GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila

Autores
Puca, Gervasio; Montes, Maria G.; Orlowski, Juan; Tomazic, Mariela Luján; Gonzalez Maglio, Daniel H.; de la Fuente, Carolina; Florin-Christensen, Mónica; Schnittger, Leonhard; Nusblat, Alejandro D.
Año de publicación
2025
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play essential roles in eukaryotic cell biology, yet their evolutionary diversity across alveolates remains poorly understood. Here, we conducted a comparative genomic analysis of GPI biosynthetic pathways and GPI-AP repertoires across representative species of Ciliophora, Apicomplexa, and Dinoflagellata. Our findings reveal lineage-specific patterns of gene loss, expansion, and functional divergence, with ciliates exhibiting reduced canonical enzyme sets but expanded trafficking components. Using a benchmarked pipeline of GPI-AP predictors combined with signal peptide detection, we identified candidate GPI-anchored proteins and performed functional annotation to determine enriched Gene Ontology terms. To complement the bioinformatic analyses, we expressed the apicomplexan GPI-anchored antigen GPI4 from Babesia bovis in Tetrahymena thermophila. This approach extends previous efforts that used Tetrahymena as a heterologous expression system for parasite surface antigens. The recombinant protein localized to ciliary membranes and showed features consistent with proper processing. This study highlights the evolutionary plasticity of GPI systems in alveolates and reinforces the utility of Tetrahymena as a eukaryotic platform for the production and analysis of GPI-anchored proteins with potential diagnostic or immunoprophylactic applications.
Instituto de Patobiología
Fil: Puca, Gervasio. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil; Puca, Gervasio. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Montes, Maria G. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Montes, Maria G. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Orlowski, Juan. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Orlowski, Juan. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Tomazic, Mariela Luján. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Tomazic, Mariela Luján. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Gonzalez Maglio, Daniel H. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); Argentina
Fil: Gonzalez Maglio, Daniel H. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); Argentina
Fil: de la Fuente, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: de la Fuente, Carolina. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Florin-Christensen, Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Schnittger, Leonhard. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Nusblat, Alejandro D. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Nusblat, Alejandro D. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fuente
Journal of Eukaryotic Microbiology 73 (1) : e70055 (January/February 2026)
Materia
Tetrahymena
Célula Eucariotica
Citología
Estructura Genética
Eukaryotic Cells
Cytology
Genetic Structures
Anchored Proteomes
Glycosylphosphatidylinositol
Proteomas Anclados
Glicosilfosfatidilinositol
Tetrahymena thermophila
Nivel de accesibilidad
acceso restringido
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
INTA Digital (INTA)
Institución
Instituto Nacional de Tecnología Agropecuaria
OAI Identificador
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spelling GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena ThermophilaPuca, GervasioMontes, Maria G.Orlowski, JuanTomazic, Mariela LujánGonzalez Maglio, Daniel H.de la Fuente, CarolinaFlorin-Christensen, MónicaSchnittger, LeonhardNusblat, Alejandro D.TetrahymenaCélula EucarioticaCitologíaEstructura GenéticaEukaryotic CellsCytologyGenetic StructuresAnchored ProteomesGlycosylphosphatidylinositolProteomas AncladosGlicosilfosfatidilinositolTetrahymena thermophilaGlycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play essential roles in eukaryotic cell biology, yet their evolutionary diversity across alveolates remains poorly understood. Here, we conducted a comparative genomic analysis of GPI biosynthetic pathways and GPI-AP repertoires across representative species of Ciliophora, Apicomplexa, and Dinoflagellata. Our findings reveal lineage-specific patterns of gene loss, expansion, and functional divergence, with ciliates exhibiting reduced canonical enzyme sets but expanded trafficking components. Using a benchmarked pipeline of GPI-AP predictors combined with signal peptide detection, we identified candidate GPI-anchored proteins and performed functional annotation to determine enriched Gene Ontology terms. To complement the bioinformatic analyses, we expressed the apicomplexan GPI-anchored antigen GPI4 from Babesia bovis in Tetrahymena thermophila. This approach extends previous efforts that used Tetrahymena as a heterologous expression system for parasite surface antigens. The recombinant protein localized to ciliary membranes and showed features consistent with proper processing. This study highlights the evolutionary plasticity of GPI systems in alveolates and reinforces the utility of Tetrahymena as a eukaryotic platform for the production and analysis of GPI-anchored proteins with potential diagnostic or immunoprophylactic applications.Instituto de PatobiologíaFil: Puca, Gervasio. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil; Puca, Gervasio. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Montes, Maria G. