Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?

Pore-forming toxins (PFTs) form nanoscale pores across target membranes causing cell death. The pore-forming cytolysins of the RTX (repeats in toxin) family belong to a steadily increasing family of proteins characterized by having in their primary sequences a number of glycine- and aspartate-rich n...

Descripción completa

Detalles Bibliográficos
Autores: Ostolaza Echabe, Elena Amaya, González Bullón, David, Belloso Uribe, Kepa, Martín Plágaro, César Augusto, Amuategi Aulestiarte, Jone, Fernández Martínez, Xabier
Tipo de recurso: artículo
Fecha de publicación:2019
País:España
Institución:Universidad del País Vasco
Repositorio:Addi. Archivo Digital para la Docencia y la Investigación
OAI Identifier:oai:addi.ehu.eus:10810/40424
Acceso en línea:http://hdl.handle.net/10810/40424
Access Level:acceso abierto
Palabra clave:pore-forming proteins
Gram-negative bacteria
bacterial protein toxins
RTX toxins
toroidal pores
adenylate-cyclase toxin
escherichia-coli hemolysin
actinobacillus-actinomycetemcomitans leukotoxin
plasmid-encoded hemolysin
C-terminal domain
bordetella-pertussis
alpha-hemolysin
nucleotide-sequence
channel formation
proapoptotic bax
id ES_9784fee00c07d0da4435817c1906d056
oai_identifier_str oai:addi.ehu.eus:10810/40424
network_acronym_str ES
network_name_str España
repository_id_str
spelling Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?Ostolaza Echabe, Elena AmayaGonzález Bullón, DavidBelloso Uribe, KepaMartín Plágaro, César AugustoAmuategi Aulestiarte, JoneFernández Martínez, Xabierpore-forming proteinsGram-negative bacteriabacterial protein toxinsRTX toxinstoroidal poresadenylate-cyclase toxinescherichia-coli hemolysinactinobacillus-actinomycetemcomitans leukotoxinplasmid-encoded hemolysinC-terminal domainbordetella-pertussisalpha-hemolysinnucleotide-sequencechannel formationproapoptotic baxPore-forming toxins (PFTs) form nanoscale pores across target membranes causing cell death. The pore-forming cytolysins of the RTX (repeats in toxin) family belong to a steadily increasing family of proteins characterized by having in their primary sequences a number of glycine- and aspartate-rich nonapeptide repeats. They are secreted by a variety of Gram-negative bacteria and form ion-permeable pores in several cell types, such as immune cells, epithelial cells, or erythrocytes. Pore-formation by RTX-toxins leads to the dissipation of ionic gradients and membrane potential across the cytoplasmic membrane of target cells, which results in cell death. The pores formed in lipid bilayers by the RTX-toxins share some common properties such as cation selectivity and voltage-dependence. Hemolytic and cytolytic RTX-toxins are important virulence factors in the pathogenesis of the producing bacteria. And hence, understanding the function of these proteins at the molecular level is critical to elucidating their role in disease processes. In this review we summarize the current state of knowledge on pore-formation by RTX toxins, and include recent results from our own laboratory regarding the pore-forming activity of adenylate cyclase toxin (ACT or CyaA), a large protein toxin secreted by Bordetella pertussis, the bacterium causative of whooping cough.This study was supported by grant from the Spanish Ministerio de Economia y Competitividad BFU2017-82758-P. D.G.-B. and A.B.G.A. were recipients of a fellowship from the Bizkaia Biophysics Foundation.MDPI202020202019info:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10810/40424reponame:Addi. Archivo Digital para la Docencia y la Investigacióninstname:Universidad del País VascoInglésinfo:eu-repo/grantAgreement/MINECO/BFU2017-82758-P/https://www.mdpi.com/2072-6651/11/6/354info:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/3.0/es/This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0)Atribución 3.0 Españaoai:addi.ehu.eus:10810/404242026-06-18T09:23:17Z
dc.title.none.fl_str_mv Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
title Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
spellingShingle Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
Ostolaza Echabe, Elena Amaya
pore-forming proteins
Gram-negative bacteria
bacterial protein toxins
