ArticleBiochimica et biophysica acta2015
Interactions between Plasmodium falciparum skeleton-binding protein 1 and the membrane skeleton of malaria-infected red blood cells.
Article in Biochimica et biophysica acta, 2015. 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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Who cites it
21 citing papers in PubMed, 29 citations in OpenAlex.
- Plasmodium knowlesi tryptophan-rich antigen 40.1 binds human erythrocyte spectrin alpha.PLoS neglected tropical diseases · 2026Article
- G6PD deficiency and the exportome of plasmodium falciparum FCB-2: A comparative analysis utilizing one-dimensional blue-native electrophoresis and timstof mass spectrometry.Parasitology research · 2026Article
- Molecular Players at the Sorting Stations of Malaria ParasiteCurrent protein & peptide science · 2024Review
- Identification of ExportedMicroorganisms · 2022Article
- Budding pouches and associated bubbles: 3D visualization of exo-membrane structures inFrontiers in cellular and infection microbiology · 2022Article
- PfAP2-EXP2, an Essential Transcription Factor for the Intraerythrocytic Development ofFrontiers in cell and developmental biology · 2021Article
- The role of vascular endothelium and exosomes in human protozoan parasitic diseases.Vessel plus · 2020Article
- A High-Resolution Map of SBP1 Interactomes in Plasmodium falciparum-infected Erythrocytes.iScience · 2019Article
- Genetic conflicts with Plasmodium parasites and functional constraints shape the evolution of erythrocyte cytoskeletal proteins.Scientific reports · 2018Article
- The Plasmodium falciparum transcriptome in severe malaria reveals altered expression of genes involved in important processes including surface antigen-encoding var genes.PLoS biology · 2018Article
- Repetitive sequences in malaria parasite proteins.FEMS microbiology reviews · 2017Review
- The Plasmodium falciparum exported protein PF3D7_0402000 binds to erythrocyte ankyrin and band 4.1.Molecular and biochemical parasitology · 2017Article
- Article
- Tryptophan-rich domains of Plasmodium falciparum SURFINMalaria journal · 2017Article
- Host-Parasite Interactions in Human Malaria: Clinical Implications of Basic Research.Frontiers in microbiology · 2017Review
- Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Microbiology and molecular biology reviews : MMBR · 2016Review
- A single point in protein trafficking by Plasmodium falciparum determines the expression of major antigens on the surface of infected erythrocytes targeted by human antibodies.Cellular and molecular life sciences : CMLS · 2016Article
- Host cell remodeling by pathogens: the exomembrane system in Plasmodium-infected erythrocytes.FEMS microbiology reviews · 2016Review
- Article
- The influence of host genetics on erythrocytes and malaria infection: is there therapeutic potential?Malaria journal · 2015Review
Corrections and comments
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Authors and funding
13 authors at 3 institutions in 2 countries.
Funding
Abstract
During development inside red blood cells (RBCs), Plasmodium falciparum malaria parasites export proteins that associate with the RBC membrane skeleton. These interactions cause profound changes to the biophysical properties of RBCs that underpin the often severe and fatal clinical manifestations of falciparum malaria. P. falciparum erythrocyte membrane protein 1 (PfEMP1) is one such exported parasite protein that plays a major role in malaria pathogenesis since its exposure on the parasitised RBC surface mediates their adhesion to vascular endothelium and placental syncytioblasts. En route to the RBC membrane skeleton, PfEMP1 transiently associates with Maurer's clefts (MCs), parasite-derived membranous structures in the RBC cytoplasm. We have previously shown that a resident MC protein, skeleton-binding protein 1 (SBP1), is essential for the placement of PfEMP1 onto the RBC surface and hypothesised that the function of SBP1 may be to target MCs to the RBC membrane. Since this would require additional protein interactions, we set out to identify binding partners for SBP1. Using a combination of approaches, we have defined the region of SBP1 that binds specifically to defined sub-domains of two major components of the RBC membrane skeleton, protein 4.1R and spectrin. We show that these interactions serve as one mechanism to anchor MCs to the RBC membrane skeleton, however, while they appear to be necessary, they are not sufficient for the translocation of PfEMP1 onto the RBC surface. The N-terminal domain of SBP1 that resides within the lumen of MCs clearly plays an essential, but presently unknown role in this process.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.