Pellicle formation in the malaria parasite

Kono, Maya; Heincke, Dorothee; Wilcke, Louisa; Wong, Tatianna Wai Ying; Bruns, C.; Herrmann, Susann; Spielmann, Tobias; Gilberger, Tim‐Wolf

doi:10.1242/jcs.181230

Cited by 28 publications

(43 citation statements)

References 35 publications

(51 reference statements)

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“…Very few basal localised proteins have been described in invasive stages in Plasmodium . Recently a transmembrane protein localising at the basal rim of nascent IMC was reported in blood stage parasites 6 . While many apically localised protein have been reported both in Toxoplasma and Plasmodium , very few have been characterised during ookinete or sporozoite stages 5 – 8 , 12 , 24 – 26 .…”

Section: Discussionmentioning

confidence: 99%

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Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

Saini

Zeeshan

Brady

et al. 2017

Sci Rep

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Plasmodium parasites, the causative agents of malaria, possess a distinctive membranous structure of flattened alveolar vesicles supported by a proteinaceous network, and referred to as the inner membrane complex (IMC). The IMC has a role in actomyosin-mediated motility and host cell invasion. Here, we examine the location, protein interactome and function of PhIL1, an IMC-associated protein on the motile and invasive stages of both human and rodent parasites. We show that PhIL1 is located in the IMC in all three invasive (merozoite, ookinete-, and sporozoite) stages of development, as well as in the male gametocyte and locates both at the apical and basal ends of ookinete and sporozoite stages. Proteins interacting with PhIL1 were identified, showing that PhIL1 was bound to only some proteins present in the glideosome motor complex (GAP50, GAPM1–3) of both P. falciparum and P. berghei. Analysis of PhIL1 function using gene targeting approaches indicated that the protein is required for both asexual and sexual stages of development. In conclusion, we show that PhIL1 is required for development of all zoite stages of Plasmodium and it is part of a novel protein complex with an overall composition overlapping with but different to that of the glideosome.

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Section: Discussionmentioning

confidence: 99%

“…A recent study has shown that a pellicle protein, BTP1 is localised to the basal rim of the IMC during P . falciparum schizogony and co-localises with MORN1 6 . The presence of MORN1 in our interactome data suggests that PhIL1 may also be part of the basal complex in P .…”

Section: Discussionmentioning

confidence: 99%

Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

Saini

Zeeshan

Brady

et al. 2017

Sci Rep

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“…This was key to understanding the mechanism of action of imidazopyrazines, a new antimalarial compound class that influence PPM development by blocking a lipid kinase involved in this process 15 . Furthermore, GFP-tagging of the PPM-localized putative sphingomyelin-synthethase (PfSMS1) allowed studying the interaction of the PPM with the inner membrane complex during blood stage development 16 . However, a similar PPM reporter parasite line for the mosquito and liver stages of the parasite has not so far been established.…”

Section: Introductionmentioning

confidence: 99%

A Plasmodium plasma membrane reporter reveals membrane dynamics by live-cell microscopy

Burda

Schaffner

Kaiser

et al. 2017

Sci Rep

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During asexual replication within the Anopheles mosquito and their vertebrate host, Plasmodium parasites depend on the generation of a massive amount of new plasma membrane to produce thousands of daughter parasites. How the parasite plasma membrane (PPM) is formed has mostly been studied by electron microscopy, which does not allow an insight into the dynamics of this process. We generated a Plasmodium berghei reporter parasite line by GFP-tagging of a non-essential PPM-localized protein, and followed plasma membrane development in living parasites through the entire Plasmodium life cycle. By generating double-fluorescent parasites in which the PPM is visualized in combination with the parasite endoplasmic reticulum, we show that membrane contact sites are formed between both membrane systems during oocyst and liver stage development that might be used to deliver lipids to the dramatically expanding PPM. In conclusion, we have established a powerful tool to follow PPM development in living parasites, which promises to greatly expand our knowledge of membrane biology in the Plasmodium parasite.

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“…The basal complex marker BTP1 has recently been shown to mark the basal rim of the forming IMC which can be seen as a contractile ring that advances in synchrony with plasma membrane invagination during cell division (Kono et al, ). Observation of the control parasites transfected with a BTP1‐GFP construct showed a labelled basal complex in segmented schizonts (Figure c(i)).…”

Section: Resultsmentioning

confidence: 99%

The malaria parasite Plasmodium falciparum Sortilin is essential for merozoite formation and apical complex biogenesis

Hallée

Counihan

Matthews

et al. 2018

Cellular Microbiology

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The inner membrane complex and the apical secretory organelles are defining features of apicomplexan parasites. Despite their critical roles, the mechanisms behind the biogenesis of these structures in the malaria parasite Plasmodium falciparum are still poorly defined. We here show that decreasing expression of the P. falciparum homologue of the conserved endolysomal escorter Sortilin-VPS10 prevents the formation of the inner membrane complex and abrogates the generation of new merozoites. Moreover, protein trafficking to the rhoptries, the micronemes, and the dense granules is disrupted, which leads to the accumulation of apical complex proteins in the endoplasmic reticulum and the parasitophorous vacuole. We further show that protein export to the erythrocyte and transport through the constitutive secretory pathway are functional. Taken together, our results suggest that the malaria parasite P. falciparum Sortilin has potentially broader functions than most of its other eukaryotic counterparts.

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Pellicle formation in the malaria parasite

Cited by 28 publications

References 35 publications

Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

Photosensitized INA-Labelled protein 1 (PhIL1) is novel component of the inner membrane complex and is required for Plasmodium parasite development

A Plasmodium plasma membrane reporter reveals membrane dynamics by live-cell microscopy

The malaria parasite Plasmodium falciparum Sortilin is essential for merozoite formation and apical complex biogenesis

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