Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes

Autores
Bakás, Laura Susana; Chanturiya, Alexandr; Herlax, Vanesa Silvana; Zimmerberg, Joshua
Año de publicación
2006
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
α-Hemolysin (HlyA) is an extracellular protein toxin (117 kDa) secreted by Escherichia coli that targets the plasma membranes of eukaryotic cells. We studied the interaction of this toxin with membranes using planar phospholipid bilayers. For all lipid mixtures tested, addition of nanomolar concentrations of toxin resulted in an increase of membrane conductance and a decrease in membrane stability. HlyA decreased membrane lifetime up to three orders of magnitude in a voltage-dependent manner. Using a theory for lipidic pore formation, we analyzed these data to quantify how HlyA diminished the line tension of the membrane (i.e., the energy required to form the edge of a new pore). However, in contrast to the expectation that adding the positive curvature agent lysophosphatidylcholine would synergistically lower line tension, its addition significantly stabilized HlyA-treated membranes. HlyA also appeared to thicken bilayers to which it was added. We discuss these results in terms of models for proteolipidic pores.
Facultad de Ciencias Exactas
Instituto de Investigaciones Bioquímicas de La Plata
Materia
Ciencias Exactas
Escherichia coli
Planar Phospholipid Bilayer Membranes
Nivel de accesibilidad
acceso abierto
Condiciones de uso
http://creativecommons.org/licenses/by-nc-sa/4.0/
Repositorio
SEDICI (UNLP)
Institución
Universidad Nacional de La Plata
OAI Identificador
oai:sedici.unlp.edu.ar:10915/83200
Acceder
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oai_identifier_str oai:sedici.unlp.edu.ar:10915/83200
network_acronym_str SEDICI
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network_name_str SEDICI (UNLP)
spelling Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranesBakás, Laura SusanaChanturiya, AlexandrHerlax, Vanesa SilvanaZimmerberg, JoshuaCiencias ExactasEscherichia coliPlanar Phospholipid Bilayer Membranesα-Hemolysin (HlyA) is an extracellular protein toxin (117 kDa) secreted by <i>Escherichia coli</i> that targets the plasma membranes of eukaryotic cells. We studied the interaction of this toxin with membranes using planar phospholipid bilayers. For all lipid mixtures tested, addition of nanomolar concentrations of toxin resulted in an increase of membrane conductance and a decrease in membrane stability. HlyA decreased membrane lifetime up to three orders of magnitude in a voltage-dependent manner. Using a theory for lipidic pore formation, we analyzed these data to quantify how HlyA diminished the line tension of the membrane (i.e., the energy required to form the edge of a new pore). However, in contrast to the expectation that adding the positive curvature agent lysophosphatidylcholine would synergistically lower line tension, its addition significantly stabilized HlyA-treated membranes. HlyA also appeared to thicken bilayers to which it was added. We discuss these results in terms of models for proteolipidic pores.Facultad de Ciencias ExactasInstituto de Investigaciones Bioquímicas de La Plata2006info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionArticulohttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdf3748-3755http://sedici.unlp.edu.ar/handle/10915/83200enginfo:eu-repo/semantics/altIdentifier/issn/0006-3495info:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.106.090019info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by-nc-sa/4.0/Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)reponame:SEDICI (UNLP)instname:Universidad Nacional de La Platainstacron:UNLP2025-09-29T11:15:46Zoai:sedici.unlp.edu.ar:10915/83200Institucionalhttp://sedici.unlp.edu.ar/Universidad públicaNo correspondehttp://sedici.unlp.edu.ar/oai/snrdalira@sedici.unlp.edu.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:13292025-09-29 11:15:46.812SEDICI (UNLP) - Universidad Nacional de La Platafalse
dc.title.none.fl_str_mv Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
title Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
spellingShingle Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
Bakás, Laura Susana
Ciencias Exactas
