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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...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2019
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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. |
format | Online Article Text |
id | pubmed-6471401 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
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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