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Montes, Maria G. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Orlowski, Juan. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Orlowski, Juan. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Tomazic, Mariela Luján. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; ArgentinaFil: Tomazic, Mariela Luján. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); ArgentinaFil: Gonzalez Maglio, Daniel H. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); ArgentinaFil: Gonzalez Maglio, Daniel H. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); ArgentinaFil: de la Fuente, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: de la Fuente, Carolina. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; ArgentinaFil: Florin-Christensen, Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); ArgentinaFil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; ArgentinaFil: Schnittger, Leonhard. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); ArgentinaFil: Nusblat, Alejandro D. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaFil: Nusblat, Alejandro D. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); ArgentinaWiley2025-12-30T12:29:39Z2025-12-30T12:29:39Z2025-11info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfhttp://hdl.handle.net/20.500.12123/24811https://onlinelibrary.wiley.com/doi/10.1111/jeu.700551550-74081066-5234https://doi.org/10.1111/jeu.70055Journal of Eukaryotic Microbiology 73 (1) : e70055 (January/February 2026)reponame:INTA Digital (INTA)instname:Instituto Nacional de Tecnología Agropecuariaenginfo:eu-repo/semantics/restrictedAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)2026-01-08T10:41:01Zoai:localhost:20.500.12123/24811instacron:INTAInstitucionalhttp://repositorio.inta.gob.ar/Organismo científico-tecnológicoNo correspondehttp://repositorio.inta.gob.ar/oai/requesttripaldi.nicolas@inta.gob.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:l2026-01-08 10:41:01.687INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuariafalse
dc.title.none.fl_str_mv GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
title GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
spellingShingle GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
Puca, Gervasio
Tetrahymena
Célula Eucariotica
Citología
Estructura Genética
Eukaryotic Cells
Cytology
Genetic Structures
Anchored Proteomes
Glycosylphosphatidylinositol
Proteomas Anclados
Glicosilfosfatidilinositol
Tetrahymena thermophila
title_short GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
title_full GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
title_fullStr GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
title_full_unstemmed GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
title_sort GPI- Anchored Proteomes and Their Biochemical Pathway in Alveolates: Evolutionary Insights and Heterologous Expression in Tetrahymena Thermophila
dc.creator.none.fl_str_mv Puca, Gervasio
Montes, Maria G.
Orlowski, Juan
Tomazic, Mariela Luján
Gonzalez Maglio, Daniel H.
de la Fuente, Carolina
Florin-Christensen, Mónica
Schnittger, Leonhard
Nusblat, Alejandro D.
author Puca, Gervasio
author_facet Puca, Gervasio
Montes, Maria G.
Orlowski, Juan
Tomazic, Mariela Luján
Gonzalez Maglio, Daniel H.
de la Fuente, Carolina
Florin-Christensen, Mónica
Schnittger, Leonhard
Nusblat, Alejandro D.
author_role author
author2 Montes, Maria G.
Orlowski, Juan
Tomazic, Mariela Luján
Gonzalez Maglio, Daniel H.
de la Fuente, Carolina
Florin-Christensen, Mónica
Schnittger, Leonhard
Nusblat, Alejandro D.
author2_role author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Tetrahymena
Célula Eucariotica
Citología
Estructura Genética
Eukaryotic Cells
Cytology
Genetic Structures
Anchored Proteomes
Glycosylphosphatidylinositol
Proteomas Anclados
Glicosilfosfatidilinositol
Tetrahymena thermophila
topic Tetrahymena
Célula Eucariotica
Citología
Estructura Genética
Eukaryotic Cells
Cytology
Genetic Structures
Anchored Proteomes
Glycosylphosphatidylinositol
Proteomas Anclados
Glicosilfosfatidilinositol
Tetrahymena thermophila
dc.description.none.fl_txt_mv Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play essential roles in eukaryotic cell biology, yet their evolutionary diversity across alveolates remains poorly understood. Here, we conducted a comparative genomic analysis of GPI biosynthetic pathways and GPI-AP repertoires across representative species of Ciliophora, Apicomplexa, and Dinoflagellata. Our findings reveal lineage-specific patterns of gene loss, expansion, and functional divergence, with ciliates exhibiting reduced canonical enzyme sets but expanded trafficking components. Using a benchmarked pipeline of GPI-AP predictors combined with signal peptide detection, we identified candidate GPI-anchored proteins and performed functional annotation to determine enriched Gene Ontology terms. To complement the bioinformatic analyses, we expressed the apicomplexan GPI-anchored antigen GPI4 from Babesia bovis in Tetrahymena thermophila. This approach extends previous efforts that used Tetrahymena as a heterologous expression system for parasite surface antigens. The recombinant protein localized to ciliary membranes and showed features consistent with proper processing. This study highlights the evolutionary plasticity of GPI systems in alveolates and reinforces the utility of Tetrahymena as a eukaryotic platform for the production and analysis of GPI-anchored proteins with potential diagnostic or immunoprophylactic applications.
