ArticleBiochimica et biophysica acta2014
Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane.
Article in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed.
- Integrative proteomic profiling of malaria-derived microparticles: A mass spectrometry-based study.MalariaWorld journal · 2026Article
- Critical role of Babesia bovis spherical body protein 3 in ridge formation on infected red blood cells.PLoS pathogens · 2024Article
- Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023Review
- Identification of ExportedMicroorganisms · 2022Article
- A particle-based computational model to analyse remodelling of the red blood cell cytoskeleton during malaria infections.PLoS computational biology · 2022Article
- Quantifying the influences of radiation therapy on deformability of human red blood cells by dual-beam optical tweezers.RSC advances · 2021Article
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- Interplay between Attenuation- and Virulence-Factors ofPathogens (Basel, Switzerland) · 2019Review
- The knob protein KAHRP assembles into a ring-shaped structure that underpins virulence complex assembly.PLoS pathogens · 2019Article
- Genetic conflicts with Plasmodium parasites and functional constraints shape the evolution of erythrocyte cytoskeletal proteins.Scientific reports · 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
- Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.PLoS pathogens · 2017Article
- Host-Parasite Interactions in Human Malaria: Clinical Implications of Basic Research.Frontiers in microbiology · 2017Review
- Oxidative insult can induce malaria-protective trait of sickle and fetal erythrocytes.Nature communications · 2016Article
- Article
- 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
- Modeling cytoadhesion of Plasmodium falciparum-infected erythrocytes and leukocytes-common principles and distinctive features.FEBS letters · 2016Review
- Proteomic analysis of Plasmodium falciparum parasites from patients with cerebral and uncomplicated malaria.Scientific reports · 2016Article
- Environmental Correlation Analysis for Genes Associated with Protection against Malaria.Molecular biology and evolution · 2016Article
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Abstract
The malaria parasite Plasmodium falciparum exports a large number of proteins into the erythrocyte cytoplasm during the asexual intraerythrocytic stage of its life cycle. A subset of these proteins interacts with erythrocyte membrane skeletal proteins and grossly alters the structure and function of the membrane. Several of the exported proteins, such as PfEMP1, PfEMP3, RESA and KAHRP, interact with the preponderant erythrocyte skeleton protein, spectrin. Here we have searched for possible interaction of these four malaria proteins with another major erythrocyte skeleton protein, ankyrin R. We have shown that KAHRP, but none of the other three, binds to ankyrin R. We have mapped the binding site for ankyrin R to a 79-residue segment of the KAHRP sequence, and the reciprocal binding site for KAHRP in ankyrin R to a subdomain (D3) of the 89kDa ankyrin R membrane-binding domain. Interaction of intact ankyrin R with KAHRP was inhibited by the free D3 subdomain. When, moreover, red cells loaded with the soluble D3 subdomain were infected with P. falciparum, KAHRP secreted by the intraerythrocytic parasite no longer migrated to the host cell membrane, but remained diffusely distributed throughout the cytosol. Our findings suggest a potentially important role for interaction of KAHRP with red cell membrane skeleton in promoting the adhesion of malaria-infected red cells to endothelial surfaces, a central element in the pathophysiology of malaria.
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