ArticleCellular microbiology2020
EXP1 is required for organisation of EXP2 in the intraerythrocytic malaria parasite vacuole.
Article in Cellular microbiology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 58 citations in OpenAlex.
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- Evolutionary Rate Covariation Across Malaria Parasite Species Enables Inference of Protein Interactions.Genome biology and evolution · 2026Article
- The parasitophorous vacuole membrane of Toxoplasma gondii: A custom structural framing with smart interior plumbing for resource allocation.PLoS pathogens · 2026Review
- A role for the poly-asparagine repeat in the Plasmodium histone acetyltransferase, PfGCN5.Nature communications · 2026Article
- Gain-of-function PfAAT1 mutations compensate for impaired PfCRT function inResearch square · 2026Article
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- Evolutionary rate covariation across malaria parasite species enables inference of protein interactions.bioRxiv : the preprint server for biology · 2026Article
- A rapid, simple, and economical method for the isolation of ribosomes and translational machinery for structural and functional studies.Nature communications · 2025Article
- Pfs16: A Key Parasitophorous Vacuole Membrane Protein Crucial for Malaria Parasite Development and Transmission.The protein journal · 2025Review
- Identification of a divalent metal transporter required for cellular iron metabolism in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Identification of a divalent metal transporter required for cellular iron metabolism in malaria parasites.bioRxiv : the preprint server for biology · 2024Article
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- Novel Ion Channel Genes in Malaria Parasites.Genes · 2024Review
- Knock-sideways by inducible ER retrieval enables a unique approach for studyingProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Labeling strategies to track protozoan parasite proteome dynamics.Current opinion in chemical biology · 2023Review
- Genome-wide CRISPR screen identifies genes synthetically lethal with GRA17, a nutrient channel encoding gene in Toxoplasma.PLoS pathogens · 2023Article
- Plasmodium falciparum gametocytes display global chromatin remodelling during sexual differentiation.BMC biology · 2023Article
- An essential endoplasmic reticulum-resident N-acetyltransferase ortholog in Plasmodium falciparum.Journal of cell science · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Intraerythrocytic malaria parasites reside within a parasitophorous vacuole membrane (PVM) that closely overlays the parasite plasma membrane. Although the PVM is the site of several transport activities essential to parasite survival, the basis for organisation of this membrane system is unknown. Here, we performed proximity labeling at the PVM with BioID2, which highlighted a group of single-pass integral membrane proteins that constitute a major component of the PVM proteome but whose function remains unclear. We investigated EXP1, the longest known member of this group, by adapting a CRISPR/Cpf1 genome editing system to install the TetR-DOZI-aptamers system for conditional translational control. Importantly, although EXP1 was required for intraerythrocytic development, a previously reported in vitro glutathione S-transferase activity could not account for this essential EXP1 function in vivo. EXP1 knockdown was accompanied by profound changes in vacuole ultrastructure, including apparent increased separation of the PVM from the parasite plasma membrane and formation of abnormal membrane structures. Furthermore, although activity of the Plasmodium translocon of exported proteins was not impacted by depletion of EXP1, the distribution of the translocon pore-forming protein EXP2 but not the HSP101 unfoldase was substantially altered. Collectively, our results reveal a novel PVM defect that indicates a critical role for EXP1 in maintaining proper organisation of EXP2 within the PVM.
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