Targeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodes
Resumen:
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.
2023 | |
Cestodes Model system Targeted proteomics Transport Echinococcosis Untargeted proteomics Antigen B |
|
Inglés | |
Universidad de la República | |
COLIBRI | |
https://hdl.handle.net/20.500.12008/43230 | |
Acceso abierto | |
Licencia Creative Commons Atribución (CC - By 4.0) |
_version_ | 1807522808111038464 |
---|---|
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_facet | Müller, Joachim Preza Pérez, Matías Facundo Kaethner, Marc Rufener, Reto Braga, Sophie Uldry, Anne-Christine Heller, Manfred Lundström-Stadelmann, Britta |
author_role | author |
bitstream.checksum.fl_str_mv | 6429389a7df7277b72b7924fdc7d47a9 a0ebbeafb9d2ec7cbb19d7137ebc392c 8010f418ede1186e294ac5448996bd7e 71ed42ef0a0b648670f707320be37b90 e781e6c69ef0dc2cf6c76f1a10729d58 |
bitstream.checksumAlgorithm.fl_str_mv | MD5 MD5 MD5 MD5 MD5 |
bitstream.url.fl_str_mv | http://localhost:8080/xmlui/bitstream/20.500.12008/43230/5/license.txt http://localhost:8080/xmlui/bitstream/20.500.12008/43230/2/license_url http://localhost:8080/xmlui/bitstream/20.500.12008/43230/3/license_text http://localhost:8080/xmlui/bitstream/20.500.12008/43230/4/license_rdf http://localhost:8080/xmlui/bitstream/20.500.12008/43230/1/10.3389.fcimb.2023.1170763.pdf |
collection | COLIBRI |
dc.contributor.filiacion.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.accessioned.none.fl_str_mv | 2024-03-20T13:53:59Z |
dc.date.available.none.fl_str_mv | 2024-03-20T13:53:59Z |
dc.date.issued.none.fl_str_mv | 2023 |
dc.description.abstract.none.fl_txt_mv | 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. |
dc.format.extent.es.fl_str_mv | 14 h. |
dc.format.mimetype.es.fl_str_mv | application/pdf |
dc.identifier.citation.es.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. |
dc.identifier.doi.none.fl_str_mv | 10.3389/fcimb.2023.1170763 |
dc.identifier.issn.none.fl_str_mv | 2235-2988 |
dc.identifier.uri.none.fl_str_mv | https://hdl.handle.net/20.500.12008/43230 |
dc.language.iso.none.fl_str_mv | en eng |
dc.publisher.es.fl_str_mv | Frontiers |
dc.relation.ispartof.es.fl_str_mv | Frontiers in Cellular and Infection Microbiology, 2023, 13: 1170763. |
dc.rights.license.none.fl_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
dc.rights.none.fl_str_mv | info:eu-repo/semantics/openAccess |
dc.source.none.fl_str_mv | reponame:COLIBRI instname:Universidad de la República instacron:Universidad de la República |
dc.subject.es.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.es.fl_str_mv | Artículo |
dc.type.none.fl_str_mv | info:eu-repo/semantics/article |
dc.type.version.none.fl_str_mv | 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 | COLIBRI_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 | COLIBRI |
network_name_str | COLIBRI |
oai_identifier_str | oai:colibri.udelar.edu.uy:20.500.12008/43230 |
publishDate | 2023 |
reponame_str | COLIBRI |
repository.mail.fl_str_mv | mabel.seroubian@seciu.edu.uy |
repository.name.fl_str_mv | COLIBRI - Universidad de la República |
repository_id_str | 4771 |
rights_invalid_str_mv | Licencia Creative Commons Atribución (CC - By 4.0) |
spelling | Müller JoachimPreza Pérez Matías Facundo, Universidad de la República (Uruguay). Facultad de Ciencias. Instituto de Biología.Kaethner MarcRufener RetoBraga SophieUldry Anne-ChristineHeller ManfredLundström-Stadelmann Britta2024-03-20T13:53:59Z2024-03-20T13:53:59Z2023Müller, 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.2023.1170763The 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.Submitted by Pintos Natalia (nataliapintosmvd@gmail.com) on 2024-03-19T16:19:35Z No. of bitstreams: 2 license_rdf: 24251 bytes, checksum: 71ed42ef0a0b648670f707320be37b90 (MD5) 10.3389.fcimb.2023.1170763.pdf: 2088946 bytes, checksum: e781e6c69ef0dc2cf6c76f1a10729d58 (MD5)Approved for entry into archive by Faget Cecilia (lfaget@fcien.edu.uy) on 2024-03-20T12:22:02Z (GMT) No. of bitstreams: 2 license_rdf: 24251 bytes, checksum: 71ed42ef0a0b648670f707320be37b90 (MD5) 10.3389.fcimb.2023.1170763.pdf: 2088946 bytes, checksum: e781e6c69ef0dc2cf6c76f1a10729d58 (MD5)Made available in DSpace by Luna Fabiana (fabiana.luna@seciu.edu.uy) on 2024-03-20T13:53:59Z (GMT). No. of bitstreams: 2 license_rdf: 24251 bytes, checksum: 71ed42ef0a0b648670f707320be37b90 (MD5) 10.3389.fcimb.2023.1170763.pdf: 2088946 bytes, checksum: e781e6c69ef0dc2cf6c76f1a10729d58 (MD5) Previous issue date: 202314 h.application/pdfenengFrontiersFrontiers 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)CestodesModel systemTargeted proteomicsTransportEchinococcosisUntargeted proteomicsAntigen BTargeted and non-targeted proteomics to characterize the parasite proteins of Echinococcus multilocularis metacestodesArtículoinfo:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionreponame:COLIBRIinstname:Universidad de la Repúblicainstacron:Universidad de la RepúblicaMüller, JoachimPreza Pérez, Matías FacundoKaethner, MarcRufener, RetoBraga, SophieUldry, Anne-ChristineHeller, ManfredLundström-Stadelmann, BrittaLICENSElicense.txtlicense.txttext/plain; charset=utf-84267http://localhost:8080/xmlui/bitstream/20.500.12008/43230/5/license.txt6429389a7df7277b72b7924fdc7d47a9MD55CC-LICENSElicense_urllicense_urltext/plain; charset=utf-844http://localhost:8080/xmlui/bitstream/20.500.12008/43230/2/license_urla0ebbeafb9d2ec7cbb19d7137ebc392cMD52license_textlicense_texttext/html; charset=utf-820277http://localhost:8080/xmlui/bitstream/20.500.12008/43230/3/license_text8010f418ede1186e294ac5448996bd7eMD53license_rdflicense_rdfapplication/rdf+xml; charset=utf-824251http://localhost:8080/xmlui/bitstream/20.500.12008/43230/4/license_rdf71ed42ef0a0b648670f707320be37b90MD54ORIGINAL10.3389.fcimb.2023.1170763.pdf10.3389.fcimb.2023.1170763.pdfapplication/pdf2088946http://localhost:8080/xmlui/bitstream/20.500.12008/43230/1/10.3389.fcimb.2023.1170763.pdfe781e6c69ef0dc2cf6c76f1a10729d58MD5120.500.12008/432302024-03-20 10:53:59.688oai:colibri.udelar.edu.uy:20.500.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Universidadhttps://udelar.edu.uy/https://www.colibri.udelar.edu.uy/oai/requestmabel.seroubian@seciu.edu.uyUruguayopendoar:47712024-07-25T14:29:26.317998COLIBRI - Universidad de la Repúblicafalse |
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 |