In vivo systems to study class II bacteriocins toxicity and immunity
- Autores
- Ríos Colombo, Natalia Soledad; Chalon, Miriam Carolina; Galván, Adriana Emilce; Navarro, Silvia Adriana; Lanza, Lucía; Barraza, Daniela Estefanía; Acuña, Leonardo; Fernandez de Ullivarri, Miguel; Minahk, Carlos Javier; Bellomio, Augusto
- Año de publicación
- 2018
- Idioma
- inglés
- Tipo de recurso
- documento de conferencia
- Estado
- versión publicada
- Descripción
- Class II bacteriocins are membrane-active peptides that act over a narrowspectrum of bacterial targets and have a great potential application as antibioticsin medical sciences. They act on the cytoplasmic membrane dissipating thetransmembrane potential by forming pores. There is solid evidence thatmembrane receptor proteins are necessary for their function, however the preciserole of this receptor and the nature of the pore remain elusive. The most acceptedmodel suggest that bacteriocins bind the receptor to change its conformation,creating a channel that remains open. Nonetheless, several studies support asecond model in which the bacteriocin is able to disrupt the membrane itself andthe receptor might act just as an anchor allowing the subsequent bacteriocininsertion to form the pore. In order to reveal whether or not the pore structureinvolves the specific receptor, we designed chimeric peptides fusing themembrane protein EtpM with different class II bacteriocins. We chose E. coli as areceptor-free expression host. The fusion EtpM-bacteriocin anchors eachbacteriocin to the membrane and kills the expressing host cell, even in theabsence of the specific receptor. These results are in line with the second model inwhich the pore is formed through a receptor-independent interaction with the lipidbilayer. The effect of these interactions was also analyzed, through a fluorophorethat changes its fluorescence intensity according to transmembrane potential.On the other hand, an immunity protein protects the producer strain against itsown bacteriocin. For antimicrobials under investigation for clinical applications, thepotential emergence of resistant pathogens and the study of immune mechanismsare a primary concern. Though no direct in vitro interaction bacteriocin-immunityhas been reported before, by using an in vivo system, we present evidence thatthis binding might occur, not in aqueous solution but in a membrane inserted .
Fil: Ríos Colombo, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Chalon, Miriam Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Galván, Adriana Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina
Fil: Navarro, Silvia Adriana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Lanza, Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Barraza, Daniela Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Fernandez de Ullivarri, Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina
XLVII Reunión Anual de la Sociedad Argentina de Biofísica
La Plata
Argentina
Sociedad Argentina de Biofísica - Materia
-
Bacteriocin
Immunity protein
Transmembrane potential
mechanism of action - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/188137
Ver los metadatos del registro completo
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In vivo systems to study class II bacteriocins toxicity and immunityRíos Colombo, Natalia SoledadChalon, Miriam CarolinaGalván, Adriana EmilceNavarro, Silvia AdrianaLanza, LucíaBarraza, Daniela EstefaníaAcuña, LeonardoFernandez de Ullivarri, MiguelMinahk, Carlos JavierBellomio, AugustoBacteriocinImmunity proteinTransmembrane potentialmechanism of actionhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Class II bacteriocins are membrane-active peptides that act over a narrowspectrum of bacterial targets and have a great potential application as antibioticsin medical sciences. They act on the cytoplasmic membrane dissipating thetransmembrane potential by forming pores. There is solid evidence thatmembrane receptor proteins are necessary for their function, however the preciserole of this receptor and the nature of the pore remain elusive. The most acceptedmodel suggest that bacteriocins bind the receptor to change its conformation,creating a channel that remains open. Nonetheless, several studies support asecond model in which the bacteriocin is able to disrupt the membrane itself andthe receptor might act just as an anchor allowing the subsequent bacteriocininsertion to form the pore. In order to reveal whether or not the pore structureinvolves the specific receptor, we designed chimeric peptides fusing themembrane protein EtpM with different class II bacteriocins. We chose E. coli as areceptor-free expression host. The fusion EtpM-bacteriocin anchors eachbacteriocin to the membrane and kills the expressing host cell, even in theabsence of the specific receptor. These results are in line with the second model inwhich the pore is formed through a receptor-independent interaction with the lipidbilayer. The effect of these interactions was also analyzed, through a fluorophorethat changes its fluorescence intensity