ArticleThe Journal of biological chemistry2012
Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- Global Proteomic Profiling of Cerebral Malaria-Infected Erythrocytes Reveals a Specific PfEMP1 Expression Pattern.Molecular & cellular proteomics : MCP · 2026Article
- Article
- Antibody levels to variant and conservedFrontiers in immunology · 2025Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Variable Surface Antigens ofProtein and peptide letters · 2024Review
- Natural immunity to malaria preferentially targets the endothelial protein C receptor-binding regions of PfEMP1s.mSphere · 2023Article
- Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023Review
- Association between Predicted Effects ofInternational journal of molecular sciences · 2021Article
- Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerization.The Journal of biological chemistry · 2020Article
- Investigating a Plasmodium falciparum erythrocyte invasion phenotype switch at the whole transcriptome level.Scientific reports · 2020Article
- Interaction Analysis of aFrontiers in microbiology · 2020Article
- Host Cytoskeleton Remodeling throughout the Blood Stages of Plasmodium falciparum.Microbiology and molecular biology reviews : MMBR · 2019Review
- A dynamically interacting flexible loop assists oligomerisation of the Caenorhabditis elegans centriolar protein SAS-6.Scientific reports · 2019Article
- Interaction between theMolecular biology of the cell · 2018Article
- Protein-Specific Features Associated with Variability in Human Antibody Responses toThe American journal of tropical medicine and hygiene · 2018Article
- SURGE complex of Plasmodium falciparum in the rhoptry-neck (SURFIN4.2-RON4-GLURP) contributes to merozoite invasion.PloS one · 2018Article
- Repetitive sequences in malaria parasite proteins.FEMS microbiology reviews · 2017Review
- Structural analysis of P. falciparum KAHRP and PfEMP1 complexes with host erythrocyte spectrin suggests a model for cytoadherent knob protrusions.PLoS pathogens · 2017Article
- Article
- Expansion of Lysine-rich Repeats in Plasmodium Proteins Generates Novel Localization Sequences That Target the Periphery of the Host Erythrocyte.The Journal of biological chemistry · 2016Article
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5 authors.
Funding
Abstract
Plasmodium falciparum-infected red blood cells adhere to endothelial cells, thereby obstructing the microvasculature. Erythrocyte adherence is directly associated with severe malaria and increased disease lethality, and it is mediated by the PfEMP1 family. PfEMP1 clustering in knob-like protrusions on the erythrocyte membrane is critical for cytoadherence, however the molecular mechanisms behind this system remain elusive. Here, we show that the intracellular domains of the PfEMP1 family (ATS) share a unique molecular architecture, which comprises a minimal folded core and extensive flexible elements. A conserved flexible segment at the ATS center is minimally restrained by the folded core. Yeast-two-hybrid data and a novel sequence analysis method suggest that this central segment contains a conserved protein interaction epitope. Interestingly, ATS in solution fails to bind the parasite knob-associated histidine-rich protein (KAHRP), an essential cytoadherence component. Instead, we demonstrate that ATS associates with PFI1780w, a member of the Plasmodium helical interspersed sub-telomeric (PHIST) family. PHIST domains are widespread in exported parasite proteins, however this is the first specific molecular function assigned to any variant of this family. We propose that PHIST domains facilitate protein interactions, and that the conserved ATS epitope may be targeted to disrupt the parasite cytoadherence system.
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