apicomplexa; parasite; toxoplasma gondii; plasmodium falciparum; plasmodium berghei; motility; Plasmodium; Toxoplasma; invasion; division; motor; adhesin; actin; protease
Mueller Christina, Klages Natacha, Jacot Damien, Santos M Joana, Cabrera Ana, Gilberger W. Tim, Dubremetz Jean Fracois, Soldati-Favre Dominique (2013), The Toxoplasma Protein ARO Mediates the Apical Positioning of Rhoptry Organelles, a Prerequisite for Host Cell Invasion, in Cell Host & Microbe
, 13, 289-301.
Jacot Damien, Daher Wassim, Soldati-Favre Dominique (2013), Toxoplasma gondii myosin F, an essential motor for centrosomes positioning and apicoplast inheritance, in EMBO Journal
, 32, 1702-1716.
Marchant Jan, Cowper Ben, Liu Yan, Lai Livia, Pinzan Camila, Marq Jean Baptiste, Friedrich Nikolas, Sawmynaden Kovilen, Liew Lloyd, Chai Wengang, Childs Robert A, Saouros Savvas, Simpson Peter, Roque Barreira Maria Cristina, Feizi Ten, Soldati-Favre Dominique, Matthews Stephen (2012), Galactose recognition by the apicomplexan parasite Toxoplasma gondii., in The Journal of biological chemistry
, 287(20), 16720-16733.
Daher W, Klages N, Carlier MF, Soldati-Favre D (2012), Molecular Characterization of Toxoplasma gondii Formin 3, an Actin Nucleator Dispensable for Tachyzoite Growth and Motility, in EUKARYOTIC CELL
, 11(3), 343-352.
Skillman KM, Daher W, Ma CI, Soldati-Favre D, Sibley LD (2012), Toxoplasma gondii Profilin Acts Primarily To Sequester G-Actin While Formins Efficiently Nucleate Actin Filament Formation in Vitro, in BIOCHEMISTRY
, 51(12), 2486-2495.
Santos JM, Ferguson DJP, Blackman MJ, Soldati-Favre D (2011), Intramembrane Cleavage of AMA1 Triggers Toxoplasma to Switch from an Invasive to a Replicative Mode, in SCIENCE
, 331(6016), 473-477.
Polonais V, Foth BJ, Chinthalapudi K, Marq JB, Manstein DJ, Soldati-Favre D, Frenal K (2011), Unusual Anchor of a Motor Complex (MyoD-MLC2) to the Plasma Membrane of Toxoplasma gondii, in TRAFFIC
, 12(3), 287-300.
Daher Wassim, Plattner Fabienne, Carlier Marie France, Soldati-Favre Dominique (2010), Concerted Action of Two Formins in Gliding Motility and Host Cell Invasion by Toxoplasma gondii, in PloS Pathogens
, 6, e1001132-e1001146.
Frenal K, Polonais V, Marq JB, Stratmann R, Limenitakis J, Soldati-Favre D (2010), Functional Dissection of the Apicomplexan Glideosome Molecular Architecture, in CELL HOST & MICROBE
, 8(4), 343-357.
Sheiner L, Santos JM, Klages N, Parussini F, Jemmely N, Friedrich N, Ward GE, Soldati-Favre D (2010), Toxoplasma gondii transmembrane microneme proteins and their modular design, in MOLECULAR MICROBIOLOGY
, 77(4), 912-929.
Protozoan parasites belonging to the phylum of Apicomplexa are of enormous medical and veterinary significance, being responsible for a wide variety of diseases in human and animals, including malaria, toxoplasmosis, coccidiosis and cryptosporidiosis. Members of Apicomplexa are obligate intracellular parasites that have elaborated a unique and powerful mode of host cell entry. In the absence of locomotive organelles such as cilia or flagella, the invasive forms of these parasites exhibit an unusual form of substrate-dependent motility that is essential for host cell invasion and establishment of infection. Genetics studies have established that gliding motility and cell penetration by T. gondii needs intact parasite actin filaments (Dobrowolski and Sibley, 1996) and is powered by the action an essential class XIV myosin motor, which propels the parasite into host cells (Meissner et al., 2002b). Drugs that interfere with actin polymerization or stabilize actin filaments have profound effects on motility (Wetzel et al., 2003), yet the mechanism by which Apicomplexa control actin polymerization is unknown. Gliding is also associated with the discharge of several complexes of proteins (MICs) that are stored in the secretory organelles called micronemes. The MICs complexes are released on parasite surface upon a raise in parasite intracellular calcium level, they bind to host cell receptors and contribute critically to attachment, motility and invasion. Remarkably, most MICs are proteolytically cleaved during their biogenesis and/or post-exocytosis. Microneme protein protease 1 (MPP1) a rhomboid protease, is responsible for the intramembrane proteolytic cleavage leading to the release of the MICs from the parasite surface and indirect evidence suggest that this activity is essential for invasion in T. gondii (Brossier et al., 2003) and in P. falciparum (O'Donnell R et al., 2006). Despite some major progress a number of unresolved issues still persist: how is F-actin dynamics regulated? How many myosin motors contribute to the three forms of Toxoplasma motility during invasion? What is the molecular basis of T. gondii broad host range specificity? What is the mechanistic significance of microneme proteins shedding during invasion?Toxoplasma is an attractive model system due to its ease of experimental use, excellent tools for cellular and even biochemical studies, and well-developed genetic systems (Roos et al., 1994) and because the gliding mechanism is very conserved, the major findings hold true for other members of the Phylum including Plasmodium species responsible for malaria.