Open AccessIdentification and characterization of T oxoplasma SIP , a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite
Author(s) -
Lentini Gaelle,
KongHap Marie,
El Hajj Hiba,
Francia Maria,
Claudet Cyrille,
Striepen Boris,
Dubremetz JeanFrançois,
Lebrun Maryse
Publication year - 2015
Publication title -
cellular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.542
H-Index - 138
eISSN - 1462-5822
pISSN - 1462-5814
DOI - 10.1111/cmi.12337
Subject(s) - biology , gliding motility , cytoskeleton , microbiology and biotechnology , motility , myosin , actin , apicomplexa , cytoplasm , membrane ruffling , microneme , toxoplasma gondii , virulence , intermediate filament , cell , gene , genetics , immunology , antibody , malaria , plasmodium falciparum
Summary Apicomplexa possess a complex pellicle that is composed of a plasma membrane and a closely apposed inner membrane complex ( IMC ) that serves as a support for the actin‐myosin motor required for motility and host cell invasion. The IMC consists of longitudinal plates of flattened vesicles, fused together and lined on the cytoplasmic side by a subpellicular network of intermediate filament‐like proteins. The spatial organization of the IMC has been well described by electron microscopy, but its composition and molecular organization is largely unknown. Here, we identify a novel protein of the IMC cytoskeletal network in T oxoplasma gondii , called TgSIP , and conserved among apicomplexan parasites. To finely pinpoint the localization of TgSIP , we used structured illumination super‐resolution microscopy and revealed that it likely decorates the transverse sutures of the plates and the basal end of the IMC . This suggests that TgSIP might contribute to the organization or physical connection among the different components of the IMC . We generated a T . gondii SIP deletion mutant and showed that parasites lacking TgSIP are significantly shorter than wild‐type parasites and show defects in gliding motility, invasion and reduced infectivity in mice.