Novel Structure In the Pellicular Complex of Plasmodium Falciparum Gametocytes1

Kaidoh, Toshiyuki; Nath, Jayasree; Okoye, Vincent; Aikawa, Masamichi

doi:10.1111/j.1550-7408.1993.tb04916.x

Cited by 10 publications

(5 citation statements)

References 11 publications

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“…Similar patchworks of sub-pellicular membrane have been described in the IMC of the invasive stages of P. falciparum, as well as in Toxoplasma and other apicomplexa (Bannister et al, 2000;Raibaud et al, 2001). Another early transmission electron microscopy study identified protein 'crosslinks' running perpendicular to the microtubule network (Kaidoh et al, 1993). We suggest that the GAP50-GFP-labelled IMC 'stripes' represent IMC cisternae laid down as rectangular plates, whereas the gaps represent proteinaceous material that holds the cisternae and the microtubules in place.…”

Section: Discussionmentioning

confidence: 75%

Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes

Dearnley

Yeoman

Hanssen

et al. 2012

Journal of Cell Science

115

161

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SummaryThe most virulent of the human malaria parasites, Plasmodium falciparum, undergoes a remarkable morphological transformation as it prepares itself for sexual reproduction and transmission via mosquitoes. Indeed P. falciparum is named for the unique falciform or crescent shape of the mature sexual stages. Once the metamorphosis is completed, the mature gametocyte releases from sequestration sites and enters the circulation, thus making it accessible to feeding mosquitoes. Early ultrastructural studies showed that gametocyte elongation is driven by the assembly of a system of flattened cisternal membrane compartments underneath the parasite plasma membrane and a supporting network of microtubules. Here we describe the molecular composition and origin of the sub-pellicular membrane complex, and show that it is analogous to the inner membrane complex, an organelle with structural and motor functions that is well conserved across the apicomplexa. We identify novel crosslinking elements that might help stabilize the inner membrane complex during gametocyte development. We show that changes in gametocyte morphology are associated with an increase in cellular deformability and postulate that this enables the gametocytes to circulate in the bloodstream without being detected and removed by the mechanical filtering mechanisms in the spleen of the host.

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Section: Discussionmentioning

confidence: 75%

Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes

Dearnley

Yeoman

Hanssen

et al. 2012

Journal of Cell Science

115

161

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“…Until now it is poorly understood, how the IMC plates are joined together. A proteinaceous material in P. falciparum gametocytes has been identified by electron microscopy (Kaidoh et al ., ) and cryo‐electron tomography (Dearnley et al ., ) running perpendicular to the microtubule network and corresponding probably to the transverse sutures encircling the gametocytes (Meszoely et al ., ). It was recently suggested that these proteinaceous sutures might provide a means of stabilizing the IMC and the subpellicular microtubule network (Dearnley et al ., ).…”

Section: Discussionmentioning

confidence: 99%

Identification and characterization ofToxoplasma SIP, a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite

et al. 2014

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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 Toxoplasma 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.

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“…2J,K). Plasmodium parasites lack an intact conoid, but retain the apical polar rings, which probably nucleate subpellicular microtubule polymerization (Russell and Sinden, 1982;Kaidoh et al, 1993). As daughter scaffolds elongate, DNA replication is completed, and the nucleus lobulates (Fig.…”

Section: Discussionmentioning

confidence: 99%

Organellar dynamics during the cell cycle of Toxoplasma gondii

Nishi

Murray

et al. 2008

Journal of Cell Science

250

341

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results in partitioning of the apicoplast, nucleus, endoplasmic reticulum, and finally the mitochondrion, which enters the developing daughters rapidly, but only very late during the division cycle. The specialized secretory organelles (micronemes and rhoptries) form de novo. This distinctive pattern of replication -in which organellar segregation spans ~75% of the cell cycle, completely encompassing S phase -suggests an unusual mechanism of cell cycle regulation. Supplementary material available online at

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Novel Structure In the Pellicular Complex of Plasmodium Falciparum Gametocytes1

Cited by 10 publications

References 11 publications

Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes

Origin, composition, organization and function of the inner membrane complex of Plasmodium falciparum gametocytes

Identification and characterization ofToxoplasma SIP, a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite

Organellar dynamics during the cell cycle of Toxoplasma gondii

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