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
2017
Idioma
inglés
Tipo de recurso
artículo
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; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes; Argentina. 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
Fil: Martínez, Melina María Belén. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes; Argentina
Fil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Materia
BACTERIOPHAGES (PHAGES)
ESCHERICHIA COLI O157
ANTIMICROBIAL PEPTIDES
ANTI-INFECTIVE AGENTS
HEMOLYTIC UREMIC SYNDROME (HUS)
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/41395
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/41395
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 VerónicaBACTERIOPHAGES (PHAGES)ESCHERICHIA COLI O157ANTIMICROBIAL PEPTIDESANTI-INFECTIVE AGENTSHEMOLYTIC UREMIC SYNDROME (HUS)https://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; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Hollmann, Axel. Universidad Nacional de Quilmes; Argentina. 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; ArgentinaFil: Martínez, Melina María Belén. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes; ArgentinaFil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFrontiers Research Foundation2017-12info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/41395del 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 Research Foundation; Frontiers in Chemistry; 5; 12-2017; 1-6; 1222296-2646CONICET 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-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:38:27Zoai:ri.conicet.gov.ar:11336/41395instacron: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 09:38:27.292CONICET 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
BACTERIOPHAGES (PHAGES)
ESCHERICHIA COLI O157
ANTIMICROBIAL PEPTIDES
ANTI-INFECTIVE AGENTS
HEMOLYTIC UREMIC SYNDROME (HUS)
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.subject.none.fl_str_mv BACTERIOPHAGES (PHAGES)
ESCHERICHIA COLI O157
ANTIMICROBIAL PEPTIDES
ANTI-INFECTIVE AGENTS
HEMOLYTIC UREMIC SYNDROME (HUS)
topic BACTERIOPHAGES (PHAGES)
ESCHERICHIA COLI O157
ANTIMICROBIAL PEPTIDES
ANTI-INFECTIVE AGENTS
HEMOLYTIC UREMIC SYNDROME (HUS)
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; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Hollmann, Axel. Universidad Nacional de Quilmes; Argentina. 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
Fil: Martínez, Melina María Belén. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes; Argentina
Fil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes; 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 2017
dc.date.none.fl_str_mv 2017-12
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/11336/41395
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 Research Foundation; Frontiers in Chemistry; 5; 12-2017; 1-6; 122
2296-2646
CONICET Digital
CONICET
url http://hdl.handle.net/11336/41395
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 Research Foundation; Frontiers in Chemistry; 5; 12-2017; 1-6; 122
2296-2646
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-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
dc.publisher.none.fl_str_mv Frontiers Research Foundation
publisher.none.fl_str_mv Frontiers Research Foundation
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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