In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study

Autores
Partouche, David; Militello, Valeria; Gomez Zavaglia, Andrea; Wien, Frank; Sandt, Christophe; Arluison, Veronique
Año de publicación
2019
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure in vitro. In the present work, we present evidence that Hfq unambiguously forms amyloid structures also in vivo. Taking into account the role of this protein in bacterial adaptation and virulence, our work opens possibilities to target Hfq amyloid self-assembly and cell location, with potential to block bacterial adaptation and treat infections.
Fil: Partouche, David. Centre National de la Recherche Scientifique; Francia. Synchrotron SOLEIL; Francia. Université Paris-Saclay; Francia
Fil: Militello, Valeria. Università degli Studi di Palermo; Italia
Fil: Gomez Zavaglia, Andrea. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Wien, Frank. Synchrotron SOLEIL; Francia
Fil: Sandt, Christophe. Synchrotron SOLEIL; Francia
Fil: Arluison, Veronique. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; Francia. Université Paris-Saclay; Francia
Materia
HFQ
FTIR
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:11336/106718
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/106718
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy StudyPartouche, DavidMilitello, ValeriaGomez Zavaglia, AndreaWien, FrankSandt, ChristopheArluison, VeroniqueHFQFTIRhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure in vitro. In the present work, we present evidence that Hfq unambiguously forms amyloid structures also in vivo. Taking into account the role of this protein in bacterial adaptation and virulence, our work opens possibilities to target Hfq amyloid self-assembly and cell location, with potential to block bacterial adaptation and treat infections.Fil: Partouche, David. Centre National de la Recherche Scientifique; Francia. Synchrotron SOLEIL; Francia. Université Paris-Saclay; FranciaFil: Militello, Valeria. Università degli Studi di Palermo; ItaliaFil: Gomez Zavaglia, Andrea. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Wien, Frank. Synchrotron SOLEIL; FranciaFil: Sandt, Christophe. Synchrotron SOLEIL; FranciaFil: Arluison, Veronique. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; Francia. Université Paris-Saclay; FranciaMDPI2019-03info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/106718Partouche, David; Militello, Valeria; Gomez Zavaglia, Andrea; Wien, Frank; Sandt, Christophe; et al.; In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study; MDPI; Pathogens; 8; 1; 3-2019; 1-122076-0817CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/8/1/36info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens8010036info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-10-22T12:00:56Zoai:ri.conicet.gov.ar:11336/106718instacron: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:34982025-10-22 12:00:56.865CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
title In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
spellingShingle In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
Partouche, David
HFQ
FTIR
title_short In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
title_full In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
title_fullStr In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
title_full_unstemmed In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
title_sort In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study
dc.creator.none.fl_str_mv Partouche, David
Militello, Valeria
Gomez Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Veronique
author Partouche, David
author_facet Partouche, David
Militello, Valeria
Gomez Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Veronique
author_role author
author2 Militello, Valeria
Gomez Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Veronique
author2_role author
author
author
author
author
dc.subject.none.fl_str_mv HFQ
FTIR
topic HFQ
FTIR
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure in vitro. In the present work, we present evidence that Hfq unambiguously forms amyloid structures also in vivo. Taking into account the role of this protein in bacterial adaptation and virulence, our work opens possibilities to target Hfq amyloid self-assembly and cell location, with potential to block bacterial adaptation and treat infections.
Fil: Partouche, David. Centre National de la Recherche Scientifique; Francia. Synchrotron SOLEIL; Francia. Université Paris-Saclay; Francia
Fil: Militello, Valeria. Università degli Studi di Palermo; Italia
Fil: Gomez Zavaglia, Andrea. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Wien, Frank. Synchrotron SOLEIL; Francia
Fil: Sandt, Christophe. Synchrotron SOLEIL; Francia
Fil: Arluison, Veronique. Centre National de la Recherche Scientifique; Francia. Université Paris Diderot - Paris 7; Francia. Université Paris-Saclay; Francia
description Hfq is a bacterial protein that regulates gene expression at the post-transcriptional level in Gram-negative bacteria. We have previously shown that Escherichia coli Hfq protein, and more precisely its C-terminal region (CTR), self-assembles into an amyloid-like structure in vitro. In the present work, we present evidence that Hfq unambiguously forms amyloid structures also in vivo. Taking into account the role of this protein in bacterial adaptation and virulence, our work opens possibilities to target Hfq amyloid self-assembly and cell location, with potential to block bacterial adaptation and treat infections.
publishDate 2019
dc.date.none.fl_str_mv 2019-03
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/11336/106718
Partouche, David; Militello, Valeria; Gomez Zavaglia, Andrea; Wien, Frank; Sandt, Christophe; et al.; In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study; MDPI; Pathogens; 8; 1; 3-2019; 1-12
2076-0817
CONICET Digital
CONICET
url http://hdl.handle.net/11336/106718
identifier_str_mv Partouche, David; Militello, Valeria; Gomez Zavaglia, Andrea; Wien, Frank; Sandt, Christophe; et al.; In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study; MDPI; Pathogens; 8; 1; 3-2019; 1-12
2076-0817
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/8/1/36
info:eu-repo/semantics/altIdentifier/doi/10.3390/pathogens8010036
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
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
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 12.982451

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