Cytoskeleton and motility in the archigregarine Selenidium pygospionis (Apicomplexa)
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| Year of publication | 2018 |
| Type | Conference abstract |
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| Description | Based on their pleomorphic features, archigregarines are considered to represent the most ancestral gregarines or even apicomplexans as a whole. Trophozoites of Selenidium pygospionis from marine polychaete Pygospio elegans Claparede, 1863 are covered by a typical apicomplexan three-layered pellicle (composed of the plasma membrane and inner membrane complex) that is folded into 28 broad and low folds separated by grooves. The pellicle is underlain by longitudinally oriented subpellicular microtubules, arranged in a single layer, the continuity of which is interrupted only under the grooves where micropores are situated [2]. The role of subpellicular microtubules on bending motility performed by trophozoites of S. pygospionis in cooperation with actomyosin motor heave been studied by different approaches (experimental motility assay on archigregarines isolated from host intestine, combination of light, electron and confocal microscopic analyses). In experimentally affected archigregarines treated with actin-modifying (jasplakinolide, cytochalasin D) or microtubule-destroying (oryzalin and colchicine) drugs, suppression or complete cessation of motility was documented. Electron microscopic analyses did not show any significant ultrastructural changes after jasplakinolide or cytochalasin D treatment. On the contrary, an obvious disappearance of normally continuous outermost microtubule set was observed in archigregarines incubated with drugs causing tubulin degradation (depolymerisation). This observation is in accordance with modifications of motility pattern monitored by the light microscopy and is additionally supported by results from confocal laser scanning microscopy, where immunolabelling revealed the presence of tubulin clusters instead of compact microtubules. |
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