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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/32112
Acceder
id CONICETDig_b44740be9fd7851775f9e2ef82221cbf
oai_identifier_str oai:ri.conicet.gov.ar:11336/32112
network_acronym_str CONICETDig
repository_id_str 3498
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 Técnicas2025-10-22T11:15:55Zoai: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:34982025-10-22 11:15:56.111CONICET 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
_version_ 1846781599887130624
score 12.982451

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