ArticleScientific reports2019
Cholesterol bound Plasmodium falciparum co-chaperone 'PFA0660w' complexes with major virulence factor 'PfEMP1' via chaperone 'PfHsp70-x'.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 42 citations in OpenAlex.
- FIKK1, a member of the FIKK kinase family, phosphorylates VAR2CSA and regulates adhesion of Plasmodium falciparum-infected erythrocytes to the placental receptor CSA.PLoS pathogens · 2026Article
- MAHRP2 is required for tether formation and cytoadherence inFrontiers in cellular and infection microbiology · 2026Article
- The J Domain Proteins ofInternational journal of molecular sciences · 2024Review
- Distribution of malaria parasite-derived phosphatidylcholine in the infected erythrocyte.mSphere · 2023Article
- Article
- Timing of dense granule biogenesis in asexual malaria parasites.Microbiology (Reading, England) · 2023Article
- TheFrontiers in molecular biosciences · 2023Review
- Article
- Deletion of the Plasmodium falciparum exported protein PTP7 leads to Maurer's clefts vesiculation, host cell remodeling defects, and loss of surface presentation of EMP1.PLoS pathogens · 2022Article
- Review
- Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022Review
- The role of cholesterol in invasion and growth of malaria parasites.Frontiers in cellular and infection microbiology · 2022Review
- Co-chaperone involvement in knob biogenesis implicates host-derived chaperones in malaria virulence.PLoS pathogens · 2021Article
- Unique Endomembrane Systems and Virulence in Pathogenic Protozoa.Life (Basel, Switzerland) · 2021Review
- Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells.Cellular microbiology · 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
- Heat Shock Proteins as Targets for Novel Antimalarial Drug Discovery.Advances in experimental medicine and biology · 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
- Chaperoning of asparagine repeat-containing proteins inJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2020Review
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Lethality of Plasmodium falciparum caused malaria results from 'cytoadherence', which is mainly effected by exported Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) family. Several exported P. falciparum proteins (exportome) including chaperones alongside cholesterol rich microdomains are crucial for PfEMP1 translocation to infected erythrocyte surface. An exported Hsp40 (heat shock protein 40) 'PFA0660w' functions as a co-chaperone of 'PfHsp70-x', and these co-localize to specialized intracellular mobile structures termed J-dots. Our studies attempt to understand the function of PFA0660w-PfHsp70-x chaperone pair using recombinant proteins. Biochemical assays reveal that N and C-terminal domains of PFA0660w and PfHsp70-x respectively are critical for their activity. We show the novel direct interaction of PfHsp70-x with the cytoplasmic tail of PfEMP1, and binding of PFA0660w with cholesterol. PFA0660w operates both as a chaperone and lipid binding molecule via its separate substrate and cholesterol binding sites. PfHsp70-x interacts with cholesterol bound PFA0660w and PfEMP1 simultaneously in vitro to form a complex. Collectively, our results and the past literature support the hypothesis that PFA0660w-PfHsp70-x chaperone pair assists PfEMP1 transport across the host erythrocyte through cholesterol containing 'J-dots'. These findings further the understanding of PfEMP1 export in malaria parasites, though their in vivo validation remains to be performed.
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