ArticlePLoS pathogens2017
Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.
Article in PLoS pathogens, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 35 citations in OpenAlex.
- Plasmodium knowlesi tryptophan-rich antigen 40.1 binds human erythrocyte spectrin alpha.PLoS neglected tropical diseases · 2026Article
- Article
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Contact Dynamics of CytoadheringACS infectious diseases · 2025Article
- Cytoadhesion of Plasmodium falciparum-Infected Red Blood Cells Changes the Expression of Cytokine-, Histone- and Antiviral Protein-Encoding Genes in Brain Endothelial Cells.Molecular microbiology · 2024Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023Review
- CD36-A Host Receptor Necessary for Malaria Parasites to Establish and Maintain Infection.Microorganisms · 2022Review
- The Medicines for Malaria Venture Malaria Box contains inhibitors of protein secretion in Plasmodium falciparum blood stage parasites.Traffic (Copenhagen, Denmark) · 2022Article
- Genetics of cerebral malaria: pathogenesis, biomarkers and emerging therapeutic interventions.Cell & bioscience · 2022Review
- A particle-based computational model to analyse remodelling of the red blood cell cytoskeleton during malaria infections.PLoS computational biology · 2022Article
- Genetic Diversity, Repeat Motifs, and Natural Selection at the C-Terminal Knob-Associated Histidine Rich Protein (KAHRP) ofJournal of tropical medicine · 2022Article
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- Unique Endomembrane Systems and Virulence in Pathogenic Protozoa.Life (Basel, Switzerland) · 2021Review
- Structures of the Plasmodium falciparum heat-shock protein 70-x ATPase domain in complex with chemical fragments identify conserved and unique binding sites.Acta crystallographica. Section F, Structural biology communications · 2021Article
- Adhesion between P. falciparum infected erythrocytes and human endothelial receptors follows alternative binding dynamics under flow and febrile conditions.Scientific reports · 2020Article
- Cerebral Plasmodium falciparum malaria: The role of PfEMP1 in its pathogenesis and immunity, and PfEMP1-based vaccines to prevent it.Immunological reviews · 2020Review
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- The knob protein KAHRP assembles into a ring-shaped structure that underpins virulence complex assembly.PLoS pathogens · 2019Article
- Single-molecule imaging and quantification of the immune-variant adhesin VAR2CSA on knobs ofCommunications biology · 2019Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) and Knob-associated Histidine-rich Protein (KAHRP) are directly linked to malaria pathology. PfEMP1 and KAHRP cluster on protrusions (knobs) on the P. falciparum-infected erythrocyte surface and enable pathogenic cytoadherence of infected erythrocytes to the host microvasculature, leading to restricted blood flow, oxygen deprivation and damage of tissues. Here we characterize the interactions of PfEMP1 and KAHRP with host erythrocyte spectrin using biophysical, structural and computational approaches. These interactions assist knob formation and, thus, promote cytoadherence. We show that the folded core of the PfEMP1 cytosolic domain interacts broadly with erythrocyte spectrin but shows weak, residue-specific preference for domain 17 of α spectrin, which is proximal to the erythrocyte cytoskeletal junction. In contrast, a protein sequence repeat region in KAHRP preferentially associates with domains 10-14 of β spectrin, proximal to the spectrin-ankyrin complex. Structural models of PfEMP1 and KAHRP with spectrin combined with previous microscopy and protein interaction data suggest a model for knob architecture.
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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.