according to transmembrane potential.On the other hand, an immunity protein protects the producer strain against itsown bacteriocin. For antimicrobials under investigation for clinical applications, thepotential emergence of resistant pathogens and the study of immune mechanismsare a primary concern. Though no direct in vitro interaction bacteriocin-immunityhas been reported before, by using an in vivo system, we present evidence thatthis binding might occur, not in aqueous solution but in a membrane inserted .Fil: Ríos Colombo, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Chalon, Miriam Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Galván, Adriana Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; ArgentinaFil: Navarro, Silvia Adriana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Lanza, Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Barraza, Daniela Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Fernandez de Ullivarri, Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaFil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; ArgentinaXLVII Reunión Anual de la Sociedad Argentina de BiofísicaLa PlataArgentinaSociedad Argentina de BiofísicaSociedad Argentina de Biofísica2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/conferenceObjectReuniónBookhttp://purl.org/coar/resource_type/c_5794info:ar-repo/semantics/documentoDeConferenciaapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/188137In vivo systems to study class II bacteriocins toxicity and immunity; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 1-2CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://biofisica.org.ar/reuniones-cientificas/reunionsab-previas/Internacionalinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2026-02-06T12:12:29Zoai:ri.conicet.gov.ar:11336/188137instacron: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:34982026-02-06 12:12:29.9CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
In vivo systems to study class II bacteriocins toxicity and immunity |
| title |
In vivo systems to study class II bacteriocins toxicity and immunity |
| spellingShingle |
In vivo systems to study class II bacteriocins toxicity and immunity Ríos Colombo, Natalia Soledad Bacteriocin Immunity protein Transmembrane potential mechanism of action |
| title_short |
In vivo systems to study class II bacteriocins toxicity and immunity |
| title_full |
In vivo systems to study class II bacteriocins toxicity and immunity |
| title_fullStr |
In vivo systems to study class II bacteriocins toxicity and immunity |
| title_full_unstemmed |
In vivo systems to study class II bacteriocins toxicity and immunity |
| title_sort |
In vivo systems to study class II bacteriocins toxicity and immunity |
| dc.creator.none.fl_str_mv |
Ríos Colombo, Natalia Soledad Chalon, Miriam Carolina Galván, Adriana Emilce Navarro, Silvia Adriana Lanza, Lucía Barraza, Daniela Estefanía Acuña, Leonardo Fernandez de Ullivarri, Miguel Minahk, Carlos Javier Bellomio, Augusto |
| author |
Ríos Colombo, Natalia Soledad |
| author_facet |
Ríos Colombo, Natalia Soledad Chalon, Miriam Carolina Galván, Adriana Emilce Navarro, Silvia Adriana Lanza, Lucía Barraza, Daniela Estefanía Acuña, Leonardo Fernandez de Ullivarri, Miguel Minahk, Carlos Javier Bellomio, Augusto |
| author_role |
author |
| author2 |
Chalon, Miriam Carolina Galván, Adriana Emilce Navarro, Silvia Adriana Lanza, Lucía Barraza, Daniela Estefanía Acuña, Leonardo Fernandez de Ullivarri, Miguel Minahk, Carlos Javier Bellomio, Augusto |
| author2_role |
author author author author author author author author author |
| dc.subject.none.fl_str_mv |
Bacteriocin Immunity protein Transmembrane potential mechanism of action |
| topic |
Bacteriocin Immunity protein Transmembrane potential mechanism of action |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
Class II bacteriocins are membrane-active peptides that act over a narrowspectrum of bacterial targets and have a great potential application as antibioticsin medical sciences. They act on the cytoplasmic membrane dissipating thetransmembrane potential by forming pores. There is solid evidence thatmembrane receptor proteins are necessary for their function, however the preciserole of this receptor and the nature of the pore remain elusive. The most acceptedmodel suggest that bacteriocins bind the receptor to change its conformation,creating a channel that remains open. Nonetheless, several studies support asecond model in which the bacteriocin is able to disrupt the membrane itself andthe receptor might act just as an anchor allowing the subsequent bacteriocininsertion to form the pore. In order to reveal whether or not the pore structureinvolves the specific receptor, we designed chimeric peptides fusing themembrane protein EtpM with different class II bacteriocins. We chose E. coli as areceptor-free expression host. The fusion EtpM-bacteriocin anchors eachbacteriocin to the membrane and kills the expressing host cell, even in theabsence of the specific receptor. These results are in line with the second model inwhich the pore is formed through a receptor-independent interaction with the lipidbilayer. The effect of these interactions was also analyzed, through a fluorophorethat changes its fluorescence intensity according to transmembrane potential.On the other hand, an immunity protein protects the producer strain against itsown bacteriocin. For antimicrobials under investigation for clinical applications, thepotential emergence of resistant pathogens and the study of immune mechanismsare a primary concern. Though no direct in vitro interaction bacteriocin-immunityhas been reported before, by using an in vivo system, we present evidence thatthis binding might occur, not in aqueous solution but in a membrane inserted . Fil: Ríos Colombo, Natalia Soledad. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Chalon, Miriam Carolina. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Galván, Adriana Emilce. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Planta Piloto de Procesos Industriales Microbiológicos; Argentina Fil: Navarro, Silvia Adriana. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Lanza, Lucía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Barraza, Daniela Estefanía. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Acuña, Leonardo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Fernandez de Ullivarri, Miguel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Minahk, Carlos Javier. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina Fil: Bellomio, Augusto. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tucumán. Instituto Superior de Investigaciones Biológicas. Universidad Nacional de Tucumán. Instituto Superior de Investigaciones Biológicas; Argentina XLVII Reunión Anual de la Sociedad Argentina de Biofísica La Plata Argentina Sociedad Argentina de Biofísica |
| description |
Class II bacteriocins are membrane-active peptides that act over a narrowspectrum of bacterial targets and have a great potential application as antibioticsin medical sciences. They act on the cytoplasmic membrane dissipating thetransmembrane potential by forming pores. There is solid evidence thatmembrane receptor proteins are necessary for their function, however the preciserole of this receptor and the nature of the pore remain elusive. The most acceptedmodel suggest that bacteriocins bind the receptor to change its conformation,creating a channel that remains open. Nonetheless, several studies support asecond model in which the bacteriocin is able to disrupt the membrane itself andthe receptor might act just as an anchor allowing the subsequent bacteriocininsertion to form the pore. In order to reveal whether or not the pore structureinvolves the specific receptor, we designed chimeric peptides fusing themembrane protein EtpM with different class II bacteriocins. We chose E. coli as areceptor-free expression host. The fusion EtpM-bacteriocin anchors eachbacteriocin to the membrane and kills the expressing host cell, even in theabsence of the specific receptor. These results are in line with the second model inwhich the pore is formed through a receptor-independent interaction with the lipidbilayer. The effect of these interactions was also analyzed, through a fluorophorethat changes its fluorescence intensity according to transmembrane potential.On the other hand, an immunity protein protects the producer strain against itsown bacteriocin. For antimicrobials under investigation for clinical applications, thepotential emergence of resistant pathogens and the study of immune mechanismsare a primary concern. Though no direct in vitro interaction bacteriocin-immunityhas been reported before, by using an in vivo system, we present evidence thatthis binding might occur, not in aqueous solution but in a membrane inserted . |
| publishDate |
2018 |
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2018 |
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info:eu-repo/semantics/publishedVersion info:eu-repo/semantics/conferenceObject Reunión Book http://purl.org/coar/resource_type/c_5794 info:ar-repo/semantics/documentoDeConferencia |
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http://hdl.handle.net/11336/188137 In vivo systems to study class II bacteriocins toxicity and immunity; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 1-2 CONICET Digital CONICET |
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http://hdl.handle.net/11336/188137 |
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In vivo systems to study class II bacteriocins toxicity and immunity; XLVII Reunión Anual de la Sociedad Argentina de Biofísica; La Plata; Argentina; 2018; 1-2 CONICET Digital CONICET |
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eng |
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eng |
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Internacional |
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Sociedad Argentina de Biofísica |
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Sociedad Argentina de Biofísica |
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