Escherichia coli
Planar Phospholipid Bilayer Membranes
title_short Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
title_full Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
title_fullStr Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
title_full_unstemmed Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
title_sort Paradoxical lipid dependence of pores formed by the Escherichia coli α-hemolysin in planar phospholipid bilayer membranes
dc.creator.none.fl_str_mv Bakás, Laura Susana
Chanturiya, Alexandr
Herlax, Vanesa Silvana
Zimmerberg, Joshua
author Bakás, Laura Susana
author_facet Bakás, Laura Susana
Chanturiya, Alexandr
Herlax, Vanesa Silvana
Zimmerberg, Joshua
author_role author
author2 Chanturiya, Alexandr
Herlax, Vanesa Silvana
Zimmerberg, Joshua
author2_role author
author
author
dc.subject.none.fl_str_mv Ciencias Exactas
Escherichia coli
Planar Phospholipid Bilayer Membranes
topic Ciencias Exactas
Escherichia coli
Planar Phospholipid Bilayer Membranes
dc.description.none.fl_txt_mv α-Hemolysin (HlyA) is an extracellular protein toxin (117 kDa) secreted by <i>Escherichia coli</i> that targets the plasma membranes of eukaryotic cells. We studied the interaction of this toxin with membranes using planar phospholipid bilayers. For all lipid mixtures tested, addition of nanomolar concentrations of toxin resulted in an increase of membrane conductance and a decrease in membrane stability. HlyA decreased membrane lifetime up to three orders of magnitude in a voltage-dependent manner. Using a theory for lipidic pore formation, we analyzed these data to quantify how HlyA diminished the line tension of the membrane (i.e., the energy required to form the edge of a new pore). However, in contrast to the expectation that adding the positive curvature agent lysophosphatidylcholine would synergistically lower line tension, its addition significantly stabilized HlyA-treated membranes. HlyA also appeared to thicken bilayers to which it was added. We discuss these results in terms of models for proteolipidic pores.
Facultad de Ciencias Exactas
Instituto de Investigaciones Bioquímicas de La Plata
description α-Hemolysin (HlyA) is an extracellular protein toxin (117 kDa) secreted by <i>Escherichia coli</i> that targets the plasma membranes of eukaryotic cells. We studied the interaction of this toxin with membranes using planar phospholipid bilayers. For all lipid mixtures tested, addition of nanomolar concentrations of toxin resulted in an increase of membrane conductance and a decrease in membrane stability. HlyA decreased membrane lifetime up to three orders of magnitude in a voltage-dependent manner. Using a theory for lipidic pore formation, we analyzed these data to quantify how HlyA diminished the line tension of the membrane (i.e., the energy required to form the edge of a new pore). However, in contrast to the expectation that adding the positive curvature agent lysophosphatidylcholine would synergistically lower line tension, its addition significantly stabilized HlyA-treated membranes. HlyA also appeared to thicken bilayers to which it was added. We discuss these results in terms of models for proteolipidic pores.
publishDate 2006
dc.date.none.fl_str_mv 2006
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
Articulo
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://sedici.unlp.edu.ar/handle/10915/83200
url http://sedici.unlp.edu.ar/handle/10915/83200
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/issn/0006-3495
info:eu-repo/semantics/altIdentifier/doi/10.1529/biophysj.106.090019
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by-nc-sa/4.0/
Creative Commons Attribution-NonCommercial-ShareAlike 4.0 International (CC BY-NC-SA 4.0)
dc.format.none.fl_str_mv application/pdf
3748-3755
dc.source.none.fl_str_mv reponame:SEDICI (UNLP)
instname:Universidad Nacional de La Plata
instacron:UNLP
reponame_str SEDICI (UNLP)
collection SEDICI (UNLP)
instname_str Universidad Nacional de La Plata
instacron_str UNLP
institution UNLP
repository.name.fl_str_mv SEDICI (UNLP) - Universidad Nacional de La Plata
repository.mail.fl_str_mv alira@sedici.unlp.edu.ar
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score 13.070432

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