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
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/8041
Ver los metadatos del registro completo
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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 Técnicas2025-09-29T09:43:13Zoai: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:34982025-09-29 09:43:13.424CONICET 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 |
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1844613360108175360 |
score |
13.070432 |