PXD039646 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Plasmepsin X activates function of the PCRCR complex in P. falciparum by processing PfRh5 for binding to basigin and invasion of human erythrocytes |
Description | Plasmodium falciparum causes the most severe form of malaria in humans. The protozoan parasite develops within erythrocytes to mature schizonts, that contain more than 16 merozoites, which egress and invade fresh erythrocytes. The aspartic protease plasmepsin X (PMX), processes proteins and proteases essential for merozoite egress from the schizont and invasion of the host erythrocyte, including the leading vaccine candidate PfRh5. PfRh5 is anchored to the merozoite surface through a 5-membered complex (PCRCR), consisting of Plasmodium thrombospondin-related apical merozoite protein (PTRAMP), cysteine-rich small secreted protein (CSS), Rh5-interacting protein (PfRipr) and cysteine-rich protective antigen (CyRPA). We show that PCRCR is processed by PMX in micronemes to remove the N-terminal prodomain and this activates the function of the complex unmasking a form that can bind basigin on the erythrocyte membrane and mediate merozoite invasion. The ability to activate PCRCR at a specific time in merozoite invasion ensures invasion inhibitory epitopes are exposed to the immune system for a minimal time but also mask potential deleterious effects of its function until they are required. These results provide an important understanding of the essential roles of PMX and the fine regulation of PCRCR function in P. falciparum biology. |
HostingRepository | PRIDE |
AnnounceDate | 2023-04-05 |
AnnouncementXML | Submission_2023-04-04_21:33:40.902.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | LauraDagley |
SpeciesList | scientific name: Plasmodium falciparum (isolate 3D7); NCBI TaxID: 36329; |
ModificationList | acetylated residue; monohydroxylated residue; iodoacetamide derivatized residue |
Instrument | timsTOF Pro |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2023-01-25 03:33:40 | ID requested | |
⏵ 1 | 2023-04-04 21:33:41 | announced | |
2 | 2024-10-04 02:01:58 | announced | 2024-10-04: Updated project metadata. |
Publication List
Dataset with its publication pending |
Keyword List
submitter keyword: Malaria, plasmepsin X, IP-MS, PCRCR |
Contact List
Professor AlanCowman |
contact affiliation | Deputy Director – Science Strategy The Walter and Eliza Hall institute of Medical Research Professor, Department of Medical Biology Faculty of Medicine, Dentistry and Health The University of Melbourne Australia |
contact email | cowman@wehi.edu.au |
lab head | |
LauraDagley |
contact affiliation | WEHI |
contact email | dagley.l@wehi.edu.au |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
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PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD039646
- Label: PRIDE project
- Name: Plasmepsin X activates function of the PCRCR complex in P. falciparum by processing PfRh5 for binding to basigin and invasion of human erythrocytes