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
.jpg)
- Institución
- Instituto Nacional de Tecnología Agropecuaria
- OAI Identificador
- oai:localhost:20.500.12123/24811
Ver los metadatos del registro completo
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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. |
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2025 |
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2025-12-30T12:29:39Z 2025-12-30T12:29:39Z 2025-11 |
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