The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains

Autores
Pedrera Puentes, Lohans; Gomide, Andreza. B.; Sanchez, Rafael E.; Ros Quincoces, Uris; Wilke, Natalia; Pazos, Fabiola; Lanio, María E.; Itri, Rosangela; Fanani, Maria Laura; Álvarez Valcárcel, Carlos Manuel
Año de publicación
2015
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Sticholysin I (St I) is a pore-forming toxin (PFT) produced by the Caribbean Sea anemone Stichodactyla helianthus belonging to the actinoporin protein family, a unique class of eukaryotic PFT. As for actinoporins, it has been proposed that the presence of cholesterol (Chol) and the coexistence of lipid phases increase binding to the target membrane and pore-forming ability. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, and the presence of lipid domains) on the activity of actinoporins or which regions of the membrane are the most favorable for protein insertion, oligomerization, and eventually pore formation. To gain insight into the role of membrane properties on the functional activity of St I, we studied its binding to monolayers and vesicles of phosphatidylcholine (PC), sphingomyelin (SM), and sterols inducing (ergosterol -Erg and cholesterol -Chol) or not (cholestenone - Cln) membrane phase segregation in liquid ordered (Lo) and liquid disordered (Ld) domains. This study revealed that St I binds and permeabilizes with higher efficiency sterol-containing membranes independently of their ability to form domains. We discuss the results in terms of the relevance of different membrane properties for the actinoporins mechanism of action, namely, molecular heterogeneity, specially potentiated in membranes with sterols inducers of phase separation (Chol or Erg) or Cln, a sterol noninducer of phase separation but with a high propensity to induce nonlamellar phase. The role of the Ld phase is pointed out as the most suitable platform for pore formation. In this regard, such regions in Chol-containing membranes seem to be the most favored due to its increased fluidity; this property promotes toxin insertion, diffusion, and oligomerization leading to pore formation.
Fil: Pedrera Puentes, Lohans. Universidad de La Habana; Cuba
Fil: Gomide, Andreza. B.. Universidade de Sao Paulo; Brasil
Fil: Sanchez, Rafael E.. Universidad de La Habana; Cuba
Fil: Ros Quincoces, Uris. Universidad de La Habana; Cuba
Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Pazos, Fabiola. Universidad de La Habana; Cuba
Fil: Lanio, María E.. Universidad de La Habana; Cuba
Fil: Itri, Rosangela. Universidade de Sao Paulo; Brasil
Fil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Álvarez Valcárcel, Carlos Manuel. Universidad de La Habana; Cuba
Materia
Actioporins
Lipid Monolayers
Liquid - Ordered Domains
Giant Unilamellar Vesicles
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/50816
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/50816
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domainsPedrera Puentes, LohansGomide, Andreza. B.Sanchez, Rafael E.Ros Quincoces, UrisWilke, NataliaPazos, FabiolaLanio, María E.Itri, RosangelaFanani, Maria LauraÁlvarez Valcárcel, Carlos ManuelActioporinsLipid MonolayersLiquid - Ordered DomainsGiant Unilamellar Vesicleshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Sticholysin I (St I) is a pore-forming toxin (PFT) produced by the Caribbean Sea anemone Stichodactyla helianthus belonging to the actinoporin protein family, a unique class of eukaryotic PFT. As for actinoporins, it has been proposed that the presence of cholesterol (Chol) and the coexistence of lipid phases increase binding to the target membrane and pore-forming ability. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, and the presence of lipid domains) on the activity of actinoporins or which regions of the membrane are the most favorable for protein insertion, oligomerization, and eventually pore formation. To gain insight into the role of membrane properties on the functional activity of St I, we studied its binding to monolayers and vesicles of phosphatidylcholine (PC), sphingomyelin (SM), and sterols inducing (ergosterol -Erg and cholesterol -Chol) or not (cholestenone - Cln) membrane phase segregation in liquid ordered (Lo) and liquid disordered (Ld) domains. This study revealed that St I binds and permeabilizes with higher efficiency sterol-containing membranes independently of their ability to form domains. We discuss the results in terms of the relevance of different membrane properties for the actinoporins mechanism of action, namely, molecular heterogeneity, specially potentiated in membranes with sterols inducers of phase separation (Chol or Erg) or Cln, a sterol noninducer of phase separation but with a high propensity to induce nonlamellar phase. The role of the Ld phase is pointed out as the most suitable platform for pore