ArticlePLoS pathogens2012
Structural and functional insights into the malaria parasite moving junction complex.
Article in PLoS pathogens, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.
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Who cites it
83 citing papers in PubMed, 144 citations in OpenAlex.
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- Erythrocyte invasion in malaria: from molecular mechanisms to rational vaccines.Nature reviews. Microbiology · 2026Review
- From Concepts to Inhibitors: A Blueprint for Targeting Protein-Protein Interactions.Chemical reviews · 2025Review
- Chemical Protein Engineering: Backbone Cyclization Rescues Folding of a 183-Residue Truncated Domain of Malaria Parasite Protein PfAMA1.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- A strain-transcending anti-AMA1 human monoclonal antibody neutralizes malaria parasites independent of direct RON2L receptor blockade.Cell reports. Medicine · 2025Article
- Potent AMA1-specific human monoclonal antibody against Plasmodium vivax Pre-erythrocytic and Blood Stages.Nature communications · 2024Article
- Conformational variability in the D2 loop ofJournal of structural biology: X · 2024Article
- Plasmodium RON11 triggers biogenesis of the merozoite rhoptry pair and is essential for erythrocyte invasion.PLoS biology · 2024Article
- A broadly cross-reactive i-body to AMA1 potently inhibits blood and liver stages of Plasmodium parasites.Nature communications · 2024Article
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- Structure guided mimicry of an essential P. falciparum receptor-ligand complex enhances cross neutralizing antibodies.Nature communications · 2023Article
- Structure-based design of a strain transcending AMA1-RON2L malaria vaccine.Nature communications · 2023Article
- Rhoptry neck protein 4 plays important roles duringmSphere · 2023Article
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- Structure guided mimicry of an essential P. falciparum receptor-ligand complex enhances cross neutralizing antibodies.Research square · 2023Article
- Defining species-specific and conserved interactions of apical membrane protein 1 during erythrocyte invasion in malaria to inform multi-species vaccines.Cellular and molecular life sciences : CMLS · 2023Article
- Invasion ofProceedings of the National Academy of Sciences of the United States of America · 2023Article
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23 more citing papers are in PubMed but not listed here.
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Authors and funding
11 authors at 5 institutions in 3 countries.
Funding
Abstract
Members of the phylum Apicomplexa, which include the malaria parasite Plasmodium, share many features in their invasion mechanism in spite of their diverse host cell specificities and life cycle characteristics. The formation of a moving junction (MJ) between the membranes of the invading apicomplexan parasite and the host cell is common to these intracellular pathogens. The MJ contains two key parasite components: the surface protein Apical Membrane Antigen 1 (AMA1) and its receptor, the Rhoptry Neck Protein (RON) complex, which is targeted to the host cell membrane during invasion. In particular, RON2, a transmembrane component of the RON complex, interacts directly with AMA1. Here, we report the crystal structure of AMA1 from Plasmodium falciparum in complex with a peptide derived from the extracellular region of PfRON2, highlighting clear specificities of the P. falciparum RON2-AMA1 interaction. The receptor-binding site of PfAMA1 comprises the hydrophobic groove and a region that becomes exposed by displacement of the flexible Domain II loop. Mutations of key contact residues of PfRON2 and PfAMA1 abrogate binding between the recombinant proteins. Although PfRON2 contacts some polymorphic residues, binding studies with PfAMA1 from different strains show that these have little effect on affinity. Moreover, we demonstrate that the PfRON2 peptide inhibits erythrocyte invasion by P. falciparum merozoites and that this strong inhibitory potency is not affected by AMA1 polymorphisms. In parallel, we have determined the crystal structure of PfAMA1 in complex with the invasion-inhibitory peptide R1 derived by phage display, revealing an unexpected structural mimicry of the PfRON2 peptide. These results identify the key residues governing the interactions between AMA1 and RON2 in P. falciparum and suggest novel approaches to antimalarial therapeutics.
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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.