Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes
The larval stage of the cestode Echinococcus multilocularis is the causative agent of alveolar echinococcosis. To investigate the biology of these stages and to test novel compounds, metacestode cultures represent a suitable in vitro model system. These metacestodes are vesicles surrounded by an env...
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| Language: | English |
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2023
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| Online Access: | https://hdl.handle.net/20.500.12008/43230 |
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| _version_ | 1868890208010764288 |
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| author | Müller, Joachim |
| author2 | Preza Pérez, Matías Facundo Kaethner, Marc Rufener, Reto Braga, Sophie Uldry, Anne-Christine Heller, Manfred Lundström-Stadelmann, Britta |
| author2_role | author author author author author author author |
| author_browse | Braga, Sophie Heller, Manfred Kaethner, Marc Lundström-Stadelmann, Britta Müller, Joachim Preza Pérez, Matías Facundo Rufener, Reto Uldry, Anne-Christine |
| author_facet | Müller, Joachim Preza Pérez, Matías Facundo Kaethner, Marc Rufener, Reto Braga, Sophie Uldry, Anne-Christine Heller, Manfred Lundström-Stadelmann, Britta |
| author_role | author |
| collection | COLIBRI |
| dc.contributor.none.fl_str_mv | Müller Joachim Preza Pérez Matías Facundo, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología. Kaethner Marc Rufener Reto Braga Sophie Uldry Anne-Christine Heller Manfred Lundström-Stadelmann Britta |
| dc.creator.none.fl_str_mv | Müller, Joachim Preza Pérez, Matías Facundo Kaethner, Marc Rufener, Reto Braga, Sophie Uldry, Anne-Christine Heller, Manfred Lundström-Stadelmann, Britta |
| dc.date.none.fl_str_mv | 2023 2024-03-20T13:53:59Z 2024-03-20T13:53:59Z |
| dc.format.none.fl_str_mv | 14 h. application/pdf |
| dc.identifier.none.fl_str_mv | Müller, J, Preza Pérez, M, Kaethner, M [y otros autores]. "Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes". Frontiers in Cellular and Infection Microbiology. [en línea] 2023, 13: 1170763. 14 h. DOI: 10.3389/fcimb.2023.1170763. 2235-2988 https://hdl.handle.net/20.500.12008/43230 10.3389/fcimb.2023.1170763 |
| dc.language.none.fl_str_mv | en eng |
| dc.publisher.none.fl_str_mv | Frontiers |
| dc.relation.none.fl_str_mv | Frontiers in Cellular and Infection Microbiology, 2023, 13: 1170763. |
| dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess Licencia Creative Commons Atribución (CC - By 4.0) |
| dc.source.none.fl_str_mv | reponame:COLIBRI instname:Universidad de la República instacron:Universidad de la República |
| dc.subject.none.fl_str_mv | Cestodes Model system Targeted proteomics Transport Echinococcosis Untargeted proteomics Antigen B |
| dc.title.none.fl_str_mv | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| dc.type.none.fl_str_mv | Artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| description | The larval stage of the cestode Echinococcus multilocularis is the causative agent of alveolar echinococcosis. To investigate the biology of these stages and to test novel compounds, metacestode cultures represent a suitable in vitro model system. These metacestodes are vesicles surrounded by an envelope formed by the vesicle tissue (VT), which is formed by the laminated and germinal layer, and filled with vesicle fluid (VF). We analyzed the proteome of VF and VT by liquid chromatography tandem mass spectrometry (LC-MS/MS) and identified a total of 2,954 parasite proteins. The most abundant protein in VT was the expressed conserved protein encoded by EmuJ_000412500, followed by the antigen B subunit AgB8/3a encoded by EmuJ_000381500 and Endophilin B1 (protein p29). In VF, the pattern was different and dominated by AgB subunits. The most abundant protein was the AgB8/3a subunit followed by three other AgB subunits. In total, the AgB subunits detected in VF represented 62.1% of the parasite proteins. In culture media (CM), 63 E. multilocularis proteins were detected, of which AgB subunits made up 93.7% of the detected parasite proteins. All AgB subunits detected in VF (encoded by EmuJ_000381100–700, corresponding to AgB8/2, AgB8/1, AgB8/4, AgB8/3a, AgB8/3b, and AgB8/3c) were also found in CM, except the subunit encoded by EmuJ_000381800 (AgB8/5) that was very rare in VF and not detected in CM. The relative abundance of the AgB subunits in VF and CM followed the same pattern. In VT, only the subunits EmuJ_000381500 (AgB8/3a) and EmuJ_000381200 (AgB8/1) were detected among the 20 most abundant proteins. To see whether this pattern was specific to VF from in vitro cultured metacestodes, we analyzed the proteome of VF from metacestodes grown in a mouse model. Here, the AgB subunits encoded by EmuJ_000381100–700 constituted the most abundant proteins, namely, 81.9% of total protein, with the same order of abundance as in vitro. Immunofluorescence on metacestodes showed that AgB is co-localized to calcareous corpuscles of E. multilocularis. Using targeted proteomics with HA-tagged EmuJ_000381200 (AgB8/1) and EmuJ_000381100 (AgB8/2), we could show that uptake of AgB subunits from CM into VF occurs within hours. |
| eu_rights_str_mv | openAccess |
| format | article |
| id | anni_db8f064fb87a7a3ea7c0fe77c8c4c171 |
