ArticleProceedings of the National Academy of Sciences of the United States of America2021
Native structure of the RhopH complex, a key determinant of malaria parasite nutrient acquisition.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 33 citations in OpenAlex.
- Article
- Physiological febrile heat stress increases cytoadhesion through increased protein trafficking ofeLife · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- An overview of the interconnectedness of the PEXEL and non-PEXEL mediated protein export iniScience · 2025Review
- Structure of endogenous Pfs230:Pfs48/45 in complex with potent malaria transmission-blocking antibodies.bioRxiv : the preprint server for biology · 2025Article
- A High-Throughput Inhibitor Screen Targeting CLAG3 Export and Membrane Insertion on Human Erythrocytes Infected with Malaria Parasites.Pathogens (Basel, Switzerland) · 2025Article
- Utilisation of an in vivo malaria model to provide functional proof for RhopH1/CLAG essentiality and conserved orthology with P. falciparum.Journal of biomedical science · 2025Article
- MagIC beads for scarce macromolecules.eLife · 2025Article
- Review
- Novel Ion Channel Genes in Malaria Parasites.Genes · 2024Review
- Proteome-Wide Identification of RNA-dependent proteins and an emerging role for RNAs in Plasmodium falciparum protein complexes.Nature communications · 2024Article
- Critical interdependencies between Plasmodium nutrient flux and drugs.Trends in parasitology · 2023Review
- Unique Properties of Nutrient Channels onPathogens (Basel, Switzerland) · 2023Review
- Article
- Structures and comparison of endogenous 2-oxoglutarate and pyruvate dehydrogenase complexes from bovine kidney.Cell discovery · 2022Article
- New cryoEM Methods for Studying Native Biological Complexes,Microscopy and microanalysis : the official journal of Microscopy Society of America, Microbeam Analysis Society, Microscopical Society of Canada · 2022Article
- Epigenetics of malaria parasite nutrient uptake, but why?Trends in parasitology · 2022Review
- Article
- Structural parasitology of the malaria parasite Plasmodium falciparum.Trends in biochemical sciences · 2022Review
- Label-free visual proteomics: Coupling MS- and EM-based approaches in structural biology.Molecular cell · 2022Review
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
The RhopH complex is implicated in malaria parasites' ability to invade and create new permeability pathways in host erythrocytes, but its mechanisms remain poorly understood. Here, we enrich the endogenous RhopH complex in a native soluble form, comprising RhopH2, CLAG3.1, and RhopH3, directly from parasite cell lysates and determine its atomic structure using cryo-electron microscopy (cryo-EM), mass spectrometry, and the cryoID program. CLAG3.1 is positioned between RhopH2 and RhopH3, which both share substantial binding interfaces with CLAG3.1 but make minimal contacts with each other. The forces stabilizing individual subunits include 13 intramolecular disulfide bonds. Notably, CLAG3.1 residues 1210 to 1223, previously predicted to constitute a transmembrane helix, are embedded within a helical bundle formed by residues 979 to 1289 near the C terminus of CLAG3.1. Buried in the core of the RhopH complex and largely shielded from solvent, insertion of this putative transmembrane helix into the erythrocyte membrane would likely require a large conformational rearrangement. Given the unusually high disulfide content of the complex, it is possible that such a rearrangement could be initiated by the breakage of allosteric disulfide bonds, potentially triggered by interactions at the erythrocyte membrane. This first direct observation of an exported
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