Cell motility in basal apicomplexans from marine invertebrates
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| Year of publication | 2013 |
| Type | Conference abstract |
| MU Faculty or unit | |
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| Description | Phylum Apicomplexa belongs to the most medically and economically monitored group of Protista and comprises exclusively parasites of vertebrates as well as invertebrates. Among other important pathogens, this group includes Plasmodium falciparum and Toxoplasma gondii responsible for dangerous human diseases (malaria, toxoplasmosis). It was already reported in numerous recent studies that the highly motile apicomplexan invasive stages, the so-called zoites, use a unique mechanism of substrate dependent gliding motility facilitated by a conserved form of acto-myosin motor (the “glideosome” concept). Nevertheless, there exist early emerging groups, such as blastogregarines, archigregarines, eugregarines, neogregarines and protococcidia, in which the exact mechanism of cell motility still remains enigmatic. These organisms exhibit various forms of motility, including rolling, bending, waving or pendular movement, gliding motility and finally movements similar to peristalsis. This variability seems to represent specific adaptations to parasitism in hosts living in different environmental conditions, and correlates with significant modifications of the cell cortex and connected cytoskeletal components. Our research focuses on experimental, electronmicroscopic and immunofluorescent analysis of subcellular structures that are considered responsible for cell motility. The studied species septate eugregarine Cephaloidophora cf. communis from crustacean Balanus balanus, blastogregarine Siedleckia nematoides from polychaete Scoloplos (Scoloplos) armiger, archigregarine Selenidium sp. and aseptate eugregarine Polyrhabdina sp. from polychaete Pygospio elegans are investigated for the presence of cytoskeletal elements and motor proteins such as actin, myosin and alpha-tubulin. Research also includes experimental application of drugs that are known to influence the polymerization of actin and tubulin (JAS, cytochalasin D, oryzalin), their distribution and modify motility. |
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