ArticlePloS one2017
The exported chaperone Hsp70-x supports virulence functions for Plasmodium falciparum blood stage parasites.
Article in PloS one, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 55 citations in OpenAlex.
- The DNA-binding protein PfAP2-V regulates erythrocyte invasion and pathogenesis of the human malaria parasite Plasmodium falciparum.Science China. Life sciences · 2026Article
- Article
- Promiscuous stimulation of HSP70 ATPase activity by parasite-derived J-domains.FEBS open bio · 2026Article
- 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
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Biochemistry of Heat Shock Proteins From Human Intracellular Protozoan Parasites as Diagnostic and Therapeutic Biomarkers.Biochemistry · 2025Review
- A Systematic Targeted Genetic Screen Identifies Proteins Involved in Cytoadherence of the Malaria Parasite P. falciparum.Molecular microbiology · 2025Article
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- Human granzyme B binds Plasmodium falciparum Hsp70-x and mediates antiplasmodial activity in vitro.Cell stress & chaperones · 2023Article
- HSP70 and their co-chaperones in the human malaria parasiteFrontiers in molecular biosciences · 2022Review
- Review
- Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence.PLoS pathogens · 2021Article
- Protein Sorting in Plasmodium Falciparum.Life (Basel, Switzerland) · 2021Review
- Structures of the Plasmodium falciparum heat-shock protein 70-x ATPase domain in complex with chemical fragments identify conserved and unique binding sites.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Transport mechanisms at the malaria parasite-host cell interface.PLoS pathogens · 2021Review
- Exported plasmodial J domain protein, PFE0055c, and PfHsp70-x form a specific co-chaperone-chaperone partnership.Cell stress & chaperones · 2021Article
- Role of Heat Shock Proteins in Immune Modulation in Malaria.Advances in experimental medicine and biology · 2021Article
- Heat Shock Proteins of Malaria: Highlights and Future Prospects.Advances in experimental medicine and biology · 2021Article
- Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 2021Article
Corrections and comments
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Authors and funding
16 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Malaria is caused by five different Plasmodium spp. in humans each of which modifies the host erythrocyte to survive and replicate. The two main causes of malaria, P. falciparum and P. vivax, differ in their ability to cause severe disease, mainly due to differences in the cytoadhesion of infected erythrocytes (IE) in the microvasculature. Cytoadhesion of P. falciparum in the brain leads to a large number of deaths each year and is a consequence of exported parasite proteins, some of which modify the erythrocyte cytoskeleton while others such as PfEMP1 project onto the erythrocyte surface where they bind to endothelial cells. Here we investigate the effects of knocking out an exported Hsp70-type chaperone termed Hsp70-x that is present in P. falciparum but not P. vivax. Although the growth of Δhsp70-x parasites was unaffected, the export of PfEMP1 cytoadherence proteins was delayed and Δhsp70-x IE had reduced adhesion. The Δhsp70-x IE were also more rigid than wild-type controls indicating changes in the way the parasites modified their host erythrocyte. To investigate the cause of this, transcriptional and translational changes in exported and chaperone proteins were monitored and some changes were observed. We propose that PfHsp70-x is not essential for survival in vitro, but may be required for the efficient export and functioning of some P. falciparum exported proteins.
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