Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli

Autores
Vazquez, Romina Florencia; Maté, Sabina María; Bakás, Laura S.; Fernández, Marisa Mariel; Malchiodi, Emilio Luis; Herlax, Vanesa Silvana
Año de publicación
2014
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Several toxins that interact with animal cells present some kind of interaction with cholesterol (Cho) or sphingomyelin. In the present work we demonstrate that alpha hemolysin of E. coli (HlyA) interacts directly with Chocholesterol, resulting in one of the first reported toxins secreted by Gram negative bacteria and the first reported member of the RTX toxin family that participates in the interaction with this sterol. We have recently reported that HlyA became associated with detergent-resistant membranes enriched in sphingomyelin and Chocholesterol; moreover, after Cho depletion, toxin oligomerization and hence hemolytic activity diminishes. Considering these results we studied the insertion process by monolayer technique, finding that HlyA insertion into membranes is favouredfavored in sphingomyelin and Chocholesterol-containing membranes. Taking into account this result, the direct interaction with either of the lipids was studied by lipid dot blot, lysis inhibition and surface plasmon resonance assays. Results demonstrated that there isit exists a direct interaction between Chocholesterol and HlyA that seems to favoursfavors a conformational state of the protein that allows the correct insertion into the membrane and further oligomerization to pore formation.
Fil: Vazquez, Romina Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
Fil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
Fil: Bakás, Laura S.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina
Fil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina
Fil: Herlax, Vanesa Silvana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
Materia
Cholesterol
Rtx Toxin
Spr
Biacore
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:11336/8041
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/8041
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coliVazquez, Romina FlorenciaMaté, Sabina MaríaBakás, Laura S.Fernández, Marisa MarielMalchiodi, Emilio LuisHerlax, Vanesa SilvanaCholesterolRtx ToxinSprBiacorehttps://purl.org/becyt/ford/3.3https://purl.org/becyt/ford/3Several toxins that interact with animal cells present some kind of interaction with cholesterol (Cho) or sphingomyelin. In the present work we demonstrate that alpha hemolysin of E. coli (HlyA) interacts directly with Chocholesterol, resulting in one of the first reported toxins secreted by Gram negative bacteria and the first reported member of the RTX toxin family that participates in the interaction with this sterol. We have recently reported that HlyA became associated with detergent-resistant membranes enriched in sphingomyelin and Chocholesterol; moreover, after Cho depletion, toxin oligomerization and hence hemolytic activity diminishes. Considering these results we studied the insertion process by monolayer technique, finding that HlyA insertion into membranes is favouredfavored in sphingomyelin and Chocholesterol-containing membranes. Taking into account this result, the direct interaction with either of the lipids was studied by lipid dot blot, lysis inhibition and surface plasmon resonance assays. Results demonstrated that there isit exists a direct interaction between Chocholesterol and HlyA that seems to favoursfavors a conformational state of the protein that allows the correct insertion into the membrane and further oligomerization to pore formation.Fil: Vazquez, Romina Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; ArgentinaFil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; ArgentinaFil: Bakás, Laura S.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; ArgentinaFil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; ArgentinaFil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; ArgentinaFil: Herlax, Vanesa Silvana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; ArgentinaPortland Press2014-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/8041Vazquez, Romina Florencia; Maté, Sabina María; Bakás, Laura S.; Fernández, Marisa Mariel; Malchiodi, Emilio Luis; et al.; Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli; Portland Press; Biochemical Journal; 458; 3; 3-2014; 481-4890264-6021enginfo:eu-repo/semantics/altIdentifier/url/http://www.biochemj.org/content/458/3/481info:eu-repo/semantics/altIdentifier/doi/10.1042/BJ20131432info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-15T14:36:23Zoai:ri.conicet.gov.ar:11336/8041instacron: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:34982025-10-15 14:36:23.724CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
title Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
spellingShingle Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
Vazquez, Romina Florencia
Cholesterol
Rtx Toxin
Spr
Biacore
title_short Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
title_full Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
title_fullStr Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
title_full_unstemmed Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
title_sort Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli
dc.creator.none.fl_str_mv Vazquez, Romina Florencia
Maté, Sabina María
Bakás, Laura S.
Fernández, Marisa Mariel
Malchiodi, Emilio Luis
Herlax, Vanesa Silvana
author Vazquez, Romina Florencia
author_facet Vazquez, Romina Florencia
Maté, Sabina María
Bakás, Laura S.
