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The mechanism of action of pepR, a viral-derived peptide, against Staphylococcus aureus biofilms

2019Journal article Open access
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dc.contributor.authorPinto, Sandra
dc.contributor.authorDias, Susana
dc.contributor.authorCruz, Ana F
dc.contributor.authorMil-Homens, Dalila
dc.contributor.authorFernandes, Fabio
dc.contributor.authorValle, Javier
dc.contributor.authorAndreu, David
dc.contributor.authorPrieto, Manuel
dc.contributor.authorCastanho, Miguel A. R. B.
dc.contributor.authorCoutinho, Ana
dc.contributor.authorVeiga, Ana Salomé
dc.date.accessioned2022-01-11T16:27:19Z
dc.date.available2022-01-11T16:27:19Z
dc.date.issued2019
dc.description© The Author(s) 2019. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.compt_PT
dc.description.abstractObjectives: To investigate the mechanism of action at the molecular level of pepR, a multifunctional peptide derived from the Dengue virus capsid protein, against Staphylococcus aureus biofilms. Methods: Biofilm mass, metabolic activity and viability were quantified using conventional microbiology techniques, while fluorescence imaging methods, including a real-time calcein release assay, were employed to investigate the kinetics of pepR activity at different biofilm depths. Results: Using flow cytometry-based assays, we showed that pepR is able to prevent staphylococcal biofilm formation due to a fast killing of planktonic bacteria, which in turn resulted from a peptide-induced increase in the permeability of the bacterial membranes. The activity of pepR against pre-formed biofilms was evaluated through the application of a quantitative live/dead confocal laser scanning microscopy (CLSM) assay. The results show that the bactericidal activity of pepR on pre-formed biofilms is dose and depth dependent. A CLSM-based assay of calcein release from biofilm-embedded bacteria was further developed to indirectly assess the diffusion and membrane permeabilization properties of pepR throughout the biofilm. A slower diffusion and delayed activity of the peptide at deeper layers of the biofilm were quantified. Conclusions: Overall, our results show that the activity of pepR on pre-formed biofilms is controlled by its diffusion along the biofilm layers, an effect that can be counteracted by an additional administration of peptide. Our study sheds new light on the antibiofilm mechanism of action of antimicrobial peptides, particularly the importance of their diffusion properties through the biofilm matrix on their activity.pt_PT
dc.description.sponsorshipThis work was supported by the Fundação para a Ciência e a Tecnologia (FCT)/Ministério da Ciência, Tecnologia e Ensino Superior (MCTES) (projects PTDC/QEQ-MED/4412/2014, FAPESP/20107/2014, SAICTPAC/0019/2015, PPBI-POCI-01-0145-FEDER-022122); by the Spanish Ministry of Economy and Competitiveness (MINECO) (grant AGL2014-5239-C2-2R); and by the Marie Skłodowska-Curie Research and Innovation Staff Exchange (grant H2020-MSCA-RISE-2014–644167). We also acknowledge project UID/BIM/50005/2019, funded by FCT/MCTES through Fundos do Orçamento de Estado. S. N. P., S. A. D., A. F. C. and D. M.-H. are the recipients of fellowships from the FCT (SFRH/BPD/92409/2013, PD/BD/114425/2016, PD/BD/136866/2018 and SFRH/BPD/91831/2012, respectively). A. S. V. and F. F. are FCT Researchers (IF/00803/2012 and IF/00386/2015, respectively).pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.citationJ Antimicrob Chemother. 2019 Sep 1;74(9):2617-2625pt_PT
dc.identifier.doi10.1093/jac/dkz223pt_PT
dc.identifier.eissn1460-2091
dc.identifier.issn0305-7453
dc.identifier.urihttp://hdl.handle.net/10451/50777
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.publisherOxford University Presspt_PT
dc.relationPPBI-POCI-01-0145-FEDER-022122pt_PT
dc.relationTowards the development of innovative highly effective dual action anti-HIV peptides
dc.relationLipid Oxidation in membrane and cell Biophysics: From Functional nanosensors to the impact on amyloid formation. Application of advanced fluorescence, X-Ray scattering and microscopy Techniques
dc.relationPRECISION ONCOLOGY BY INNOVATIVE THERAPIES AND TECHNOLOGIES
dc.relationInstituto de Medicina Molecular
dc.relationIF/00803/2012pt_PT
dc.relationTowards the development of antimicrobial peptides active against bacterial biofilms
dc.relationDevelopment of viral-derived peptides to fight bacterial bioflims and unraveling their mechanism of action
dc.relation.publisherversionhttps://academic.oup.com/jacpt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.titleThe mechanism of action of pepR, a viral-derived peptide, against Staphylococcus aureus biofilmspt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.awardTitleTowards the development of innovative highly effective dual action anti-HIV peptides
oaire.awardTitleLipid Oxidation in membrane and cell Biophysics: From Functional nanosensors to the impact on amyloid formation. Application of advanced fluorescence, X-Ray scattering and microscopy Techniques
oaire.awardTitlePRECISION ONCOLOGY BY INNOVATIVE THERAPIES AND TECHNOLOGIES
oaire.awardTitleInstituto de Medicina Molecular
oaire.awardTitleTowards the development of antimicrobial peptides active against bacterial biofilms
oaire.awardTitleDevelopment of viral-derived peptides to fight bacterial bioflims and unraveling their mechanism of action
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/PTDC%2FQEQ-MED%2F4412%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/3599-PPCDT/FAPESP%2F20107%2F2014/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/9471 - RIDTI/SAICTPAC%2F0019%2F2015/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UID%2FBIM%2F50005%2F2019/PT
oaire.awardURIinfo:eu-repo/grantAgreement/FCT/SFRH/SFRH%2FBPD%2F92409%2F2013/PT
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oaire.citation.endPage2625pt_PT
oaire.citation.issue9pt_PT
oaire.citation.startPage2617pt_PT
oaire.citation.titleJournal of Antimicrobial Chemotherapypt_PT
oaire.citation.volume74pt_PT
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person.givenNameMiguel
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