Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity
- Autores
- Pedrera, Lohans; Fanani, Maria Laura; Ros, Uris; Lanio, Maria E.; Maggio, Bruno; Alvarez, Carlos
- Año de publicación
- 2014
- 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 exclusively found in sea anemones. As for actinoporins, it has been proposed that the presence of sphingomyelin (SM) and the coexistence of lipid phases increase binding to the target membrane. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, presence of lipid domains) on actinoporins' activity or which regions of the membrane are the most favorable platforms for protein insertion. To gain insight into the role of SM on the interaction of St I to lipid membranes we studied their binding to monolayers of phosphatidylcholine (PC) and SM in different proportions. Additionally, the effect of acyl chain length and unsaturation, two features related to membrane fluidity, was evaluated on St I binding to monolayers. This study revealed that St I binds and penetrates preferentially and with a faster kinetic to liquid-expanded films with high lateral mobility and moderately enriched in SM. A high content of SM induces a lower lateral diffusion and/or liquid-condensed phases, which hinder St I binding and penetration to the lipid monolayer. Furthermore, the presence of lipid domain borders does not appear as an important factor for St I binding to the lipid monolayer.
Fil: Pedrera, Lohans. Universidad de la Habana; Cuba
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: Ros, Uris. Universidad de la Habana; Cuba
Fil: Lanio, Maria E.. Universidad de la Habana; Cuba
Fil: Maggio, Bruno. 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: Alvarez, Carlos. Universidad de la Habana; Cuba - Materia
-
Sticholysin
Actinoporin
Sphingomyelin
Membrane Fluidity
Lipid Monolayer
Lipid Phase Separation - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/32112
Ver los metadatos del registro completo
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network_name_str |
CONICET Digital (CONICET) |
spelling |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidityPedrera, LohansFanani, Maria LauraRos, UrisLanio, Maria E.Maggio, BrunoAlvarez, CarlosSticholysinActinoporinSphingomyelinMembrane FluidityLipid MonolayerLipid Phase Separationhttps://purl.org/becyt/ford/1.4https://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 exclusively found in sea anemones. As for actinoporins, it has been proposed that the presence of sphingomyelin (SM) and the coexistence of lipid phases increase binding to the target membrane. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, presence of lipid domains) on actinoporins' activity or which regions of the membrane are the most favorable platforms for protein insertion. To gain insight into the role of SM on the interaction of St I to lipid membranes we studied their binding to monolayers of phosphatidylcholine (PC) and SM in different proportions. Additionally, the effect of acyl chain length and unsaturation, two features related to membrane fluidity, was evaluated on St I binding to monolayers. This study revealed that St I binds and penetrates preferentially and with a faster kinetic to liquid-expanded films with high lateral mobility and moderately enriched in SM. A high content of SM induces a lower lateral diffusion and/or liquid-condensed phases, which hinder St I binding and penetration to the lipid monolayer. Furthermore, the presence of lipid domain borders does not appear as an important factor for St I binding to the lipid monolayer.Fil: Pedrera, Lohans. Universidad de la Habana; CubaFil: 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: Ros, Uris. Universidad de la Habana; CubaFil: Lanio, Maria E.. Universidad de la Habana; CubaFil: Maggio, Bruno. 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: Alvarez, Carlos. Universidad de la Habana; CubaElsevier Science2014-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/32112Alvarez, Carlos; Maggio, Bruno; Lanio, Maria E.; Ros, Uris; Fanani, Maria Laura; Pedrera, Lohans; et al.; Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 7; 1-2014; 1752-17590005-2736CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273614001059info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2014.03.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:47:05Zoai:ri.conicet.gov.ar:11336/32112instacron: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 09:47:05.324CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
title |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
spellingShingle |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity Pedrera, Lohans Sticholysin Actinoporin Sphingomyelin Membrane Fluidity Lipid Monolayer Lipid Phase Separation |
title_short |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
