Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins

Permeabilization of the plasma membrane represents an important threat for any cell, since it compromises its viability by disrupting cell homeostasis. Numerous pathogenic bacteria produce pore-forming toxins that break plasma membrane integrity and cause cell death by colloid-osmotic lysis. Eukaryo...

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Detalles Bibliográficos
Autores: Etxaniz, Asier, González‐Bullón, David, Martín, César, Ostolaza, Helena
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/397566
Acceso en línea:http://hdl.handle.net/10261/397566
https://api.elsevier.com/content/abstract/scopus_id/85048703229
Access Level:acceso abierto
Palabra clave:Bordetella pertussis
RTX toxins
Adenylate cyclase toxin
Membrane permeabilization
Membrane repair
Pore-forming toxins
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spelling Membrane Repair Mechanisms against Permeabilization by Pore-Forming ToxinsEtxaniz, AsierGonzález‐Bullón, DavidMartín, CésarOstolaza, HelenaBordetella pertussisRTX toxinsAdenylate cyclase toxinMembrane permeabilizationMembrane repairPore-forming toxinsPermeabilization of the plasma membrane represents an important threat for any cell, since it compromises its viability by disrupting cell homeostasis. Numerous pathogenic bacteria produce pore-forming toxins that break plasma membrane integrity and cause cell death by colloid-osmotic lysis. Eukaryotic cells, in turn, have developed different ways to cope with the effects of such membrane piercing. Here, we provide a short overview of the general mechanisms currently proposed for plasma membrane repair, focusing more specifically on the cellular responses to membrane permeabilization by pore-forming toxins and presenting new data on the effects and cellular responses to the permeabilization by an RTX (repeats in toxin) toxin, the adenylate cyclase toxin-hemolysin secreted by the whooping cough bacterium Bordetella pertussis, which we have studied in the laboratory.This study was supported by grants from the Basque Government (Grupos Consolidados IT849-13) and grant from the Spanish Ministerio de Economía y Competitividad (BFU2017-82758-P AEI/FEDER, UE).Peer reviewedMultidisciplinary Digital Publishing InstituteEusko JaurlaritzaMinisterio de Economía y Competitividad (España)Ostolaza, Helena [0000-0002-2346-5228]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202520252018info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_dcae04bcPublisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/397566https://api.elsevier.com/content/abstract/scopus_id/85048703229reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2017-82758-Phttps://doi.org/10.3390/toxins10060234Síinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3975662026-05-22T06:33:51Z
dc.title.none.fl_str_mv Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
title Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
spellingShingle Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
Etxaniz, Asier
Bordetella pertussis
RTX toxins
Adenylate cyclase toxin
Membrane permeabilization
Membrane repair
Pore-forming toxins
title_short Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
title_full Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
title_fullStr Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
title_full_unstemmed Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
title_sort Membrane Repair Mechanisms against Permeabilization by Pore-Forming Toxins
dc.creator.none.fl_str_mv Etxaniz, Asier
González‐Bullón, David
Martín, César
Ostolaza, Helena
author Etxaniz, Asier
author_facet Etxaniz, Asier
González‐Bullón, David
Martín, César
Ostolaza, Helena
author_role author
author2 González‐Bullón, David
Martín, César
Ostolaza, Helena
author2_role author
author
author
dc.contributor.none.fl_str_mv Eusko Jaurlaritza
Ministerio de Economía y Competitividad (España)
Ostolaza, Helena [0000-0002-2346-5228]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Bordetella pertussis
RTX toxins
Adenylate cyclase toxin
Membrane permeabilization
Membrane repair
Pore-forming toxins
topic Bordetella pertussis
RTX toxins
Adenylate cyclase toxin
Membrane permeabilization
Membrane repair
Pore-forming toxins
description Permeabilization of the plasma membrane represents an important threat for any cell, since it compromises its viability by disrupting cell homeostasis. Numerous pathogenic bacteria produce pore-forming toxins that break plasma membrane integrity and cause cell death by colloid-osmotic lysis. Eukaryotic cells, in turn, have developed different ways to cope with the effects of such membrane piercing. Here, we provide a short overview of the general mechanisms currently proposed for plasma membrane repair, focusing more specifically on the cellular responses to membrane permeabilization by pore-forming toxins and presenting new data on the effects and cellular responses to the permeabilization by an RTX (repeats in toxin) toxin, the adenylate cyclase toxin-hemolysin secreted by the whooping cough bacterium Bordetella pertussis, which we have studied in the laboratory.
publishDate 2018
dc.date.none.fl_str_mv 2018
2025
2025
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_dcae04bc
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/397566
https://api.elsevier.com/content/abstract/scopus_id/85048703229
url http://hdl.handle.net/10261/397566
https://api.elsevier.com/content/abstract/scopus_id/85048703229
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2013-2016/BFU2017-82758-P
https://doi.org/10.3390/toxins10060234
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
publisher.none.fl_str_mv Multidisciplinary Digital Publishing Institute
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
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