Instituto de Patobiología
Fil: Puca, Gervasio. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil; Puca, Gervasio. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Montes, Maria G. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Montes, Maria G. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Orlowski, Juan. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Orlowski, Juan. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Tomazic, Mariela Luján. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Tomazic, Mariela Luján. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Gonzalez Maglio, Daniel H. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); Argentina
Fil: Gonzalez Maglio, Daniel H. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Estudios de la Inmunidad Humoral Prof. Ricardo A. Margni (IDEHU); Argentina
Fil: de la Fuente, Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: de la Fuente, Carolina. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Florin-Christensen, Mónica. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Florin-Christensen, Mónica. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Schnittger, Leonhard. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Patobiología Veterinaria; Argentina
Fil: Schnittger, Leonhard. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET); Argentina
Fil: Nusblat, Alejandro D. Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
Fil: Nusblat, Alejandro D. Universidad de Buenos Aires (UBA). Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología (NANOBIOTEC); Argentina
description Glycosylphosphatidylinositol (GPI)-anchored proteins (GPI-APs) play essential roles in eukaryotic cell biology, yet their evolutionary diversity across alveolates remains poorly understood. Here, we conducted a comparative genomic analysis of GPI biosynthetic pathways and GPI-AP repertoires across representative species of Ciliophora, Apicomplexa, and Dinoflagellata. Our findings reveal lineage-specific patterns of gene loss, expansion, and functional divergence, with ciliates exhibiting reduced canonical enzyme sets but expanded trafficking components. Using a benchmarked pipeline of GPI-AP predictors combined with signal peptide detection, we identified candidate GPI-anchored proteins and performed functional annotation to determine enriched Gene Ontology terms. To complement the bioinformatic analyses, we expressed the apicomplexan GPI-anchored antigen GPI4 from Babesia bovis in Tetrahymena thermophila. This approach extends previous efforts that used Tetrahymena as a heterologous expression system for parasite surface antigens. The recombinant protein localized to ciliary membranes and showed features consistent with proper processing. This study highlights the evolutionary plasticity of GPI systems in alveolates and reinforces the utility of Tetrahymena as a eukaryotic platform for the production and analysis of GPI-anchored proteins with potential diagnostic or immunoprophylactic applications.
publishDate 2025
dc.date.none.fl_str_mv 2025-12-30T12:29:39Z
2025-12-30T12:29:39Z
2025-11
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
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info:ar-repo/semantics/articulo
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status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/20.500.12123/24811
https://onlinelibrary.wiley.com/doi/10.1111/jeu.70055
1550-7408
1066-5234
https://doi.org/10.1111/jeu.70055
url http://hdl.handle.net/20.500.12123/24811
https://onlinelibrary.wiley.com/doi/10.1111/jeu.70055
https://doi.org/10.1111/jeu.70055
identifier_str_mv 1550-7408
1066-5234
dc.language.none.fl_str_mv eng
language eng
dc.rights.none.fl_str_mv info:eu-repo/semantics/restrictedAccess
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Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv restrictedAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Wiley
publisher.none.fl_str_mv Wiley
dc.source.none.fl_str_mv Journal of Eukaryotic Microbiology 73 (1) : e70055 (January/February 2026)
reponame:INTA Digital (INTA)
instname:Instituto Nacional de Tecnología Agropecuaria
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repository.name.fl_str_mv INTA Digital (INTA) - Instituto Nacional de Tecnología Agropecuaria
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