title_full |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
title_fullStr |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
title_full_unstemmed |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
title_sort |
Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity |
dc.creator.none.fl_str_mv |
Pedrera, Lohans Fanani, Maria Laura Ros, Uris Lanio, Maria E. Maggio, Bruno Alvarez, Carlos |
author |
Pedrera, Lohans |
author_facet |
Pedrera, Lohans Fanani, Maria Laura Ros, Uris Lanio, Maria E. Maggio, Bruno Alvarez, Carlos |
author_role |
author |
author2 |
Fanani, Maria Laura Ros, Uris Lanio, Maria E. Maggio, Bruno Alvarez, Carlos |
author2_role |
author author author author author |
dc.subject.none.fl_str_mv |
Sticholysin Actinoporin Sphingomyelin Membrane Fluidity Lipid Monolayer Lipid Phase Separation |
topic |
Sticholysin Actinoporin Sphingomyelin Membrane Fluidity Lipid Monolayer Lipid Phase Separation |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.4 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 exclusively found in sea anemones. As for actinoporins, it has been proposed that the presence of sphingomyelin (SM) and the coexistence of lipid phases increase binding to the target membrane. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, presence of lipid domains) on actinoporins' activity or which regions of the membrane are the most favorable platforms for protein insertion. To gain insight into the role of SM on the interaction of St I to lipid membranes we studied their binding to monolayers of phosphatidylcholine (PC) and SM in different proportions. Additionally, the effect of acyl chain length and unsaturation, two features related to membrane fluidity, was evaluated on St I binding to monolayers. This study revealed that St I binds and penetrates preferentially and with a faster kinetic to liquid-expanded films with high lateral mobility and moderately enriched in SM. A high content of SM induces a lower lateral diffusion and/or liquid-condensed phases, which hinder St I binding and penetration to the lipid monolayer. Furthermore, the presence of lipid domain borders does not appear as an important factor for St I binding to the lipid monolayer. Fil: Pedrera, Lohans. Universidad de la Habana; Cuba 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: Ros, Uris. Universidad de la Habana; Cuba Fil: Lanio, Maria E.. Universidad de la Habana; Cuba Fil: Maggio, Bruno. 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: Alvarez, Carlos. 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 exclusively found in sea anemones. As for actinoporins, it has been proposed that the presence of sphingomyelin (SM) and the coexistence of lipid phases increase binding to the target membrane. However, little is known about the role of membrane structure and dynamics (phase state, fluidity, presence of lipid domains) on actinoporins' activity or which regions of the membrane are the most favorable platforms for protein insertion. To gain insight into the role of SM on the interaction of St I to lipid membranes we studied their binding to monolayers of phosphatidylcholine (PC) and SM in different proportions. Additionally, the effect of acyl chain length and unsaturation, two features related to membrane fluidity, was evaluated on St I binding to monolayers. This study revealed that St I binds and penetrates preferentially and with a faster kinetic to liquid-expanded films with high lateral mobility and moderately enriched in SM. A high content of SM induces a lower lateral diffusion and/or liquid-condensed phases, which hinder St I binding and penetration to the lipid monolayer. Furthermore, the presence of lipid domain borders does not appear as an important factor for St I binding to the lipid monolayer. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-01 |
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/11336/32112 Alvarez, Carlos; Maggio, Bruno; Lanio, Maria E.; Ros, Uris; Fanani, Maria Laura; Pedrera, Lohans; et al.; Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 7; 1-2014; 1752-1759 0005-2736 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/32112 |
identifier_str_mv |
Alvarez, Carlos; Maggio, Bruno; Lanio, Maria E.; Ros, Uris; Fanani, Maria Laura; Pedrera, Lohans; et al.; Sticholysin I–membrane interaction: An interplay between the presence of sphingomyelin and membrane fluidity; Elsevier Science; Biochimica et Biophysica Acta - Biomembranes; 1838; 7; 1-2014; 1752-1759 0005-2736 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S0005273614001059 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.bbamem.2014.03.011 |
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 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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1844613467382743040 |
score |
13.070432 |