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dc.creatordel Cogliano, Manuel Eugenio-
dc.creatorHollmann, Axel-
dc.creatorMartínez, Melina María Belén-
dc.creatorSemorile, Liliana Carmen-
dc.creatorGhiringhelli, Pablo Daniel-
dc.creatorMaffia, Paulo Cesar-
dc.creatorBentancor, Leticia Verónica-
dc.date2018-04-09T19:17:37Z-
dc.date2018-04-09T19:17:37Z-
dc.date2017-12-
dc.date2018-04-09T15:10:53Z-
dc.date.accessioned2019-04-29T15:48:32Z-
dc.date.available2019-04-29T15:48:32Z-
dc.date.issued2017-12-
dc.identifierdel 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-
dc.identifierhttp://hdl.handle.net/11336/41395-
dc.identifier2296-2646-
dc.identifierCONICET Digital-
dc.identifierCONICET-
dc.identifier.urihttp://rodna.bn.gov.ar:8080/jspui/handle/bnmm/302604-
dc.descriptionShiga 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.-
dc.descriptionFil: del Cogliano, Manuel Eugenio. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: 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-
dc.descriptionFil: Martínez, Melina María Belén. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Semorile, Liliana Carmen. Universidad Nacional de Quilmes; Argentina-
dc.descriptionFil: Ghiringhelli, Pablo Daniel. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Maffia, Paulo Cesar. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.descriptionFil: Bentancor, Leticia Verónica. Universidad Nacional de Quilmes; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina-
dc.formatapplication/pdf-
dc.formatapplication/pdf-
dc.languageeng-
dc.publisherFrontiers Research Foundation-
dc.relationinfo:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3389/fchem.2017.00122-
dc.relationinfo:eu-repo/semantics/altIdentifier/url/https://www.frontiersin.org/articles/10.3389/fchem.2017.00122/full-
dc.rightsinfo:eu-repo/semantics/openAccess-
dc.rightshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/-
dc.sourcereponame:CONICET Digital (CONICET)-
dc.sourceinstname:Consejo Nacional de Investigaciones Científicas y Técnicas-
dc.sourceinstacron:CONICET-
dc.source.urihttp://hdl.handle.net/11336/66536-
dc.subjectBACTERIOPHAGES (PHAGES)-
dc.subjectESCHERICHIA COLI O157-
dc.subjectANTIMICROBIAL PEPTIDES-
dc.subjectANTI-INFECTIVE AGENTS-
dc.subjectHEMOLYTIC UREMIC SYNDROME (HUS)-
dc.subjectOtras Ciencias Biológicas-
dc.subjectCiencias Biológicas-
dc.subjectCIENCIAS NATURALES Y EXACTAS-
dc.titleCationic Antimicrobial Peptides Inactivate Shiga Toxin-Encoding Bacteriophages-
dc.typeinfo:eu-repo/semantics/article-
dc.typeinfo:eu-repo/semantics/publishedVersion-
dc.typeinfo:ar-repo/semantics/articulo-
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