Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations]
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. fa...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Wellcome
2017-11-01
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| Series: | Wellcome Open Research |
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| Online Access: | https://wellcomeopenresearch.org/articles/2-50/v2 |
| _version_ | 1811263442365972480 |
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| author | Abdirahman Abdi Lu Yu David Goulding Martin K. Rono Philip Bejon Jyoti Choudhary Julian Rayner |
| author_facet | Abdirahman Abdi Lu Yu David Goulding Martin K. Rono Philip Bejon Jyoti Choudhary Julian Rayner |
| author_sort | Abdirahman Abdi |
| collection | DOAJ |
| description | 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. Methods: 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 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). Results: 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. Comparison of this dataset with previously published datasets helps to define a core secretome present in PfEVs. Conclusions: P. falciparum extracellular vesicles contain virulence-associated parasite proteins. 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 new targets for interventions or diagnostics. |
| first_indexed | 2024-04-12T19:45:28Z |
| format | Article |
| id | doaj.art-73c63b2967704e6e9aaecf0b5ece2424 |
| institution | Directory Open Access Journal |
| issn | 2398-502X |
| language | English |
| last_indexed | 2024-04-12T19:45:28Z |
| publishDate | 2017-11-01 |
| publisher | Wellcome |
| record_format | Article |
| series | Wellcome Open Research |
| spelling | doaj.art-73c63b2967704e6e9aaecf0b5ece24242022-12-22T03:18:58ZengWellcomeWellcome Open Research2398-502X2017-11-01210.12688/wellcomeopenres.11910.214296Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations]Abdirahman Abdi0Lu Yu1David Goulding2Martin K. Rono3Philip Bejon4Jyoti Choudhary5Julian Rayner6Pwani University Bioscience Research Centre, Pwani University, Kilifi, KenyaWellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, UKWellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, UKPwani University Bioscience Research Centre, Pwani University, Kilifi, KenyaKEMRI-Wellcome Trust Research Programme, Kilifi, KenyaWellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, UKWellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, Cambridge, UKBackground: 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. Methods: 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 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). Results: 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. Comparison of this dataset with previously published datasets helps to define a core secretome present in PfEVs. Conclusions: P. falciparum extracellular vesicles contain virulence-associated parasite proteins. 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 new targets for interventions or diagnostics.https://wellcomeopenresearch.org/articles/2-50/v2Membranes & SortingMethods for Diagnostic & Therapeutic StudiesParasitologyProtein Chemistry & Proteomics |
| spellingShingle | Abdirahman Abdi Lu Yu David Goulding Martin K. Rono Philip Bejon Jyoti Choudhary Julian Rayner Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] Wellcome Open Research Membranes & Sorting Methods for Diagnostic & Therapeutic Studies Parasitology Protein Chemistry & Proteomics |
| title | Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] |
| title_full | Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] |
| title_fullStr | Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] |
| title_full_unstemmed | Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] |
| title_short | Proteomic analysis of extracellular vesicles from a Plasmodium falciparum Kenyan clinical isolate defines a core parasite secretome [version 2; referees: 1 approved, 2 approved with reservations] |
| title_sort | proteomic analysis of extracellular vesicles from a plasmodium falciparum kenyan clinical isolate defines a core parasite secretome version 2 referees 1 approved 2 approved with reservations |
| topic | Membranes & Sorting Methods for Diagnostic & Therapeutic Studies Parasitology Protein Chemistry & Proteomics |
| url | https://wellcomeopenresearch.org/articles/2-50/v2 |
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