Fernández, Marisa Mariel
Malchiodi, Emilio Luis
Herlax, Vanesa Silvana
author_role author
author2 Maté, Sabina María
Bakás, Laura S.
Fernández, Marisa Mariel
Malchiodi, Emilio Luis
Herlax, Vanesa Silvana
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv Cholesterol
Rtx Toxin
Spr
Biacore
topic Cholesterol
Rtx Toxin
Spr
Biacore
purl_subject.fl_str_mv https://purl.org/becyt/ford/3.3
https://purl.org/becyt/ford/3
dc.description.none.fl_txt_mv Several toxins that interact with animal cells present some kind of interaction with cholesterol (Cho) or sphingomyelin. In the present work we demonstrate that alpha hemolysin of E. coli (HlyA) interacts directly with Chocholesterol, resulting in one of the first reported toxins secreted by Gram negative bacteria and the first reported member of the RTX toxin family that participates in the interaction with this sterol. We have recently reported that HlyA became associated with detergent-resistant membranes enriched in sphingomyelin and Chocholesterol; moreover, after Cho depletion, toxin oligomerization and hence hemolytic activity diminishes. Considering these results we studied the insertion process by monolayer technique, finding that HlyA insertion into membranes is favouredfavored in sphingomyelin and Chocholesterol-containing membranes. Taking into account this result, the direct interaction with either of the lipids was studied by lipid dot blot, lysis inhibition and surface plasmon resonance assays. Results demonstrated that there isit exists a direct interaction between Chocholesterol and HlyA that seems to favoursfavors a conformational state of the protein that allows the correct insertion into the membrane and further oligomerization to pore formation.
Fil: Vazquez, Romina Florencia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
Fil: Maté, Sabina María. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
Fil: Bakás, Laura S.. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas; Argentina
Fil: Fernández, Marisa Mariel. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina
Fil: Malchiodi, Emilio Luis. Consejo Nacional de Investigaciones Cientiâ­ficas y Tecnicas. Oficina de Coordinacion Administrativa Houssay. Instituto de Estudios de la Inmunidad Humoral "profesor R. A. Margni"; Argentina
Fil: Herlax, Vanesa Silvana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico La Plata. Instituto de Investigaciones Bioquímicas de La Plata; Argentina
description Several toxins that interact with animal cells present some kind of interaction with cholesterol (Cho) or sphingomyelin. In the present work we demonstrate that alpha hemolysin of E. coli (HlyA) interacts directly with Chocholesterol, resulting in one of the first reported toxins secreted by Gram negative bacteria and the first reported member of the RTX toxin family that participates in the interaction with this sterol. We have recently reported that HlyA became associated with detergent-resistant membranes enriched in sphingomyelin and Chocholesterol; moreover, after Cho depletion, toxin oligomerization and hence hemolytic activity diminishes. Considering these results we studied the insertion process by monolayer technique, finding that HlyA insertion into membranes is favouredfavored in sphingomyelin and Chocholesterol-containing membranes. Taking into account this result, the direct interaction with either of the lipids was studied by lipid dot blot, lysis inhibition and surface plasmon resonance assays. Results demonstrated that there isit exists a direct interaction between Chocholesterol and HlyA that seems to favoursfavors a conformational state of the protein that allows the correct insertion into the membrane and further oligomerization to pore formation.
publishDate 2014
dc.date.none.fl_str_mv 2014-03
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/11336/8041
Vazquez, Romina Florencia; Maté, Sabina María; Bakás, Laura S.; Fernández, Marisa Mariel; Malchiodi, Emilio Luis; et al.; Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli; Portland Press; Biochemical Journal; 458; 3; 3-2014; 481-489
0264-6021
url http://hdl.handle.net/11336/8041
identifier_str_mv Vazquez, Romina Florencia; Maté, Sabina María; Bakás, Laura S.; Fernández, Marisa Mariel; Malchiodi, Emilio Luis; et al.; Novel evidence for the specific interaction between cholesterol and α-haemolysin of Escherichia coli; Portland Press; Biochemical Journal; 458; 3; 3-2014; 481-489
0264-6021
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/http://www.biochemj.org/content/458/3/481
info:eu-repo/semantics/altIdentifier/doi/10.1042/BJ20131432
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
application/pdf
dc.publisher.none.fl_str_mv Portland Press
publisher.none.fl_str_mv Portland Press
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_ 1846082830052884480
score 13.22299

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