formation. In this regard, such regions in Chol-containing membranes seem to be the most favored due to its increased fluidity; this property promotes toxin insertion, diffusion, and oligomerization leading to pore formation.Fil: Pedrera Puentes, Lohans. Universidad de La Habana; CubaFil: Gomide, Andreza. B.. Universidade de Sao Paulo; BrasilFil: Sanchez, Rafael E.. Universidad de La Habana; CubaFil: Ros Quincoces, Uris. Universidad de La Habana; CubaFil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Pazos, Fabiola. Universidad de La Habana; CubaFil: Lanio, María E.. Universidad de La Habana; CubaFil: Itri, Rosangela. Universidade de Sao Paulo; BrasilFil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; ArgentinaFil: Álvarez Valcárcel, Carlos Manuel. Universidad de La Habana; CubaAmerican Chemical Society2015-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/50816Pedrera Puentes, Lohans; Gomide, Andreza. B.; Sanchez, Rafael E.; Ros Quincoces, Uris; Wilke, Natalia; et al.; The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains; American Chemical Society; Langmuir; 31; 36; 9-2015; 9911-99230743-74631520-5827CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1021/acs.langmuir.5b01687info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.langmuir.5b01687info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:56:30Zoai:ri.conicet.gov.ar:11336/50816instacron: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:34982025-09-29 09:56:30.876CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
title The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
spellingShingle The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
Pedrera Puentes, Lohans
Actioporins
Lipid Monolayers
Liquid - Ordered Domains
Giant Unilamellar Vesicles
title_short The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
title_full The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
title_fullStr The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
title_full_unstemmed The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
title_sort The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains
dc.creator.none.fl_str_mv Pedrera Puentes, Lohans
Gomide, Andreza. B.
Sanchez, Rafael E.
Ros Quincoces, Uris
Wilke, Natalia
Pazos, Fabiola
Lanio, María E.
Itri, Rosangela
Fanani, Maria Laura
Álvarez Valcárcel, Carlos Manuel
author Pedrera Puentes, Lohans
author_facet Pedrera Puentes, Lohans
Gomide, Andreza. B.
Sanchez, Rafael E.
Ros Quincoces, Uris
Wilke, Natalia
Pazos, Fabiola
Lanio, María E.
Itri, Rosangela
Fanani, Maria Laura
Álvarez Valcárcel, Carlos Manuel
author_role author
author2 Gomide, Andreza. B.
Sanchez, Rafael E.
Ros Quincoces, Uris
Wilke, Natalia
Pazos, Fabiola
Lanio, María E.
Itri, Rosangela
Fanani, Maria Laura
Álvarez Valcárcel, Carlos Manuel
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Actioporins
Lipid Monolayers
Liquid - Ordered Domains
Giant Unilamellar Vesicles
topic Actioporins
Lipid Monolayers
Liquid - Ordered Domains
Giant Unilamellar Vesicles
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Sticholysin I (St I) is a pore-forming toxin (PFT) produced by the Caribbean Sea anemone Stichodactyla helianthus belonging to the actinoporin protein family, a unique class of eukaryotic PFT. As for actinoporins, it has been proposed that the presence of cholesterol (Chol) and the coexistence of lipid phases increase binding to the target membrane and pore-forming ability. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, and the presence of lipid domains) on the activity of actinoporins or which regions of the membrane are the most favorable for protein insertion, oligomerization, and eventually pore formation. To gain insight into the role of membrane properties on the functional activity of St I, we studied its binding to monolayers and vesicles of phosphatidylcholine (PC), sphingomyelin (SM), and sterols inducing (ergosterol -Erg and cholesterol -Chol) or not (cholestenone - Cln) membrane phase segregation in liquid ordered (Lo) and liquid disordered (Ld) domains. This study revealed that St I binds and permeabilizes with higher efficiency sterol-containing membranes independently of their ability to form domains. We discuss the results in terms of the relevance of different membrane properties for the actinoporins mechanism of action, namely, molecular heterogeneity, specially potentiated in membranes with sterols inducers of phase separation (Chol or Erg) or Cln, a sterol noninducer of phase separation but with a high propensity to induce nonlamellar phase. The role of the Ld phase is pointed out as the most suitable platform for pore formation. In this regard, such regions in Chol-containing membranes seem to be the most favored due to its increased fluidity; this property promotes toxin insertion, diffusion, and oligomerization leading to pore formation.
