ArticleEukaryotic cell2011
An erythrocyte cytoskeleton-binding motif in exported Plasmodium falciparum proteins.
Article in Eukaryotic cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 32 citations in OpenAlex.
- 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
- MAHRP2 is required for tether formation and cytoadherence inFrontiers in cellular and infection microbiology · 2026Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Identification of ExportedMicroorganisms · 2022Article
- Exported J domain proteins of the human malaria parasite.Frontiers in molecular biosciences · 2022Review
- 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 the J Domain Protein Family in the Survival and Pathogenesis of Plasmodium falciparum.Advances in experimental medicine and biology · 2021Review
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- Plasmodium helical interspersed subtelomeric family-an enigmatic piece of the Plasmodium biology puzzle.Parasitology research · 2019Review
- The Plasmodium falciparum MESA erythrocyte cytoskeleton-binding (MEC) motif binds to erythrocyte ankyrin.Molecular and biochemical parasitology · 2019Article
- The Plasmodium falciparum exported protein PF3D7_0402000 binds to erythrocyte ankyrin and band 4.1.Molecular and biochemical parasitology · 2017Article
- Plasmodium Helical Interspersed Subtelomeric (PHIST) Proteins, at the Center of Host Cell Remodeling.Microbiology and molecular biology reviews : MMBR · 2016Review
- Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton.Cellular microbiology · 2016Article
- Genomes of cryptic chimpanzee Plasmodium species reveal key evolutionary events leading to human malaria.Nature communications · 2016Article
- Expression, Purification, and Biological Characterization of Babesia microti Apical Membrane Antigen 1.Infection and immunity · 2015Article
- Targeted disruption of a ring-infected erythrocyte surface antigen (RESA)-like export protein gene in Plasmodium falciparum confers stable chondroitin 4-sulfate cytoadherence capacity.The Journal of biological chemistry · 2014Article
- A conserved domain targets exported PHISTb family proteins to the periphery of Plasmodium infected erythrocytes.Molecular and biochemical parasitology · 2014Article
- Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane.Biochimica et biophysica acta · 2014Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Binding of exported malaria parasite proteins to the host cell membrane and cytoskeleton contributes to the morphological, functional, and antigenic changes seen in Plasmodium falciparum-infected erythrocytes. One such exported protein that targets the erythrocyte cytoskeleton is the mature parasite-infected erythrocyte surface antigen (MESA), which interacts with the N-terminal 30-kDa domain of protein 4.1R via a 19-residue sequence. We report here that the MESA erythrocyte cytoskeleton-binding (MEC) domain is present in at least 13 other P. falciparum proteins predicted to be exported to the host cell. An alignment of the putative cytoskeleton-binding sequences revealed a conserved aspartic acid at the C terminus that was omitted from the originally reported binding domain. Mutagenesis experiments demonstrated that this aspartic acid was required for the optimal binding of MESA to inside-out vesicles (IOVs) prepared from erythrocytes. Using pulldown assays, we characterized the binding of fragments encoding the MEC domains from PFE0040c/MESA and six other proteins (PF10_0378, PFA0675w, PFB0925w, PFD0095c, PFF1510w, and PFI1790w) to IOVs. All seven proteins bound to IOVs, with MESA showing the strongest affinity in saturation binding experiments. We further examined the interaction of the MEC domain proteins with components of the erythrocyte cytoskeleton and showed that MESA, PF10_0378, and PFA0675w coprecipitated full-length 4.1R from lysates prepared from IOVs. These data demonstrated that the MEC motif is present and functional in at least six other P. falciparum proteins that are exported to the host cell cytoplasm.
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