Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages

Autores
del Cogliano, Manuel Eugenio; Hollmann, Axel; Martínez, Melina María Belén; Semorile, Liliana Carmen; Ghiringhelli, Pablo Daniel; Maffia, Paulo Cesar; Bentancor, Leticia Verónica
Año de publicación
2018
Idioma
inglés
Tipo de recurso
parte de libro
Estado
versión publicada
Descripción
Shiga toxin (Stx) is the principal virulence factor during Shiga toxin-producing Escherichia coli (STEC) infections. We have previously reported the inactivation of bacteriophage encoding Stx after treatment with chitosan, a linear polysaccharide polymer with cationic properties. Cationic antimicrobial peptides (cAMPs) are short linear aminoacidic sequences, with a positive net charge, which display bactericidal or bacteriostatic activity against a wide range of bacterial species. They are promising novel antibiotics since they have shown bactericidal effects against multiresistant bacteria. To evaluate whether cationic properties are responsible for bacteriophage inactivation, we tested seven cationic peptides with proven antimicrobial activity as anti-bacteriophage agents, and one random sequence cationic peptide with no antimicrobial activity as a control. We observed bacteriophage inactivation after incubation with five cAMPs, but no inactivating activity was observed with the random sequence cationic peptide or with the non-alpha helical cAMP Omiganan. Finally, to confirm peptide-bacteriophage interaction, zeta potential was analyzed by following changes on bacteriophage surface charges after peptide incubation. According to our results we could propose that: (1) direct interaction of peptides with phage is a necessary step for bacteriophage inactivation, (2) cationic properties are necessary but not sufficient for bacteriophage inactivation, and (3) inactivation by cationic peptides could be sequence (or structure) specific. Overall our data suggest that these peptides could be considered a new family of molecules potentially useful to decrease bacteriophage replication and Stx expression.
Fil: del Cogliano, Manuel Eugenio. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Hollmann, Axel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Martínez, Melina María Belén. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina
Fil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
Synthetic peptides
Antimicrobial peptides
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/106633
Acceder
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network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophagesdel Cogliano, Manuel EugenioHollmann, AxelMartínez, Melina María BelénSemorile, Liliana CarmenGhiringhelli, Pablo DanielMaffia, Paulo CesarBentancor, Leticia VerónicaSynthetic peptidesAntimicrobial peptideshttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Shiga toxin (Stx) is the principal virulence factor during Shiga toxin-producing Escherichia coli (STEC) infections. We have previously reported the inactivation of bacteriophage encoding Stx after treatment with chitosan, a linear polysaccharide polymer with cationic properties. Cationic antimicrobial peptides (cAMPs) are short linear aminoacidic sequences, with a positive net charge, which display bactericidal or bacteriostatic activity against a wide range of bacterial species. They are promising novel antibiotics since they have shown bactericidal effects against multiresistant bacteria. To evaluate whether cationic properties are responsible for bacteriophage inactivation, we tested seven cationic peptides with proven antimicrobial activity as anti-bacteriophage agents, and one random sequence cationic peptide with no antimicrobial activity as a control. We observed bacteriophage inactivation after incubation with five cAMPs, but no inactivating activity was observed with the random sequence cationic peptide or with the non-alpha helical cAMP Omiganan. Finally, to confirm peptide-bacteriophage interaction, zeta potential was analyzed by following changes on bacteriophage surface charges after peptide incubation. According to our results we could propose that: (1) direct interaction of peptides with phage is a necessary step for bacteriophage inactivation, (2) cationic properties are necessary but not sufficient for bacteriophage inactivation, and (3) inactivation by cationic peptides could be sequence (or structure) specific. Overall our data suggest that these peptides could be considered a new family of molecules potentially useful to decrease bacteriophage replication and Stx expression.Fil: del Cogliano, Manuel Eugenio. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Hollmann, Axel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; ArgentinaFil: Martínez, Melina María Belén. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; ArgentinaFil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFrontiers Media S.A.O´Brien Simpson, Neil M.Hoffmann, RalfBrian Chia, C. S.Wade, John D.2018info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/bookParthttp://purl.org/coar/resource_type/c_3248info:ar-repo/semantics/parteDeLibroapplication/pdfapplication/pdfapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/106633del Cogliano, Manuel Eugenio; Hollmann, Axel; Martínez, Melina María Belén; Semorile, Liliana Carmen; Ghiringhelli, Pablo Daniel; et al.; Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages; Frontiers Media S.A.; 2018; 126-131978-2-88945-470-9CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3389/fchem.2017.00122info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00122/fullinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:41:43Zoai:ri.conicet.gov.ar:11336/106633instacron: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 10:41:43.838CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
title Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
spellingShingle Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
del Cogliano, Manuel Eugenio
Synthetic peptides
Antimicrobial peptides
title_short Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
title_full Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
title_fullStr Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
title_full_unstemmed Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
title_sort Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages
dc.creator.none.fl_str_mv del Cogliano, Manuel Eugenio
Hollmann, Axel
Martínez, Melina María Belén
Semorile, Liliana Carmen
Ghiringhelli, Pablo Daniel
Maffia, Paulo Cesar
Bentancor, Leticia Verónica
author del Cogliano, Manuel Eugenio
author_facet del Cogliano, Manuel Eugenio
Hollmann, Axel
Martínez, Melina María Belén
Semorile, Liliana Carmen
Ghiringhelli, Pablo Daniel
Maffia, Paulo Cesar
Bentancor, Leticia Verónica
author_role author
author2 Hollmann, Axel
Martínez, Melina María Belén
Semorile, Liliana Carmen
Ghiringhelli, Pablo Daniel
Maffia, Paulo Cesar
Bentancor, Leticia Verónica
author2_role author
author
author
author
author
author
dc.contributor.none.fl_str_mv O´Brien Simpson, Neil M.
