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P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5

Author

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  • Francis Galaway

    (Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute)

  • Laura G. Drought

    (Malaria Programme, Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK)

  • Maria Fala

    (Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute)

  • Nadia Cross

    (Malaria Programme, Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK)

  • Alison C. Kemp

    (Malaria Programme, Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK)

  • Julian C. Rayner

    (Malaria Programme, Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK)

  • Gavin J. Wright

    (Cell Surface Signalling Laboratory, Wellcome Trust Sanger Institute
    Malaria Programme, Wellcome Trust Sanger Institute, Cambridge CB10 1SA, UK)

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.

Suggested Citation

  • Francis Galaway & Laura G. Drought & Maria Fala & Nadia Cross & Alison C. Kemp & Julian C. Rayner & Gavin J. Wright, 2017. "P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5," Nature Communications, Nature, vol. 8(1), pages 1-11, April.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_ncomms14333
    DOI: 10.1038/ncomms14333
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    Cited by:

    1. Mubasher Mohammed & Alexis Dziedziech & Diego Macedo & Frederik Huppertz & Ylva Veith & Zoé Postel & Elena Christ & Richard Scheytt & Tanja Slotte & Johan Henriksson & Johan Ankarklev, 2024. "Single-cell transcriptomics reveal transcriptional programs underlying male and female cell fate during Plasmodium falciparum gametocytogenesis," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    2. Tony Triglia & Stephen W. Scally & Benjamin A. Seager & Michał Pasternak & Laura F. Dagley & Alan F. Cowman, 2023. "Plasmepsin X activates the PCRCR complex of Plasmodium falciparum by processing PfRh5 for erythrocyte invasion," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Barnabas G. Williams & Lloyd D. W. King & David Pulido & Doris Quinkert & Amelia M. Lias & Sarah E. Silk & Robert J. Ragotte & Hannah Davies & Jordan R. Barrett & Kirsty McHugh & Cassandra A. Rigby & , 2024. "Development of an improved blood-stage malaria vaccine targeting the essential RH5-CyRPA-RIPR invasion complex," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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