ArticleNature communications2017
P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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Who cites it
50 citing papers in PubMed, 78 citations in OpenAlex.
- Antibodies from malaria-exposed Malians generally interact additively or synergistically with human vaccine-induced RH5 antibodies.Cell reports. Medicine · 2021Trial
- Human vaccination against RH5 induces neutralizing antimalarial antibodies that inhibit RH5 invasion complex interactions.JCI insight · 2017Trial
- Proteome-wide characterization of Plasmodium vivax antigens using a high-density peptide array.PLoS pathogens · 2026Article
- Targeting protein-protein interactions in Plasmodium: from asexual replication to sexual development.Parasites & vectors · 2026Review
- Immunoinformatics-Based Multi-Epitope Vaccine Design AgainstHealth science reports · 2025Article
- Single-cell transcriptomics reveal transcriptional programs underlying male and female cell fate during Plasmodium falciparum gametocytogenesis.Nature communications · 2024Article
- Preclinical development of a stabilized RH5 virus-like particle vaccine that induces improved antimalarial antibodies.Cell reports. Medicine · 2024Article
- Development of an improved blood-stage malaria vaccine targeting the essential RH5-CyRPA-RIPR invasion complex.Nature communications · 2024Article
- A panel of recombinantmBio · 2024Article
- Article
- Construction, Expression, and Evaluation of the Naturally Acquired Humoral Immune Response againstInternational journal of molecular sciences · 2023Article
- Plasmepsin X activates the PCRCR complex of Plasmodium falciparum by processing PfRh5 for erythrocyte invasion.Nature communications · 2023Article
- Limited genetic variations of the Rh5-CyRPA-Ripr invasion complex inFrontiers in tropical diseases · 2023Article
- Reticulocyte Binding Protein Homologue 5 is a target of balancing selection in theFrontiers in parasitology · 2023Article
- PCRCR complex is essential for invasion of human erythrocytes by Plasmodium falciparum.Nature microbiology · 2022Article
- The Plasmodium falciparum parasitophorous vacuole protein P113 interacts with the parasite protein export machinery and maintains normal vacuole architecture.Molecular microbiology · 2022Article
- The Cellular and Molecular Interaction Between Erythrocytes andFrontiers in cellular and infection microbiology · 2022Review
- The Plasmodium falciparum Rh5 invasion protein complex reveals an excess of rare variant mutations.Malaria journal · 2021Article
- Antibody Combinations Targeting the Essential Antigens CyRPA, RH5, and MSP-119 Potently Neutralize Plasmodium falciparum Clinical Isolates From India and Africa.The Journal of infectious diseases · 2021Article
- Assessing the functional impact of PfRh5 genetic diversity on ex vivo erythrocyte invasion inhibition.Scientific reports · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Invasion of erythrocytes by Plasmodium falciparum merozoites is necessary for malaria pathogenesis and is therefore a primary target for vaccine development. RH5 is a leading subunit vaccine candidate because anti-RH5 antibodies inhibit parasite growth and the interaction with its erythrocyte receptor basigin is essential for invasion. RH5 is secreted, complexes with other parasite proteins including CyRPA and RIPR, and contains a conserved N-terminal region (RH5Nt) of unknown function that is cleaved from the native protein. Here, we identify P113 as a merozoite surface protein that directly interacts with RH5Nt. Using recombinant proteins and a sensitive protein interaction assay, we establish the binding interdependencies of all the other known RH5 complex components and conclude that the RH5Nt-P113 interaction provides a releasable mechanism for anchoring RH5 to the merozoite surface. We exploit these findings to design a chemically synthesized peptide corresponding to RH5Nt, which could contribute to a cost-effective malaria vaccine.
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Registered trials
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