| identifier_str_mv | Müller, J, Preza Pérez, M, Kaethner, M [y otros autores]. "Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes". Frontiers in Cellular and Infection Microbiology. [en línea] 2023, 13: 1170763. 14 h. DOI: 10.3389/fcimb.2023.1170763. 2235-2988 10.3389/fcimb.2023.1170763 |
| instacron_str | Universidad de la República |
| institution | Universidad de la República |
| instname_str | Universidad de la República |
| language | eng |
| language_invalid_str_mv | en |
| network_acronym_str | anni |
| network_name_str | oai-lr-anni |
| oai_identifier_str | oai:colibri.udelar.edu.uy:20.500.12008/43230 |
| publishDate | 2023 |
| publishDateSort | 2023 |
| publisher.none.fl_str_mv | Frontiers |
| reponame_str | COLIBRI |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
| spelling | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodesMüller, JoachimPreza Pérez, Matías FacundoKaethner, MarcRufener, RetoBraga, SophieUldry, Anne-ChristineHeller, ManfredLundström-Stadelmann, BrittaCestodesModel systemTargeted proteomicsTransportEchinococcosisUntargeted proteomicsAntigen BThe larval stage of the cestode Echinococcus multilocularis is the causative agent of alveolar echinococcosis. To investigate the biology of these stages and to test novel compounds, metacestode cultures represent a suitable in vitro model system. These metacestodes are vesicles surrounded by an envelope formed by the vesicle tissue (VT), which is formed by the laminated and germinal layer, and filled with vesicle fluid (VF). We analyzed the proteome of VF and VT by liquid chromatography tandem mass spectrometry (LC-MS/MS) and identified a total of 2,954 parasite proteins. The most abundant protein in VT was the expressed conserved protein encoded by EmuJ_000412500, followed by the antigen B subunit AgB8/3a encoded by EmuJ_000381500 and Endophilin B1 (protein p29). In VF, the pattern was different and dominated by AgB subunits. The most abundant protein was the AgB8/3a subunit followed by three other AgB subunits. In total, the AgB subunits detected in VF represented 62.1% of the parasite proteins. In culture media (CM), 63 E. multilocularis proteins were detected, of which AgB subunits made up 93.7% of the detected parasite proteins. All AgB subunits detected in VF (encoded by EmuJ_000381100–700, corresponding to AgB8/2, AgB8/1, AgB8/4, AgB8/3a, AgB8/3b, and AgB8/3c) were also found in CM, except the subunit encoded by EmuJ_000381800 (AgB8/5) that was very rare in VF and not detected in CM. The relative abundance of the AgB subunits in VF and CM followed the same pattern. In VT, only the subunits EmuJ_000381500 (AgB8/3a) and EmuJ_000381200 (AgB8/1) were detected among the 20 most abundant proteins. To see whether this pattern was specific to VF from in vitro cultured metacestodes, we analyzed the proteome of VF from metacestodes grown in a mouse model. Here, the AgB subunits encoded by EmuJ_000381100–700 constituted the most abundant proteins, namely, 81.9% of total protein, with the same order of abundance as in vitro. Immunofluorescence on metacestodes showed that AgB is co-localized to calcareous corpuscles of E. multilocularis. Using targeted proteomics with HA-tagged EmuJ_000381200 (AgB8/1) and EmuJ_000381100 (AgB8/2), we could show that uptake of AgB subunits from CM into VF occurs within hours.FrontiersMüller JoachimPreza Pérez Matías Facundo, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Kaethner MarcRufener RetoBraga SophieUldry Anne-ChristineHeller ManfredLundström-Stadelmann Britta2024-03-20T13:53:59Z2024-03-20T13:53:59Z2023Artículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersion14 h.application/pdfMüller, J, Preza Pérez, M, Kaethner, M [y otros autores]. "Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes". Frontiers in Cellular and Infection Microbiology. [en línea] 2023, 13: 1170763. 14 h. DOI: 10.3389/fcimb.2023.1170763.2235-2988https://hdl.handle.net/20.500.12008/4323010.3389/fcimb.2023.1170763reponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaenengFrontiers in Cellular and Infection Microbiology, 2023, 13: 1170763.Las obras depositadas en el Repositorio se rigen por la Ordenanza de los Derechos de la Propiedad Intelectual de la Universidad de la República.(Res. Nº 91 de C.D.C. de 8/III/1994 – D.O. 7/IV/1994) y por la Ordenanza del Repositorio Abierto de la Universidad de la República (Res. Nº 16 de C.D.C. de 07/10/2014)info:eu-repo/semantics/openAccessLicencia Creative Commons Atribución (CC - By 4.0)oai:colibri.udelar.edu.uy:20.500.12008/432302026-04-14T10:10:35Z |
| spellingShingle | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes Müller, Joachim Cestodes Model system Targeted proteomics Transport Echinococcosis Untargeted proteomics Antigen B |
| status_str | publishedVersion |
| title | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| title_full | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| title_fullStr | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| title_full_unstemmed | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| title_short | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| title_sort | Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes |
| topic | Cestodes Model system Targeted proteomics Transport Echinococcosis Untargeted proteomics Antigen B |
| url | https://hdl.handle.net/20.500.12008/43230 |