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Divergent roles for the RH5 complex components, CyRPA and RIPR in human-infective malaria parasites

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dc.contributor.author Knuepfer, Ellen
dc.contributor.author Wright, Katherine E.
dc.contributor.author Kumar Prajapati, Surendra
dc.contributor.author Rawlinson, Thomas A.
dc.contributor.author Mohring, Franziska
dc.contributor.author Koch, Marion
dc.contributor.author Lyth, Oliver R.
dc.contributor.author Howell, Steven A.
dc.contributor.author Villasis, Elizabeth
dc.contributor.author Snijders, Ambrosius P.
dc.contributor.author Moon, Robert W.
dc.contributor.author Draper, Simon J.
dc.contributor.author Rosanas-Urgell, Anna
dc.contributor.author Higgins, Matthew K.
dc.contributor.author Baum, Jake
dc.contributor.author Holder, Anthony A.
dc.date.accessioned 2019-07-04T16:59:29Z
dc.date.available 2019-07-04T16:59:29Z
dc.date.issued 2019
dc.identifier.uri https://hdl.handle.net/20.500.12866/6770
dc.description.abstract Malaria is caused by Plasmodium parasites, which invade and replicate in erythrocytes. For Plasmodium falciparum, the major cause of severe malaria in humans, a heterotrimeric complex comprised of the secreted parasite proteins, PfCyRPA, PfRIPR and PfRH5 is essential for erythrocyte invasion, mediated by the interaction between PfRH5 and erythrocyte receptor basigin (BSG). However, whilst CyRPA and RIPR are present in most Plasmodium species, RH5 is found only in the small Laverania subgenus. Existence of a complex analogous to PfRH5-PfCyRPA-PfRIPR targeting BSG, and involvement of CyRPA and RIPR in invasion, however, has not been addressed in non-Laverania parasites. Here, we establish that unlike P. falciparum, P. knowlesi and P. vivax do not universally require BSG as a host cell invasion receptor. Although we show that both PkCyRPA and PkRIPR are essential for successful invasion of erythrocytes by P. knowlesi parasites in vitro, neither protein forms a complex with each other or with an RH5-like molecule. Instead, PkRIPR is part of a different trimeric protein complex whereas PkCyRPA appears to function without other parasite binding partners. It therefore appears that in the absence of RH5, outside of the Laverania subgenus, RIPR and CyRPA have different, independent functions crucial for parasite survival. en_US
dc.language.iso eng
dc.publisher PLoS
dc.relation.ispartof urn:issn:1553-7374
dc.rights info:eu-repo/semantics/restrictedAccess
dc.rights.uri https://creativecommons.org/licenses/by-nc-nd/4.0/deed.es
dc.subject Plasmodium en_US
dc.subject Red blood cells en_US
dc.subject Merozoites en_US
dc.subject Malarial parasites en_US
dc.subject Immunoprecipitation en_US
dc.subject Host cells en_US
dc.subject Parasitic life cycles en_US
dc.subject Polymerase chain reaction en_US
dc.title Divergent roles for the RH5 complex components, CyRPA and RIPR in human-infective malaria parasites en_US
dc.type info:eu-repo/semantics/review
dc.identifier.doi https://doi.org/10.1371/journal.ppat.1007809
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.02.00 es_PE
dc.subject.ocde https://purl.org/pe-repo/ocde/ford#3.01.09


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