High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action

The increase in speed of the high-speed atomic force microscopy (HS-AFM) compared to that of the conventional AFM made possible the first-ever visualisation at the molecular-level of the activity of an antimicrobial peptide on a membrane. We investigated the medically prescribed but poorly understoo...

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Detalles Bibliográficos
Autores: Zuttion, Francesca, Colom, Adai, Matile, Stefan, Farago, Denes, Pompeo, Frédérique, Kokavecz, Janos, Galinier, Anne, Sturgis, James, Casuso, Ignacio
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2020
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/338046
Acceso en línea:http://hdl.handle.net/10261/338046
https://api.elsevier.com/content/abstract/scopus_id/85097432725
Access Level:acceso abierto
Palabra clave:Applications of AFM
Nanoscale biophysics
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spelling High-speed atomic force microscopy highlights new molecular mechanism of daptomycin actionZuttion, FrancescaColom, AdaiMatile, StefanFarago, DenesPompeo, FrédériqueKokavecz, JanosGalinier, AnneSturgis, JamesCasuso, IgnacioApplications of AFMNanoscale biophysicsThe increase in speed of the high-speed atomic force microscopy (HS-AFM) compared to that of the conventional AFM made possible the first-ever visualisation at the molecular-level of the activity of an antimicrobial peptide on a membrane. We investigated the medically prescribed but poorly understood lipopeptide Daptomycin under infection-like conditions (37 °C, bacterial lipid composition and antibiotic concentrations). We confirmed so far hypothetical models: Dap oligomerization and the existence of half pores. Moreover, we detected unknown molecular mechanisms: new mechanisms to form toroidal pores or to resist Dap action, and to unprecedently quantify the energy profile of interacting oligomers. Finally, the biological and medical relevance of the findings was ensured by a multi-scale multi-nativeness—from the molecule to the cell—correlation of molecular-level information from living bacteria (Bacillus subtilis strains) to liquid-suspended vesicles and supported-membranes using electron and optical microscopies and the lipid tension probe FliptR, where we found that the cells with a healthier state of their cell wall show smaller membrane deformations.This work was supported by a Agence National de la Recherche (ANR) grant ANR-16-CE15-0023, the Inserm, the CNRS, Aix-Marseille Univ., the University of Geneva, the National Centre Chemical Biology (NCCR), the NCCR Molecular Systems Engineering and the Swiss NSF.Peer reviewedNature Publishing GroupAgence Nationale de la Recherche (France)Institut National de la Santé et de la Recherche Médicale (France)Centre National de la Recherche Scientifique (France)Aix-Marseille UniversitéUniversité de GenèveNational Centres of Competence in Research (Switzerland)Swiss National Science FoundationGalinier, Anne [0000-0001-5988-016X]Sturgis, James [0000-0001-5125-7699]Casuso, Ignacio [0000-0001-7192-0136]Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]202320232020info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Publisher's versioninfo:eu-repo/semantics/publishedVersionapplication/pdfhttp://hdl.handle.net/10261/338046https://api.elsevier.com/content/abstract/scopus_id/85097432725reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Ingléshttps://doi.org/10.1038/s41467-020-19710-zSíinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/3380462026-05-22T06:33:51Z
dc.title.none.fl_str_mv High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
title High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
spellingShingle High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
Zuttion, Francesca
Applications of AFM
Nanoscale biophysics
title_short High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
title_full High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
title_fullStr High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
title_full_unstemmed High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
title_sort High-speed atomic force microscopy highlights new molecular mechanism of daptomycin action
dc.creator.none.fl_str_mv Zuttion, Francesca
Colom, Adai
Matile, Stefan
Farago, Denes
Pompeo, Frédérique
Kokavecz, Janos
Galinier, Anne
Sturgis, James
Casuso, Ignacio
author Zuttion, Francesca
author_facet Zuttion, Francesca
Colom, Adai
Matile, Stefan
Farago, Denes
Pompeo, Frédérique
Kokavecz, Janos
Galinier, Anne
Sturgis, James
Casuso, Ignacio
author_role author
author2 Colom, Adai
Matile, Stefan
Farago, Denes
Pompeo, Frédérique
Kokavecz, Janos
Galinier, Anne
Sturgis, James
Casuso, Ignacio
author2_role author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Agence Nationale de la Recherche (France)
Institut National de la Santé et de la Recherche Médicale (France)
Centre National de la Recherche Scientifique (France)
Aix-Marseille Université
Université de Genève
National Centres of Competence in Research (Switzerland)
Swiss National Science Foundation
Galinier, Anne [0000-0001-5988-016X]
Sturgis, James [0000-0001-5125-7699]
Casuso, Ignacio [0000-0001-7192-0136]
Consejo Superior de Investigaciones Científicas [https://ror.org/02gfc7t72]
dc.subject.none.fl_str_mv Applications of AFM
Nanoscale biophysics
topic Applications of AFM
Nanoscale biophysics
description The increase in speed of the high-speed atomic force microscopy (HS-AFM) compared to that of the conventional AFM made possible the first-ever visualisation at the molecular-level of the activity of an antimicrobial peptide on a membrane. We investigated the medically prescribed but poorly understood lipopeptide Daptomycin under infection-like conditions (37 °C, bacterial lipid composition and antibiotic concentrations). We confirmed so far hypothetical models: Dap oligomerization and the existence of half pores. Moreover, we detected unknown molecular mechanisms: new mechanisms to form toroidal pores or to resist Dap action, and to unprecedently quantify the energy profile of interacting oligomers. Finally, the biological and medical relevance of the findings was ensured by a multi-scale multi-nativeness—from the molecule to the cell—correlation of molecular-level information from living bacteria (Bacillus subtilis strains) to liquid-suspended vesicles and supported-membranes using electron and optical microscopies and the lipid tension probe FliptR, where we found that the cells with a healthier state of their cell wall show smaller membrane deformations.
publishDate 2020
dc.date.none.fl_str_mv 2020
2023
2023
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Publisher's version
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/338046
https://api.elsevier.com/content/abstract/scopus_id/85097432725
url http://hdl.handle.net/10261/338046
https://api.elsevier.com/content/abstract/scopus_id/85097432725
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv https://doi.org/10.1038/s41467-020-19710-z
Sí
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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