Characterization of the subpellicular network, a filamentous membrane skeletal component in the parasite Toxoplasma gondii.
Electron microscopic examination of detergent-extracted Toxoplasma tachyzoites reveals the presence of a mechanically stable cytoskeletal structure associated with the pellicle of this parasite. This structure, composed of interwoven 8-10 nm filaments, is associated with the cytoplasmic face of the pellicle and surrounds the microtubule-based cytoskeleton. Two protein components of this network, TgIMC1 and TgIMC2, were identified. Both are novel proteins, but have a resemblance to mammalian filament proteins in that they are predicted to have extended, coiled-coil domains. TgIMC1 is also homologous to articulins, the major components of the membrane skeleton of algae and free-living protists. A homologue of TgIMC1 in the related malaria parasite Plasmodium falciparum was also identified suggesting the presence of structurally similar membrane skeletons in all apicomplexan parasites. We suggest that the subpellicular network, formed by TgIMC1 and 2 in Toxoplasma gondii and related parasites, plays a role in the determination of cell shape and is a source of mechanical strength.
Mann
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Department of Cell Biology, University of Alabama at Birmingham, BBRB 540, 845 19th Street South, 35294-2170, Birmingham, AL, USA.
Beckers
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D000595:Amino Acid Sequence; D000818:Animals; D003001:Cloning, Molecular; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism / Q000648:ultrastructure*; D008854:Microscopy, Electron; D016253:Microscopy, Immunoelectron; D008969:Molecular Sequence Data; D015800:Protozoan Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA; D014122:Toxoplasma / Q000235:genetics / Q000378:metabolism / Q000648:ultrastructure*
D003598:Cytoskeletal Proteins; C435912:IMC1 protein, Toxoplasma gondii; C435913:IMC2 protein, Toxoplasma gondii; D015800:Protozoan Proteins