Galaway, Francis, Drought, Laura G, Fala, Maria et al. (4 more authors) (2017) P113 is a merozoite surface protein that binds the N terminus of Plasmodium falciparum RH5. Nature Communications. 14333. ISSN 2041-1723
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.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Keywords: | first & last 3 (QQ only),first & last (all papers) |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Biology (York) The University of York > Faculty of Sciences (York) > Hull York Medical School (York) |
Depositing User: | Pure (York) |
Date Deposited: | 19 Oct 2020 15:50 |
Last Modified: | 02 Apr 2025 23:20 |
Published Version: | https://doi.org/10.1038/ncomms14333 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1038/ncomms14333 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:166884 |