Fil: Pedrera Puentes, Lohans. Universidad de La Habana; Cuba
Fil: Gomide, Andreza. B.. Universidade de Sao Paulo; Brasil
Fil: Sanchez, Rafael E.. Universidad de La Habana; Cuba
Fil: Ros Quincoces, Uris. Universidad de La Habana; Cuba
Fil: Wilke, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Pazos, Fabiola. Universidad de La Habana; Cuba
Fil: Lanio, María E.. Universidad de La Habana; Cuba
Fil: Itri, Rosangela. Universidade de Sao Paulo; Brasil
Fil: Fanani, Maria Laura. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Córdoba. Centro de Investigaciones en Química Biológica de Córdoba. Universidad Nacional de Córdoba. Facultad de Ciencias Químicas. Centro de Investigaciones en Química Biológica de Córdoba; Argentina
Fil: Álvarez Valcárcel, Carlos Manuel. Universidad de La Habana; Cuba
description Sticholysin I (St I) is a pore-forming toxin (PFT) produced by the Caribbean Sea anemone Stichodactyla helianthus belonging to the actinoporin protein family, a unique class of eukaryotic PFT. As for actinoporins, it has been proposed that the presence of cholesterol (Chol) and the coexistence of lipid phases increase binding to the target membrane and pore-forming ability. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, and the presence of lipid domains) on the activity of actinoporins or which regions of the membrane are the most favorable for protein insertion, oligomerization, and eventually pore formation. To gain insight into the role of membrane properties on the functional activity of St I, we studied its binding to monolayers and vesicles of phosphatidylcholine (PC), sphingomyelin (SM), and sterols inducing (ergosterol -Erg and cholesterol -Chol) or not (cholestenone - Cln) membrane phase segregation in liquid ordered (Lo) and liquid disordered (Ld) domains. This study revealed that St I binds and permeabilizes with higher efficiency sterol-containing membranes independently of their ability to form domains. We discuss the results in terms of the relevance of different membrane properties for the actinoporins mechanism of action, namely, molecular heterogeneity, specially potentiated in membranes with sterols inducers of phase separation (Chol or Erg) or Cln, a sterol noninducer of phase separation but with a high propensity to induce nonlamellar phase. The role of the Ld phase is pointed out as the most suitable platform for pore formation. In this regard, such regions in Chol-containing membranes seem to be the most favored due to its increased fluidity; this property promotes toxin insertion, diffusion, and oligomerization leading to pore formation.
publishDate 2015
dc.date.none.fl_str_mv 2015-09
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/11336/50816
Pedrera Puentes, Lohans; Gomide, Andreza. B.; Sanchez, Rafael E.; Ros Quincoces, Uris; Wilke, Natalia; et al.; The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains; American Chemical Society; Langmuir; 31; 36; 9-2015; 9911-9923
0743-7463
1520-5827
CONICET Digital
CONICET
url http://hdl.handle.net/11336/50816
identifier_str_mv Pedrera Puentes, Lohans; Gomide, Andreza. B.; Sanchez, Rafael E.; Ros Quincoces, Uris; Wilke, Natalia; et al.; The presence of sterols favors Sticholysin I - membrane association and pore formation regardless of their ability to form laterally segregated domains; American Chemical Society; Langmuir; 31; 36; 9-2015; 9911-9923
0743-7463
1520-5827
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1021/acs.langmuir.5b01687
info:eu-repo/semantics/altIdentifier/url/https://pubs.acs.org/doi/10.1021/acs.langmuir.5b01687
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
dc.publisher.none.fl_str_mv American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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 13.070432

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