Dataset Information

Inner membrane complex proteomics reveals a palmitoylation cascade regulating intraerythrocytic development of malaria parasite

ABSTRACT: Malaria is caused by infection of the erythrocytes by the parasites Plasmodium. Inside the erythrocytes, the parasites grow and multiply via schizogony, an unconventional cell division mode. The Inner Membrane Complex (IMC), an organelle located beneath the plasma membrane of the parasites, is essential for schizogony, serving as the platform for protein anchorage. However, the protein compositions of IMC and their localization determinants remain unclear. Here we used biotin ligase (TurboID)-based proximity labelling and quantitative mass spectrometry to compile the proteome of the schizont IMC of rodent malaria parasite Plasmodium yoelii. In total, the IMC proteome consisting of 488 proteins were identified. 19 of the 22 selected candidates were confirmed to localize in the IMC, indicating good reliability. In light of the existing palmitome of Plasmodium falciparum, 136 proteins of the P. yoelii IMC proteome are potentially palmitoylated. We further identified DHHC2 the major resident palmitoyl-acyl-transferase of the IMC. Conditional depletion of DHHC2 led to defective schizont segmentation and growth arrest in vitro and in vivo. DHHC2 was found to palmitoylate two critical IMC proteins CDPK1 and GAP45 for their IMC localization. In summary, this study reports a comprehensive inventory of P. yoelii IMC proteins and demonstrates a central role of DHHC2 governing IMC localization of proteins during the schizont development.

ORGANISM(S): Plasmodium Yoelii Yoelii 17xnl

SUBMITTER: Jing Yuan

PROVIDER: PXD028193 | iProX | Fri Jul 01 00:00:00 BST 2022

REPOSITORIES: iProX

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Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite.

Qian Pengge P Wang Xu X Zhong Chuan-Qi CQ Wang Jiaxu J Cai Mengya M Nguitragool Wang W Li Jian J Cui Huiting H Yuan Jing J

eLife 20220701

Malaria is caused by infection of the erythrocytes by the parasites <i>Plasmodium</i>. Inside the erythrocytes, the parasites multiply via schizogony, an unconventional cell division mode. The inner membrane complex (IMC), an organelle located beneath the parasite plasma membrane, serving as the platform for protein anchorage, is essential for schizogony. So far, the complete repertoire of IMC proteins and their localization determinants remain unclear. Here we used biotin ligase (TurboID)-based ...[more]

PMID: 35775739

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Project description:The ability of Leishmania to survive in their insect or mammalian host is dependent upon an ability to sense and adapt to changes in the microenvironment. However, little is known about the molecular mechanisms underlying the parasite response to environmental changes, such as nutrient availability. To elucidate nutrient stress response pathways in Leishmania donovani, we have used purine starvation as the paradigm. The salvage of purines from the host milieu is obligatory for parasite replication; nevertheless, purine-starved parasites can persist in culture without supplementary purine for over 3 months, indicating that the response to purine starvation is robust and engenders parasite survival under conditions of extreme scarcity. To understand metabolic reprogramming during purine starvation we have employed global approaches. Whole proteome comparisons between purine-starved and purine-replete parasites over a 6-48 h span have revealed a temporal and coordinated response to purine starvation. Purine transporters and enzymes involved in acquisition at the cell surface are upregulated within a few hours of purine removal from the media, while other key purine salvage components are upregulated later in the time-course and more modestly.Â After 48 h, the proteome of purine-starved parasites is extensively remodeled and adaptations to purine stress appear tailored to deal with both purine deprivation and general stress. To probe the molecular mechanisms affecting proteome remodeling in response to purine starvation, comparative RNA-seq analyses, qRT-PCR, and luciferase reporter assays were performed on purine-starved versus purine-replete parasites.Â While the regulation of a minority of proteins tracked with changes at the mRNA level, for many regulated proteins it appears that proteome remodeling during purine stress occurs primarily via translational and post-translational mechanisms. One mRNA sample from each of Purine-Starved and Purine-Replete cells were analyzed using SL RNA-Seq methodology

Dataset Information

Inner membrane complex proteomics reveals a palmitoylation cascade regulating intraerythrocytic development of malaria parasite

Publications

Inner membrane complex proteomics reveals a palmitoylation regulation critical for intraerythrocytic development of malaria parasite.

Similar Datasets

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