Hoffmann, Ralf
Brian Chia, C. S.
Wade, John D.
dc.subject.none.fl_str_mv Synthetic peptides
Antimicrobial peptides
topic Synthetic peptides
Antimicrobial peptides
purl_subject.fl_str_mv https://purl.org/becyt/ford/1.6
https://purl.org/becyt/ford/1
dc.description.none.fl_txt_mv Shiga toxin (Stx) is the principal virulence factor during Shiga toxin-producing Escherichia coli (STEC) infections. We have previously reported the inactivation of bacteriophage encoding Stx after treatment with chitosan, a linear polysaccharide polymer with cationic properties. Cationic antimicrobial peptides (cAMPs) are short linear aminoacidic sequences, with a positive net charge, which display bactericidal or bacteriostatic activity against a wide range of bacterial species. They are promising novel antibiotics since they have shown bactericidal effects against multiresistant bacteria. To evaluate whether cationic properties are responsible for bacteriophage inactivation, we tested seven cationic peptides with proven antimicrobial activity as anti-bacteriophage agents, and one random sequence cationic peptide with no antimicrobial activity as a control. We observed bacteriophage inactivation after incubation with five cAMPs, but no inactivating activity was observed with the random sequence cationic peptide or with the non-alpha helical cAMP Omiganan. Finally, to confirm peptide-bacteriophage interaction, zeta potential was analyzed by following changes on bacteriophage surface charges after peptide incubation. According to our results we could propose that: (1) direct interaction of peptides with phage is a necessary step for bacteriophage inactivation, (2) cationic properties are necessary but not sufficient for bacteriophage inactivation, and (3) inactivation by cationic peptides could be sequence (or structure) specific. Overall our data suggest that these peptides could be considered a new family of molecules potentially useful to decrease bacteriophage replication and Stx expression.
Fil: del Cogliano, Manuel Eugenio. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Hollmann, Axel. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro de Investigaciones y Transferencia de Santiago del Estero. Universidad Nacional de Santiago del Estero. Centro de Investigaciones y Transferencia de Santiago del Estero; Argentina. Universidad Nacional de Quilmes; Argentina
Fil: Martínez, Melina María Belén. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina
Fil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnologia. Instituto de Microbiologia Basica y Aplicada. Laboratorio de Micologia Molecular.; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes. Departamento de Ciencia y Tecnología. Laboratorio de Ingeniería Genética y Biología Molecular y Celular; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
description Shiga toxin (Stx) is the principal virulence factor during Shiga toxin-producing Escherichia coli (STEC) infections. We have previously reported the inactivation of bacteriophage encoding Stx after treatment with chitosan, a linear polysaccharide polymer with cationic properties. Cationic antimicrobial peptides (cAMPs) are short linear aminoacidic sequences, with a positive net charge, which display bactericidal or bacteriostatic activity against a wide range of bacterial species. They are promising novel antibiotics since they have shown bactericidal effects against multiresistant bacteria. To evaluate whether cationic properties are responsible for bacteriophage inactivation, we tested seven cationic peptides with proven antimicrobial activity as anti-bacteriophage agents, and one random sequence cationic peptide with no antimicrobial activity as a control. We observed bacteriophage inactivation after incubation with five cAMPs, but no inactivating activity was observed with the random sequence cationic peptide or with the non-alpha helical cAMP Omiganan. Finally, to confirm peptide-bacteriophage interaction, zeta potential was analyzed by following changes on bacteriophage surface charges after peptide incubation. According to our results we could propose that: (1) direct interaction of peptides with phage is a necessary step for bacteriophage inactivation, (2) cationic properties are necessary but not sufficient for bacteriophage inactivation, and (3) inactivation by cationic peptides could be sequence (or structure) specific. Overall our data suggest that these peptides could be considered a new family of molecules potentially useful to decrease bacteriophage replication and Stx expression.
publishDate 2018
dc.date.none.fl_str_mv 2018
dc.type.none.fl_str_mv info:eu-repo/semantics/publishedVersion
info:eu-repo/semantics/bookPart
http://purl.org/coar/resource_type/c_3248
info:ar-repo/semantics/parteDeLibro
status_str publishedVersion
format bookPart
dc.identifier.none.fl_str_mv http://hdl.handle.net/11336/106633
del Cogliano, Manuel Eugenio; Hollmann, Axel; Martínez, Melina María Belén; Semorile, Liliana Carmen; Ghiringhelli, Pablo Daniel; et al.; Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages; Frontiers Media S.A.; 2018; 126-131
978-2-88945-470-9
CONICET Digital
CONICET
url http://hdl.handle.net/11336/106633
identifier_str_mv del Cogliano, Manuel Eugenio; Hollmann, Axel; Martínez, Melina María Belén; Semorile, Liliana Carmen; Ghiringhelli, Pablo Daniel; et al.; Cationic antimicrobial peptides inactivate shiga toxin-encoding bacteriophages; Frontiers Media S.A.; 2018; 126-131
978-2-88945-470-9
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.3389/fchem.2017.00122
info:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00122/full
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/pdf
application/pdf
application/pdf
application/pdf
dc.publisher.none.fl_str_mv Frontiers Media S.A.
publisher.none.fl_str_mv Frontiers Media S.A.
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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score 13.070432

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