ArticlePLoS pathogens2013
Identification of new PNEPs indicates a substantial non-PEXEL exportome and underpins common features in Plasmodium falciparum protein export.
Article in PLoS pathogens, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.
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Who cites it
87 citing papers in PubMed, 165 citations in OpenAlex.
- Plasmepsins as Antimalarial Drug Targets-Then, Now, and the Future.Medicinal research reviews · 2026Review
- Physiological febrile heat stress increases cytoadhesion through increased protein trafficking ofeLife · 2026Article
- MAHRP2 is required for tether formation and cytoadherence inFrontiers in cellular and infection microbiology · 2026Article
- Article
- MAP-X reveals distinct protein complex dynamics across Plasmodium falciparum blood stages.Nature microbiology · 2025Article
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Genome-wide gene expression profiles throughout human malaria parasite liver stage development in humanized mice.Nature microbiology · 2025Article
- Flp/Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Article
- Novel Ion Channel Genes in Malaria Parasites.Genes · 2024Review
- Article
- Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors.Journal of cell science · 2023Article
- Specific Cryptosporidium antigens associate with reinfection immunity and protection from cryptosporidiosis.The Journal of clinical investigation · 2023Article
- VAR2CSA Ectodomain Labeling inBio-protocol · 2023Article
- Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023Review
- PTEX helps efficiently traffic haemoglobinases to the food vacuole in Plasmodium falciparum.PLoS pathogens · 2023Article
- Chemogenomic Profiling of a Plasmodium falciparum Transposon Mutant Library Reveals Shared Effects of Dihydroartemisinin and Bortezomib on Lipid Metabolism and Exported Proteins.Microbiology spectrum · 2023Article
- Formation of ER-lumenal intermediates during export of Plasmodium proteins containing transmembrane-like hydrophobic sequences.PLoS pathogens · 2023Article
- Advances in understanding red blood cell modifications by Babesia.PLoS pathogens · 2022Review
27 more citing papers are in PubMed but not listed here.
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Authors and funding
15 authors at 4 institutions in 3 countries.
Funding
Abstract
Malaria blood stage parasites export a large number of proteins into their host erythrocyte to change it from a container of predominantly hemoglobin optimized for the transport of oxygen into a niche for parasite propagation. To understand this process, it is crucial to know which parasite proteins are exported into the host cell. This has been aided by the PEXEL/HT sequence, a five-residue motif found in many exported proteins, leading to the prediction of the exportome. However, several PEXEL/HT negative exported proteins (PNEPs) indicate that this exportome is incomplete and it remains unknown if and how many further PNEPs exist. Here we report the identification of new PNEPs in the most virulent malaria parasite Plasmodium falciparum. This includes proteins with a domain structure deviating from previously known PNEPs and indicates that PNEPs are not a rare exception. Unexpectedly, this included members of the MSP-7 related protein (MSRP) family, suggesting unanticipated functions of MSRPs. Analyzing regions mediating export of selected new PNEPs, we show that the first 20 amino acids of PNEPs without a classical N-terminal signal peptide are sufficient to promote export of a reporter, confirming the concept that this is a shared property of all PNEPs of this type. Moreover, we took advantage of newly found soluble PNEPs to show that this type of exported protein requires unfolding to move from the parasitophorous vacuole (PV) into the host cell. This indicates that soluble PNEPs, like PEXEL/HT proteins, are exported by translocation across the PV membrane (PVM), highlighting protein translocation in the parasite periphery as a general means in protein export of malaria parasites.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.