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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Main Author: Müller, Joachim (author)
Other Authors: Preza Pérez, Matías Facundo (author), Kaethner, Marc (author), Rufener, Reto (author), Braga, Sophie (author), Uldry, Anne-Christine (author), Heller, Manfred (author), Lundström-Stadelmann, Britta (author)
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Language:English
Published: 2023
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Online Access:https://hdl.handle.net/20.500.12008/43230
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_version_ 1868890208010764288
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