ArticleCellular microbiology2019
The endoplasmic reticulum chaperone PfGRP170 is essential for asexual development and is linked to stress response in malaria parasites.
Article in Cellular microbiology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 26 citations in OpenAlex.
- Characterisation of the thermal and non-thermal stress conditions that activate the Plasmodium falciparum AP2-HS-dependent heat-shock response.PLoS pathogens · 2026Article
- 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
- Biochemical and biophysical characterization of Plasmodium falciparum glucose regulated protein 170.Scientific reports · 2025Article
- Extracellular Proteomic Profiling from the Erythrocytes Infected with Plasmodium Falciparum 3D7 Holds Promise for the Detection of Biomarkers.The protein journal · 2024Article
- Article
- Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors.Journal of cell science · 2023Article
- 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
- Plasmepsin X activates the PCRCR complex of Plasmodium falciparum by processing PfRh5 for erythrocyte invasion.Nature communications · 2023Article
- Review
- HSP70 and their co-chaperones in the human malaria parasiteFrontiers in molecular biosciences · 2022Review
- A heat-shock response regulated by the PfAP2-HS transcription factor protects human malaria parasites from febrile temperatures.Nature microbiology · 2021Article
- Some conditions apply: Systems for studying Plasmodium falciparum protein function.PLoS pathogens · 2021Review
- A redox-active crosslinker reveals an essential and inhibitable oxidative folding network in the endoplasmic reticulum of malaria parasites.PLoS pathogens · 2021Article
- The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells.Advances in experimental medicine and biology · 2021Review
- The Role of Hsp70s in the Development and Pathogenicity of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Article
- Heat Shock Proteins of Malaria: Highlights and Future Prospects.Advances in experimental medicine and biology · 2021Article
- Directing traffic: Chaperone-mediated protein transport in malaria parasites.Cellular microbiology · 2020Review
- Plastid biogenesis in malaria parasites requires the interactions and catalytic activity of the Clp proteolytic system.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- The endoplasmic reticulum chaperone PfGRP170 is essential for asexual development and is linked to stress response in malaria parasites.Cellular microbiology · 2019Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
The vast majority of malaria mortality is attributed to one parasite species: Plasmodium falciparum. Asexual replication of the parasite within the red blood cell is responsible for the pathology of the disease. In Plasmodium, the endoplasmic reticulum (ER) is a central hub for protein folding and trafficking as well as stress response pathways. In this study, we tested the role of an uncharacterised ER protein, PfGRP170, in regulating these key functions by generating conditional mutants. Our data show that PfGRP170 localises to the ER and is essential for asexual growth, specifically required for proper development of schizonts. PfGRP170 is essential for surviving heat shock, suggesting a critical role in cellular stress response. The data demonstrate that PfGRP170 interacts with the Plasmodium orthologue of the ER chaperone, BiP. Finally, we found that loss of PfGRP170 function leads to the activation of the Plasmodium eIF2α kinase, PK4, suggesting a specific role for this protein in this parasite stress response pathway.
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