ArticleNature2014
PTEX component HSP101 mediates export of diverse malaria effectors into host erythrocytes.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 164 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
164 citing papers in PubMed, 276 citations in OpenAlex.
- Plasmepsins as Antimalarial Drug Targets-Then, Now, and the Future.Medicinal research reviews · 2026Review
- Unpacking boxes: identification of novel inhibitors of malaria parasite invasion.International journal for parasitology. Drugs and drug resistance · 2026Article
- Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Article
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- A High-Throughput Inhibitor Screen Targeting CLAG3 Export and Membrane Insertion on Human Erythrocytes Infected with Malaria Parasites.Pathogens (Basel, Switzerland) · 2025Article
- Genome-wide gene expression profiles throughout human malaria parasite liver stage development in humanized mice.Nature microbiology · 2025Article
- Comparative 3D ultrastructure of Plasmodium falciparum gametocytes.Nature communications · 2025Article
- Malaria parasites require a divergent heme oxygenase for apicoplast gene expression and biogenesis.eLife · 2024Article
- Malaria parasites require a divergent heme oxygenase for apicoplast gene expression and biogenesis.bioRxiv : the preprint server for biology · 2024Article
- Flp/Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Article
- Novel Ion Channel Genes in Malaria Parasites.Genes · 2024Review
- Article
- Toxoplasma protein export and effector function.Nature microbiology · 2024Review
- Sequence elements within the PEXEL motif and its downstream region modulate PTEX-dependent protein export in Plasmodium falciparum.Traffic (Copenhagen, Denmark) · 2024Article
- The mature N-termini ofmBio · 2023Article
- Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors.Journal of cell science · 2023Article
- Profile of Daniel E. Goldberg.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
104 more citing papers are in PubMed but not listed here.
Corrections and comments
- Commented on by
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
To mediate its survival and virulence, the malaria parasite Plasmodium falciparum exports hundreds of proteins into the host erythrocyte. To enter the host cell, exported proteins must cross the parasitophorous vacuolar membrane (PVM) within which the parasite resides, but the mechanism remains unclear. A putative Plasmodium translocon of exported proteins (PTEX) has been suggested to be involved for at least one class of exported proteins; however, direct functional evidence for this has been elusive. Here we show that export across the PVM requires heat shock protein 101 (HSP101), a ClpB-like AAA+ ATPase component of PTEX. Using a chaperone auto-inhibition strategy, we achieved rapid, reversible ablation of HSP101 function, resulting in a nearly complete block in export with substrates accumulating in the vacuole in both asexual and sexual parasites. Surprisingly, this block extended to all classes of exported proteins, revealing HSP101-dependent translocation across the PVM as a convergent step in the multi-pathway export process. Under export-blocked conditions, association between HSP101 and other components of the PTEX complex was lost, indicating that the integrity of the complex is required for efficient protein export. Our results demonstrate an essential and universal role for HSP101 in protein export and provide strong evidence for PTEX function in protein translocation into the host cell.
Indexed as
Identifiers
What OpenQuestion holds
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.