ArticleCellular microbiology2021
Characterisation of complexes formed by parasite proteins exported into the host cell compartment of Plasmodium falciparum infected red blood cells.
Article in Cellular microbiology, 2021. 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, 27 citations in OpenAlex.
- Evolutionary Rate Covariation Across Malaria Parasite Species Enables Inference of Protein Interactions.Genome biology and evolution · 2026Article
- The spatial proteome of the Plasmodium falciparum schizont illuminates the composition and evolutionary trajectories of its organelles.Nature communications · 2026Article
- Physiological febrile heat stress increases cytoadhesion through increased protein trafficking ofeLife · 2026Article
- Evolutionary rate covariation across malaria parasite species enables inference of protein interactions.bioRxiv : the preprint server for biology · 2026Article
- MAHRP2 is required for tether formation and cytoadherence inFrontiers in cellular and infection microbiology · 2026Article
- Beyond VAR2CSA: redefining the antigenic landscape of placental malaria vaccines.Open research Africa · 2026Review
- Shared host, distinct invaders: metabolomic footprints of plasmodium and babesia in host red cells.Current opinion in hematology · 2025Review
- A Systematic Targeted Genetic Screen Identifies Proteins Involved in Cytoadherence of the Malaria Parasite P. falciparum.Molecular microbiology · 2025Article
- A scalable CRISPR-Cas9 gene editing system facilitates CRISPR screens in the malaria parasite Plasmodium berghei.Nucleic acids research · 2025Article
- APEX2-based proximity proteomic analysis identifies candidate interactors for Plasmodium falciparum knob-associated histidine-rich protein in infected erythrocytes.Scientific reports · 2024Article
- Time-resolved proximity biotinylation implicates a porin protein in export of transmembrane malaria parasite effectors.Journal of cell science · 2023Article
- Article
- Knobs, Adhesion, and Severe Falciparum Malaria.Tropical medicine and infectious disease · 2023Review
- PTEX helps efficiently traffic haemoglobinases to the food vacuole in Plasmodium falciparum.PLoS pathogens · 2023Article
- Down the membrane hole: Ion channels in protozoan parasites.PLoS pathogens · 2022Review
- The Medicines for Malaria Venture Malaria Box contains inhibitors of protein secretion in Plasmodium falciparum blood stage parasites.Traffic (Copenhagen, Denmark) · 2022Article
- Deletion of the Plasmodium falciparum exported protein PTP7 leads to Maurer's clefts vesiculation, host cell remodeling defects, and loss of surface presentation of EMP1.PLoS pathogens · 2022Article
- The Plasmodium falciparum parasitophorous vacuole protein P113 interacts with the parasite protein export machinery and maintains normal vacuole architecture.Molecular microbiology · 2022Article
- Structured to conquer: transport across the Plasmodium parasitophorous vacuole.Current opinion in microbiology · 2021Review
- Unique Endomembrane Systems and Virulence in Pathogenic Protozoa.Life (Basel, Switzerland) · 2021Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
During its intraerythrocytic life cycle, the human malaria parasite Plasmodium falciparum supplements its nutritional requirements by scavenging substrates from the plasma through the new permeability pathways (NPPs) installed in the red blood cell (RBC) membrane. Parasite proteins of the RhopH complex: CLAG3, RhopH2, RhopH3, have been implicated in NPP activity. Here, we studied 13 exported proteins previously hypothesised to interact with RhopH2, to study their potential contribution to the function of NPPs. NPP activity assays revealed that the 13 proteins do not appear to be individually important for NPP function, as conditional knockdown of these proteins had no effect on sorbitol uptake. Intriguingly, reciprocal immunoprecipitation assays showed that five of the 13 proteins interact with all members of the RhopH complex, with PF3D7_1401200 showing the strongest association. Mass spectrometry-based proteomics further identified new protein complexes; a cytoskeletal complex and a Maurer's clefts/J-dot complex, which overall helps clarify protein-protein interactions within the infected RBC (iRBC) and is suggestive of the potential trafficking route of the RhopH complex itself to the RBC membrane.
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Registered trials
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