37 results found
    1. Evolutionary Biology
    2. Microbiology and Infectious Disease

    Apicomplexan-like parasites are polyphyletic and widely but selectively dependent on cryptic plastid organelles

    Jan Janouškovec et al.
    Apicomplexan-like parasites originated several times independently and many of them contain cryptic plastid organelles, which demonstrate that the parasites evolved from photosynthetic algae.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    Identification of cryptic subunits from an apicomplexan ATP synthase

    Diego Huet et al.
    A phylum-specific ATP synthase subunit is needed for proper mitochondrial function and stability of the complex in Toxoplasma gondii.
    1. Structural Biology and Molecular Biophysics
    2. Evolutionary Biology

    An atomic-resolution view of neofunctionalization in the evolution of apicomplexan lactate dehydrogenases

    Jeffrey I Boucher et al.
    The convergent evolution of unusually strict substrate specificity in apicomplexan LDHs arose by classic neofunctionalization of a duplicated MDH gene via few mutations of large effect.
    1. Microbiology and Infectious Disease

    Modifications at K31 on the lateral surface of histone H4 contribute to genome structure and expression in apicomplexan parasites

    Fabien Sindikubwabo et al.
    A versatile acetylation-methylation switch at lysine 31 on the lateral surface of histone H4 contributes to chromatin structure in apicomplexan parasites.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    Toxoplasma gondii F-actin forms an extensive filamentous network required for material exchange and parasite maturation

    Javier Periz et al.
    In contrast to current knowledge that predicts that apicomplexan actin is unconventional, use of Chromobodies demonstrate that Toxoplasma F-actin forms a long, stable, highly dynamic tubular network that is required for material transfer and parasite maturation.
    1. Microbiology and Infectious Disease

    Elucidating the mitochondrial proteome of Toxoplasma gondii reveals the presence of a divergent cytochrome c oxidase

    Azadeh Seidi et al.
    The proteins found in the mitochondria of apicomplexan parasites, including key proteins involved in energy generation, are very different from mitochondrial proteins of the animals these parasites infect.
    1. Biochemistry and Chemical Biology
    2. Microbiology and Infectious Disease

    Small molecule inhibition of apicomplexan FtsH1 disrupts plastid biogenesis in human pathogens

    Katherine Amberg-Johnson et al.
    An unbiased chemical screen identifies the AAA+ membrane metalloprotease FtsH1 as a novel apicoplast biogenesis factor and druggable antimalarial target.
    1. Structural Biology and Molecular Biophysics
    2. Microbiology and Infectious Disease

    Malaria parasite CelTOS targets the inner leaflet of cell membranes for pore-dependent disruption

    John R Jimah et al.
    The structure, function and mechanism of the malaria vaccine candidate CelTOS reveal a unique pore-forming and membrane-disrupting protein with specificity for the inner leaflet of host and vector cells.
    1. Microbiology and Infectious Disease

    A druggable secretory protein maturase of Toxoplasma essential for invasion and egress

    Sunil Kumar Dogga et al.
    An aspartyl protease is essential for the lytic cycle of Toxoplasma gondii and is involved in the maturation of proteins critical for invasion and egress, and it can be targeted selectively with an ethylamine scaffold based peptidomimetic inhibitor.
    1. Cell Biology
    2. Microbiology and Infectious Disease

    Formin-2 drives polymerisation of actin filaments enabling segregation of apicoplasts and cytokinesis in Plasmodium falciparum

    Johannes Felix Stortz et al.
    Formin-2 controls spatiotemporal polymerisation of actin filaments, a common mechanism used by apicomplexans for effective segregation of essential chloroplast-like organelles called apicoplasts, and additionally for daughter formation in Plasmodium falciparum.

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