ArticleScientific reports2016
Trafficking of the exported P. falciparum chaperone PfHsp70x.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 29 citations in OpenAlex.
- Is the Association of Granzyme B and the Exported Parasite Hsp70 a Possible Trojan Horse of Severe Malaria?Advances in experimental medicine and biology · 2026Article
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- The mature N-termini ofmBio · 2023Article
- Review
- HSP70 and their co-chaperones in the human malaria parasiteFrontiers in molecular biosciences · 2022Review
- Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022Review
- Trafficking and Association ofPathogens (Basel, Switzerland) · 2021Article
- Cholesterol bound Plasmodium falciparum co-chaperone 'PFA0660w' complexes with major virulence factor 'PfEMP1' via chaperone 'PfHsp70-x'.Scientific reports · 2019Article
- Article
- Membrane heat shock protein 70: a theranostic target for cancer therapy.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Immunoproteomics of Plasmodium falciparum-infected red blood cell membrane fractions.Memorias do Instituto Oswaldo Cruz · 2017Article
- The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.PloS one · 2017Article
- Article
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Authors and funding
14 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium falciparum extensively modifies its chosen host cell, the mature human erythrocyte. This remodelling is carried out by parasite-encoded proteins that are exported into the host cell. To gain access to the human red blood cell, these proteins must cross the parasitophorous vacuole, a membrane bound compartment surrounding the parasite that is generated during the invasion process. Many exported proteins carry a so-called PEXEL/HT signal that directs their transport. We recently reported the unexpected finding of a species-restricted parasite-encoded Hsp70, termed PfHsp70x, which is exported into the host erythrocyte cytosol. PfHsp70x lacks a classical PEXEL/HT motif, and its transport appears to be mediated by a 7 amino acid motif directly following the hydrophobic N-terminal secretory signal. In this report, we analyse this short targeting sequence in detail. Surprisingly, both a reversed and scrambled version of the motif retained the capacity to confer protein export. Site directed mutagenesis of glutamate residues within this region leads to a block of protein trafficking within the lumen of the PV. In contrast to PEXEL-containing proteins, the targeting signal is not cleaved, but appears to be acetylated. Furthermore we show that, like other exported proteins, trafficking of PfHsp70x requires the vacuolar translocon, PTEX.
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