Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome.

{"sci_version": "1.2", "schema": "https://corpus.bntrg.co.uk/sci/1.0/sci.schema.json", "id": "pmid:28944300", "kind": "science-record", "revision": 3, "content_hash": "sha256:14dd3729fe501f6566be8f70e62c7ac56c531c7c67cb74b9a094ff091da4cbb7", "created_at": "2026-11-01T15:40:28Z", "updated_at": "2026-11-01T21:21:05Z", "generator": {"name": "corpus-assay-engine", "run_id": "reading-sci-2026-11-01"}, "paper": {"state": "complete", "title": "Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome.", "doi": "10.12688/wellcomeopenres.11910.2", "pmid": "28944300", "authors": ["Abdirahman Abdi", "Lu Yu", "David Goulding", "Martin K Rono", "Philip Bejon", "Jyoti Choudhary", "Julian Rayner"], "journal": "Wellcome open research", "year": 2017, "abstract": "BACKGROUND: Many pathogens secrete effector molecules to subvert host immune responses, to acquire nutrients, and/or to prepare host cells for invasion. One of the ways that effector molecules are secreted is through extracellular vesicles (EVs) such as exosomes. Recently, the malaria parasite P. falciparum has been shown to produce EVs that can mediate transfer of genetic material between parasites and induce sexual commitment. Characterizing the content of these vesicles may improve our understanding of P. falciparum pathogenesis and virulence.\nMETHODS: Previous studies of P. falciparum EVs have been limited to long-term adapted laboratory isolates. In this study, we isolated EVs from a Kenyan P. falciparum clinical isolate adapted to in vitro culture for a short period and characterized their protein content by mass spectrometry (data are available via ProteomeXchange, with identifier PXD006925).\nRESULTS: We show that P. falciparum extracellular vesicles ( PfEVs) are enriched in proteins found within the exomembrane compartments of infected erythrocytes such as Maurer's clefts (MCs), as well as the secretory endomembrane compartments in the apical end of the merozoites, suggesting that these proteins play a role in parasite-host interactions. Comparison of this novel clinically relevant dataset with previously published datasets helps to define a core secretome present in Plasmodium EVs.\nCONCLUSIONS: P. falciparum extracellular vesicles contain virulence-associated parasite proteins. Therefore, analysis of PfEVs contents from a range of clinical isolates, and their functional validation may improve our understanding of the virulence mechanisms of the parasite, and potentially identify targets for interventions or diagnostics.", "claims": [{"id": "claim-method", "statement": "The –log p-value was generated from the Bonferroni adjusted p-value.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:28944300", "locator": "sections[21] \"Supplementary material\" paragraph 3", "quote": "The –log p-value was generated from the Bonferroni adjusted p-value."}], "state": "complete"}, {"id": "claim-data-access", "statement": "The raw mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE 50 partner repository, with the dataset identifier PXD006925”. Project name: ‘Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome’. The original gel image for Figure 1c is available at https://osf.io/wdg96/ 81.", "kind": "methodological", "target": null, "evidence": [{"asset": "source:pmid:28944300", "locator": "sections[16] \"Data availability\" paragraph 2", "quote": "The raw mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium via the PRIDE 50 partner repository, with the dataset identifier PXD006925”. Project name: ‘Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome’. The original gel image for Figure 1c is available at https://osf.io/wdg96/ 81."}], "state": "complete"}, {"id": "claim-target-result", "statement": "The study characterized the PfEV proteome by mass spectrometry, and the source data are available through ProteomeXchange under identifier PXD006925.", "kind": "qualitative", "target": null, "evidence": [{"asset": "source:pmid:28944300", "locator": "sections[0] \"Abstract\" paragraph 2", "quote": "In this study, we isolated EVs from a Kenyan P. falciparum clinical isolate that had been adapted to in vitro culture for a relatively shorter period, and characterized their protein content by mass spectrometry (data are available via ProteomeXchange, with identifier PXD006925)."}, {"asset": "source:pmid:28944300", "locator": "sections[0] \"Abstract\" paragraph 3", "quote": "We show that P. falciparum extracellular vesicles ( PfEVs) are enriched in proteins found within the exomembrane compartments of infected erythrocytes such as Maurer’s clefts (MCs), as well as the secretory endomembrane compartments in the apical end of the merozoites, suggesting that PfEVs may play a role in parasite-host interactions."}], "state": "complete"}], "gaps": []}, "experiment": {"state": "complete", "objective": "The study characterized the PfEV proteome by mass spectrometry, and the source data are available through ProteomeXchange under identifier PXD006925.", "steps": [{"id": "read_published_estimate", "order": 1, "name": "Read the published estimate from the source", "kind": "other", "state": "complete", "blocked_on": null, "description": "The claim, method and evidence span published with the source article.", "duration_hours": null, "parameters": {}, "inputs": ["source:pmid:28944300"], "outputs": ["the published estimate and its evidence"], "instruments": [], "reagents": []}, {"id": "obtain_source_data", "order": 2, "name": "Obtain the source data from the named repository", "kind": "data-preparation", "state": "complete", "blocked_on": null, "description": "The GEO series accession resolves and its sample accessions are listed. 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