Identification of new palmitoylated proteins in Toxoplasma gondii

Autores
Caballero, Marina; Alonso, Andrés Mariano; Deng, Bin; Attias, Marcia; De Souza, Wanderley; Corvi, Maria Martha
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.
Fil: Caballero, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
Fil: Alonso, Andrés Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
Fil: Deng, Bin. University of Vermont; Estados Unidos
Fil: Attias, Marcia. Universidade Federal do Rio de Janeiro; Brasil
Fil: De Souza, Wanderley. Universidade Federal do Rio de Janeiro; Brasil
Fil: Corvi, Maria Martha. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
Materia
Acyl-Biotin Exchange
Host-Cell Invasion
Palmitoylome
Protein Identification
Rhoptry
Toxoplasma Gondii
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/53623
Acceder
id CONICETDig_2025ea4d095e5332467266600765c111
oai_identifier_str oai:ri.conicet.gov.ar:11336/53623
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Identification of new palmitoylated proteins in Toxoplasma gondiiCaballero, MarinaAlonso, Andrés MarianoDeng, BinAttias, MarciaDe Souza, WanderleyCorvi, Maria MarthaAcyl-Biotin ExchangeHost-Cell InvasionPalmitoylomeProtein IdentificationRhoptryToxoplasma Gondiihttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.Fil: Caballero, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; ArgentinaFil: Alonso, Andrés Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; ArgentinaFil: Deng, Bin. University of Vermont; Estados UnidosFil: Attias, Marcia. Universidade Federal do Rio de Janeiro; BrasilFil: De Souza, Wanderley. Universidade Federal do Rio de Janeiro; BrasilFil: Corvi, Maria Martha. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; ArgentinaElsevier Science2016-04info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/53623Caballero, Marina; Alonso, Andrés Mariano; Deng, Bin; Attias, Marcia; De Souza, Wanderley; et al.; Identification of new palmitoylated proteins in Toxoplasma gondii; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1864; 4; 4-2016; 400-4081570-9639CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2016.01.010info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1570963916300024info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4857766/info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-nd/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-08-25T14:37:45Zoai:ri.conicet.gov.ar:11336/53623instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982026-08-25 14:37:45.613CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Identification of new palmitoylated proteins in Toxoplasma gondii
title Identification of new palmitoylated proteins in Toxoplasma gondii
spellingShingle Identification of new palmitoylated proteins in Toxoplasma gondii
Caballero, Marina
Acyl-Biotin Exchange
Host-Cell Invasion
Palmitoylome
Protein Identification
Rhoptry
Toxoplasma Gondii
title_short Identification of new palmitoylated proteins in Toxoplasma gondii
title_full Identification of new palmitoylated proteins in Toxoplasma gondii
title_fullStr Identification of new palmitoylated proteins in Toxoplasma gondii
title_full_unstemmed Identification of new palmitoylated proteins in Toxoplasma gondii
title_sort Identification of new palmitoylated proteins in Toxoplasma gondii
dc.creator.none.fl_str_mv Caballero, Marina
Alonso, Andrés Mariano
Deng, Bin
Attias, Marcia
De Souza, Wanderley
Corvi, Maria Martha
author Caballero, Marina
author_facet Caballero, Marina
Alonso, Andrés Mariano
Deng, Bin
Attias, Marcia
De Souza, Wanderley
Corvi, Maria Martha
author_role author
author2 Alonso, Andrés Mariano
Deng, Bin
Attias, Marcia
De Souza, Wanderley
Corvi, Maria Martha
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Acyl-Biotin Exchange
Host-Cell Invasion
Palmitoylome
Protein Identification
Rhoptry
Toxoplasma Gondii
topic Acyl-Biotin Exchange
Host-Cell Invasion
Palmitoylome
Protein Identification
Rhoptry
Toxoplasma Gondii
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.
Fil: Caballero, Marina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
Fil: Alonso, Andrés Mariano. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
Fil: Deng, Bin. University of Vermont; Estados Unidos
Fil: Attias, Marcia. Universidade Federal do Rio de Janeiro; Brasil
Fil: De Souza, Wanderley. Universidade Federal do Rio de Janeiro; Brasil
Fil: Corvi, Maria Martha. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Instituto de Investigaciones Biotecnológicas. Instituto de Investigaciones Biotecnológicas ; Argentina
description Protein palmitoylation has been shown to be an important post-translational modification in eukaryotic cells. This modification alters the localization and/or the function of the targeted protein. In recent years, protein palmitoylation has risen in importance in apicomplexan parasites as well. In Toxoplasma gondii, some proteins have been reported to be modified by palmitate. With the development of new techniques that allow the isolation of palmitoylated proteins, this significant post-translational modification has begun to be studied in more detail in T. gondii. Here we describe the palmitoylome of the tachyzoite stage of T. gondii using a combination of the acyl-biotin exchange chemistry method and mass spectrometry analysis. We identified 401 proteins found in multiple cellular compartments, with a wide range of functions that vary from metabolic processes, gliding and host-cell invasion to even regulation of transcription and translation. Besides, we found that more rhoptry proteins than the ones already described for Toxoplasma are palmitoylated, suggesting an important role for this modification in the invasion mechanism of the host-cell. This study documents that protein palmitoylation is a common modification in T. gondii that could have an impact on different cellular processes.
publishDate 2016
dc.date.none.fl_str_mv 2016-04
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
http://purl.org/coar/resource_type/c_6501
info:ar-repo/semantics/articulo
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/53623
Caballero, Marina; Alonso, Andrés Mariano; Deng, Bin; Attias, Marcia; De Souza, Wanderley; et al.; Identification of new palmitoylated proteins in Toxoplasma gondii; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1864; 4; 4-2016; 400-408
1570-9639
CONICET Digital
CONICET
url http://hdl.handle.net/11336/53623
identifier_str_mv Caballero, Marina; Alonso, Andrés Mariano; Deng, Bin; Attias, Marcia; De Souza, Wanderley; et al.; Identification of new palmitoylated proteins in Toxoplasma gondii; Elsevier Science; Biochimica Et Biophysica Acta-proteins And Proteomics; 1864; 4; 4-2016; 400-408
1570-9639
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbapap.2016.01.010
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S1570963916300024
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4857766/
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-nd/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Elsevier Science
publisher.none.fl_str_mv Elsevier Science
dc.source.none.fl_str_mv reponame:CONICET Digital (CONICET)
instname:Consejo Nacional de Investigaciones Científicas y Técnicas
reponame_str CONICET Digital (CONICET)
collection CONICET Digital (CONICET)
instname_str Consejo Nacional de Investigaciones Científicas y Técnicas
repository.name.fl_str_mv CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas
repository.mail.fl_str_mv dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar
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score 13.364332

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