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

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 wo...

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Autores principales: Partouche, David, Militello, Valeria, Gomez-Zavaglia, Andrea, Wien, Frank, Sandt, Christophe, Arluison, Véronique
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6471401/
https://www.ncbi.nlm.nih.gov/pubmed/30889801
http://dx.doi.org/10.3390/pathogens8010036
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author Partouche, David
Militello, Valeria
Gomez-Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Véronique
author_facet Partouche, David
Militello, Valeria
Gomez-Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Véronique
author_sort Partouche, David
collection PubMed
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 important potential to block bacterial adaptation and treat infections.
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spelling pubmed-64714012019-04-27 In Situ Characterization of Hfq Bacterial Amyloid: A Fourier-Transform Infrared Spectroscopy Study Partouche, David Militello, Valeria Gomez-Zavaglia, Andrea Wien, Frank Sandt, Christophe Arluison, Véronique Pathogens Article 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 important potential to block bacterial adaptation and treat infections. MDPI 2019-03-18 /pmc/articles/PMC6471401/ /pubmed/30889801 http://dx.doi.org/10.3390/pathogens8010036 Text en © 2019 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Partouche, David
Militello, Valeria
Gomez-Zavaglia, Andrea
Wien, Frank
Sandt, Christophe
Arluison, Véronique
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
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_short 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
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6471401/
https://www.ncbi.nlm.nih.gov/pubmed/30889801
http://dx.doi.org/10.3390/pathogens8010036
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