ArticleThe Biochemical journal1996
Protein sorting in Plasmodium falciparum-infected red blood cells permeabilized with the pore-forming protein streptolysin O.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed, 180 citations in OpenAlex.
- Article
- Novel Ion Channel Genes in Malaria Parasites.Genes · 2024Review
- Article
- Sequence elements within the PEXEL motif and its downstream region modulate PTEX-dependent protein export in Plasmodium falciparum.Traffic (Copenhagen, Denmark) · 2024Article
- Red Blood Cell BCL-xMicroorganisms · 2022Article
- Article
- A revised mechanism for how Plasmodium falciparum recruits and exports proteins into its erythrocytic host cell.PLoS pathogens · 2022Article
- Trafficking and Association ofPathogens (Basel, Switzerland) · 2021Article
- Transport mechanisms at the malaria parasite-host cell interface.PLoS pathogens · 2021Review
- The Role of Malaria Parasite Heat Shock Proteins in Protein Trafficking and Remodelling of Red Blood Cells.Advances in experimental medicine and biology · 2021Review
- Role of Hsp90 in Plasmodium falciparum Malaria.Advances in experimental medicine and biology · 2021Article
- Plasmodium falciparum parasites exit the infected erythrocyte after haemolysis with saponin and streptolysin O.Parasitology research · 2020Article
- The genetic CaThe Journal of biological chemistry · 2020Article
- The parasitophorous vacuole of the blood-stage malaria parasite.Nature reviews. Microbiology · 2020Review
- EXP1 is required for organisation of EXP2 in the intraerythrocytic malaria parasite vacuole.Cellular microbiology · 2020Article
- A pan-apicomplexan phosphoinositide-binding protein acts in malarial microneme exocytosis.EMBO reports · 2019Article
- Article
- Characterization of a putative Plasmodium falciparum SAC1 phosphoinositide-phosphatase homologue potentially required for survival during the asexual erythrocytic stages.Scientific reports · 2017Article
- An exported protein-interacting complex involved in the trafficking of virulence determinants in Plasmodium-infected erythrocytes.Nature communications · 2017Article
- The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol.Cellular microbiology · 2017Article
5 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Plasmodium falciparum is an intracellular parasite of human red blood cells (RBCs). Like many other intracellular parasites, P. falciparum resides and develops within a parasitophorous vacuole which is bound by a membrane that separates the host cell cytoplasm from the parasite surface. Some parasite proteins are secreted into the vacuolar space and others are secreted, by an as yet poorly defined pathway, into the RBC cytosol. The transport of proteins from the parasite has been followed mainly using morphological methods. In search of an experimental system that would allow (i) dissection of the individual steps involved in transport from the parasite surface into the RBC cytosol, and (ii) an assessment of the molecular requirements for the process at the erythrocytic side of the vacuolar membrane, we permeabilized infected RBCs with the pore-forming protein streptolysin O using conditions which left the vacuole intact. The distribution of two parasite proteins which served as markers for the vacuolar space and the RBC cytosol respectively was analysed morphologically and biochemically. In permeabilized RBCs the two marker proteins were sorted to the same compartments as in intact RBCs. The protein which was destined for the RBC cytosol traversed the vacuolar space before it was translocated across the vacuolar membrane. Protein transport could be arrested in the vacuole by removing the RBC cytosol. Translocation across the vacuolar membrane required ATP and a protein source at the erythrocytic face of the membrane, but it was independent of the intracellular ionic milieu of the RBC.
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