on "Export Reference in RIS Format" and choose "open with... Endnote".
- Click on "Export Reference in RIS Format". Login to Refworks, go to References => Import References