TY - JOUR

T1 - Motility in blastogregarines (Apicomplexa)

T2 - Native and drug-induced organisation of Siedleckia nematoides cytoskeletal elements

AU - Valigurová, Andrea

AU - Vaškovicová, Naděžda

AU - Diakin, Andrei

AU - Paskerova, Gita G.

AU - Simdyanov, Timur G.

AU - Kováčiková, Magdaléna

N1 - Funding Information: AV, AD and MK were funded from the project from Czech Science Foundation No. GBP505/12/G112 (ECIP - Centre of excellence) and acknowledge support from the Department of Botany and Zoology, Faculty of Science, Masaryk University, towards the preparation of this manuscript. NV was supported by MEYS CR (LO1212) and its infrastructure by MEYS CR and EC (CZ.1.05/2.1.00/01.0017). TGS was supported by the grants from the Council of President of the Russian Federation NSh-7770.2016.4 and from the Russian Foundation of Basic Researches 15-29-02601. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. The authors would like to thank the staff of the White Sea Biological Station of Lomonosov Moscow State University (WSBS MSU) and the Marine Biological Station of St. Petersburg State University (MBS SPbSU) for providing facilities for field sampling and material processing, as well as their kind and friendly approach. The authors are greatly indebted to the Laboratory of Electron Microscopy, Biology Centre CAS, supported by the Czech-BioImaging large RI project (LM2015062 funded by MEYS CR) for their support and technical assistance with obtaining of EM data presented in this paper. The present study also utilised equipment of core facility centres 'Culturing of microorganisms', 'Observatory of Environmental Safety' and 'Development of molecular and cell technologies' of St. Petersburg State University. Many thanks to Prof. Dominique Soldati-Favre (University of Geneva) for kindly providing the monoclonal anti-actin antibody. Publisher Copyright: © 2017 Valigurová et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Copyright: Copyright 2017 Elsevier B.V., All rights reserved.

PY - 2017/6

Y1 - 2017/6

N2 - 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 (Müller, 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.

AB - 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 (Müller, 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.

KW - actin

KW - cell motility

KW - colchicine

KW - cytochalasin D

KW - epicyte

KW - freeze-etching

KW - glycocalyx

KW - gregarine

KW - jasplakinolide

KW - micronemes

KW - myosin

KW - oryzalin

KW - pellicle

KW - subpellicularmicrotubules

KW - tubulin, ultrastructure

UR - http://www.scopus.com/inward/record.url?scp=85021248415&partnerID=8YFLogxK

U2 - 10.1371/journal.pone.0179709

DO - 10.1371/journal.pone.0179709

M3 - Article

C2 - 28640849

VL - 12

JO - PLoS ONE

JF - PLoS ONE

SN - 1932-6203

IS - 6

M1 - e0179709

ER -