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TitleThe PfRCR complex bridges malaria parasite and erythrocyte during invasion.
Journal, issue, pagesNature, Vol. 625, Issue 7995, Page 578-584, Year 2024
Publish dateDec 20, 2023
AuthorsBrendan Farrell / Nawsad Alam / Melissa N Hart / Abhishek Jamwal / Robert J Ragotte / Hannah Walters-Morgan / Simon J Draper / Ellen Knuepfer / Matthew K Higgins /
PubMed AbstractThe symptoms of malaria occur during the blood stage of infection, when parasites invade and replicate within human erythrocytes. The PfPCRCR complex, containing PfRH5 (refs. ), PfCyRPA, PfRIPR, ...The symptoms of malaria occur during the blood stage of infection, when parasites invade and replicate within human erythrocytes. The PfPCRCR complex, containing PfRH5 (refs. ), PfCyRPA, PfRIPR, PfCSS and PfPTRAMP, is essential for erythrocyte invasion by the deadliest human malaria parasite, Plasmodium falciparum. Invasion can be prevented by antibodies or nanobodies against each of these conserved proteins, making them the leading blood-stage malaria vaccine candidates. However, little is known about how PfPCRCR functions during invasion. Here we present the structure of the PfRCR complex, containing PfRH5, PfCyRPA and PfRIPR, determined by cryogenic-electron microscopy. We test the hypothesis that PfRH5 opens to insert into the membrane, instead showing that a rigid, disulfide-locked PfRH5 can mediate efficient erythrocyte invasion. We show, through modelling and an erythrocyte-binding assay, that PfCyRPA-binding antibodies neutralize invasion through a steric mechanism. We determine the structure of PfRIPR, showing that it consists of an ordered, multidomain core flexibly linked to an elongated tail. We also show that the elongated tail of PfRIPR, which is the target of growth-neutralizing antibodies, binds to the PfCSS-PfPTRAMP complex on the parasite membrane. A modular PfRIPR is therefore linked to the merozoite membrane through an elongated tail, and its structured core presents PfCyRPA and PfRH5 to interact with erythrocyte receptors. This provides fresh insight into the molecular mechanism of erythrocyte invasion and opens the way to new approaches in rational vaccine design.
External linksNature / PubMed:38123677 / PubMed Central
MethodsEM (single particle)
Resolution2.89 - 3.95 Å
Structure data

16569

8cdd

EMDB-16569, PDB-8cdd:
PfRH5-PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003
Method: EM (single particle) / Resolution: 3.0 Å

16570

8cde

EMDB-16570, PDB-8cde:
PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-16635: PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 - maps for local refinement on PfRIPR
Method: EM (single particle) / Resolution: 3.33 Å

EMDB-16636: PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 consensus maps
Method: EM (single particle) / Resolution: 3.02 Å

EMDB-16637: PfRH5-PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 - consensus map
Method: EM (single particle) / Resolution: 2.89 Å

EMDB-16638: PfRH5-PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 - local refinement on PfRH5
Method: EM (single particle) / Resolution: 2.89 Å

EMDB-16639: PfRH5-PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 - local refinement on PfRIPR
Method: EM (single particle) / Resolution: 3.31 Å

EMDB-16640: PfRH5-PfCyRPA-PfRIPR complex from Plasmodium falciparum bound to antibody Cy.003 - map with additional PfRIPR tail density
Method: EM (single particle) / Resolution: 3.95 Å

Source
  • plasmodium falciparum 3d7 (eukaryote)
  • gallus gallus (chicken)
KeywordsCELL ADHESION / Plasmodium falciparum / erythrocyte-invasion / PfRCR / blood stage malaria vaccine

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