Back to Search
Start Over
Motility in blastogregarines (Apicomplexa): Native and drug-induced organisation of Siedleckia nematoides cytoskeletal elements
- Source :
- PLoS ONE, Vol 12, Iss 6, p e0179709 (2017), PLoS ONE
- Publication Year :
- 2017
- Publisher :
- Public Library of Science (PLoS), 2017.
-
Abstract
- Recent studies on motility of Apicomplexa concur with the so-called glideosome concept applied for apicomplexan zoites, describing a unique mechanism of substrate-dependent gliding motility facilitated by a conserved form of actomyosin motor and subpellicular microtubules. In contrast, the gregarines and blastogregarines exhibit different modes and mechanisms of motility, correlating with diverse modifications of their cortex. This study focuses on the motility and cytoskeleton of the blastogregarine Siedleckia nematoides Caullery et Mesnil, 1898 parasitising the polychaete Scoloplos cf. armiger (Muller, 1776). The blastogregarine moves independently on a solid substrate without any signs of gliding motility; the motility in a liquid environment (in both the attached and detached forms) rather resembles a sequence of pendular, twisting, undulation, and sometimes spasmodic movements. Despite the presence of key glideosome components such as pellicle consisting of the plasma membrane and the inner membrane complex, actin, myosin, subpellicular microtubules, micronemes and glycocalyx layer, the motility mechanism of S. nematoides differs from the glideosome machinery. Nevertheless, experimental assays using cytoskeletal probes proved that the polymerised forms of actin and tubulin play an essential role in the S. nematoides movement. Similar to Selenidium archigregarines, the subpellicular microtubules organised in several layers seem to be the leading motor structures in blastogregarine motility. The majority of the detected actin was stabilised in a polymerised form and appeared to be located beneath the inner membrane complex. The experimental data suggest the subpellicular microtubules to be associated with filamentous structures (= cross-linking protein complexes), presumably of actin nature.
- Subjects :
- 0301 basic medicine
food.ingredient
Gliding motility
Movement
Cell Membranes
Motility
lcsh:Medicine
Microtubules
Biochemistry
03 medical and health sciences
food
Contractile Proteins
Myosin
Parasite Groups
Medicine and Health Sciences
Trophozoites
Cytoskeleton
lcsh:Science
Actin
Pharmacology
Inner membrane complex
Microscopy
Multidisciplinary
biology
lcsh:R
Biology and Life Sciences
Proteins
Drugs
Cell Biology
030108 mycology & parasitology
Actins
Cell biology
Cytoskeletal Proteins
Cell Motility
030104 developmental biology
Tubulin
biology.protein
Selenidium
Parasitology
lcsh:Q
Cellular Structures and Organelles
Colchicine
Apicomplexa
Research Article
Subjects
Details
- Language :
- English
- ISSN :
- 19326203
- Volume :
- 12
- Issue :
- 6
- Database :
- OpenAIRE
- Journal :
- PLoS ONE
- Accession number :
- edsair.doi.dedup.....6744e5d8f3fffe7cfc2ee62f7e0d47b4