RTX toxins
toroidal pores
adenylate-cyclase toxin
escherichia-coli hemolysin
actinobacillus-actinomycetemcomitans leukotoxin
plasmid-encoded hemolysin
C-terminal domain
bordetella-pertussis
alpha-hemolysin
nucleotide-sequence
channel formation
proapoptotic bax
title_short Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
title_full Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
title_fullStr Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
title_full_unstemmed Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
title_sort Membrane Permeabilization by Pore-Forming RTX Toxins: What Kind of Lesions Do These Toxins Form?
dc.creator.none.fl_str_mv Ostolaza Echabe, Elena Amaya
González Bullón, David
Belloso Uribe, Kepa
Martín Plágaro, César Augusto
Amuategi Aulestiarte, Jone
Fernández Martínez, Xabier
author Ostolaza Echabe, Elena Amaya
author_facet Ostolaza Echabe, Elena Amaya
González Bullón, David
Belloso Uribe, Kepa
Martín Plágaro, César Augusto
Amuategi Aulestiarte, Jone
Fernández Martínez, Xabier
author_role author
author2 González Bullón, David
Belloso Uribe, Kepa
Martín Plágaro, César Augusto
Amuategi Aulestiarte, Jone
Fernández Martínez, Xabier
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv pore-forming proteins
Gram-negative bacteria
bacterial protein toxins
RTX toxins
toroidal pores
adenylate-cyclase toxin
escherichia-coli hemolysin
actinobacillus-actinomycetemcomitans leukotoxin
plasmid-encoded hemolysin
C-terminal domain
bordetella-pertussis
alpha-hemolysin
nucleotide-sequence
channel formation
proapoptotic bax
topic pore-forming proteins
Gram-negative bacteria
bacterial protein toxins
RTX toxins
toroidal pores
adenylate-cyclase toxin
escherichia-coli hemolysin
actinobacillus-actinomycetemcomitans leukotoxin
plasmid-encoded hemolysin
C-terminal domain
bordetella-pertussis
alpha-hemolysin
nucleotide-sequence
channel formation
proapoptotic bax
description Pore-forming toxins (PFTs) form nanoscale pores across target membranes causing cell death. The pore-forming cytolysins of the RTX (repeats in toxin) family belong to a steadily increasing family of proteins characterized by having in their primary sequences a number of glycine- and aspartate-rich nonapeptide repeats. They are secreted by a variety of Gram-negative bacteria and form ion-permeable pores in several cell types, such as immune cells, epithelial cells, or erythrocytes. Pore-formation by RTX-toxins leads to the dissipation of ionic gradients and membrane potential across the cytoplasmic membrane of target cells, which results in cell death. The pores formed in lipid bilayers by the RTX-toxins share some common properties such as cation selectivity and voltage-dependence. Hemolytic and cytolytic RTX-toxins are important virulence factors in the pathogenesis of the producing bacteria. And hence, understanding the function of these proteins at the molecular level is critical to elucidating their role in disease processes. In this review we summarize the current state of knowledge on pore-formation by RTX toxins, and include recent results from our own laboratory regarding the pore-forming activity of adenylate cyclase toxin (ACT or CyaA), a large protein toxin secreted by Bordetella pertussis, the bacterium causative of whooping cough.
publishDate 2019
dc.date.none.fl_str_mv 2019
2020
2020
dc.type.none.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv http://hdl.handle.net/10810/40424
url http://hdl.handle.net/10810/40424
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/MINECO/BFU2017-82758-P/
https://www.mdpi.com/2072-6651/11/6/354
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/3.0/es/
Atribución 3.0 España
eu_rights_str_mv openAccess
rights_invalid_str_mv http://creativecommons.org/licenses/by/3.0/es/
Atribución 3.0 España
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Addi. Archivo Digital para la Docencia y la Investigación
instname:Universidad del País Vasco
instname_str Universidad del País Vasco
reponame_str Addi. Archivo Digital para la Docencia y la Investigación
collection Addi. Archivo Digital para la Docencia y la Investigación
repository.name.fl_str_mv
repository.mail.fl_str_mv
_version_ 1869414086160154624
score 15,300719

Similares en LA Referencia