{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Reddy KS"],"funding":["Department of Biotechnology , Ministry of Science and Technology","Bill and Melinda Gates Foundation"],"pagination":["1179-84"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC4313826"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["112(4)"],"pubmed_abstract":["Erythrocyte invasion by Plasmodium falciparum merozoites is a highly intricate process in which Plasmodium falciparum reticulocyte binding-like homologous protein 5 (PfRH5) is an indispensable parasite ligand that binds with its erythrocyte receptor, Basigin. PfRH5 is a leading blood-stage vaccine candidate because it exhibits limited polymorphisms and elicits potent strain-transcending parasite neutralizing antibodies. However, the mechanism by which it is anchored to the merozoite surface remains unknown because both PfRH5 and the PfRH5-interacting protein (PfRipr) lack transmembrane domains and GPI anchors. Here we have identified a conserved GPI-linked parasite protein, Cysteine-rich protective antigen (CyRPA) as an interacting partner of PfRH5-PfRipr that tethers the PfRH5/PfRipr/CyRP"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion."],"pmcid":["PMC4313826"],"funding_grant_id":["BT/PR13376/GBD/27/ 260/2009","BT/01/CEIB/11/V/01","BT/HRD/35 /02/14/2008","GCE OPP1007027"],"pubmed_authors":["Reddy KS","Pandey AK","Mitra P","Chauhan VS","Amlabu E","Gaur D"],"additional_accession":[]},"is_claimable":false,"name":"Multiprotein complex between the GPI-anchored CyRPA with PfRH5 and PfRipr is crucial for Plasmodium falciparum erythrocyte invasion.","description":"Erythrocyte invasion by Plasmodium falciparum merozoites is a highly intricate process in which Plasmodium falciparum reticulocyte binding-like homologous protein 5 (PfRH5) is an indispensable parasite ligand that binds with its erythrocyte receptor, Basigin. PfRH5 is a leading blood-stage vaccine candidate because it exhibits limited polymorphisms and elicits potent strain-transcending parasite neutralizing antibodies. However, the mechanism by which it is anchored to the merozoite surface remains unknown because both PfRH5 and the PfRH5-interacting protein (PfRipr) lack transmembrane domains and GPI anchors. Here we have identified a conserved GPI-linked parasite protein, Cysteine-rich protective antigen (CyRPA) as an interacting partner of PfRH5-PfRipr that tethers the PfRH5/PfRipr/CyRP","dates":{"release":"2015-01-01T00:00:00Z","publication":"2015 Jan","modification":"2025-04-21T19:49:31.179Z","creation":"2019-03-27T01:44:25Z"},"accession":"S-EPMC4313826","cross_references":{"pubmed":["25583518"],"doi":["10.1073/pnas.1415466112"]}}