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Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq
Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance for bacterial adaptation and survival in host...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8000489/ https://www.ncbi.nlm.nih.gov/pubmed/33806663 http://dx.doi.org/10.3390/antibiotics10030257 |
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author | Turbant, Florian Partouche, David El Hamoui, Omar Trépout, Sylvain Legoubey, Théa Wien, Frank Arluison, Véronique |
author_facet | Turbant, Florian Partouche, David El Hamoui, Omar Trépout, Sylvain Legoubey, Théa Wien, Frank Arluison, Véronique |
author_sort | Turbant, Florian |
collection | PubMed |
description | Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance for bacterial adaptation and survival in hosts. Small RNAs and Hfq are, for instance, involved in the response to antibiotics. Previous work has shown that the E. coli Hfq C-terminal region (Hfq-CTR) self-assembles into an amyloid structure. It was also demonstrated that the green tea compound EpiGallo Catechin Gallate (EGCG) binds to Hfq-CTR amyloid fibrils and remodels them into nonamyloid structures. Thus, compounds that target the amyloid region of Hfq may be used as antibacterial agents. Here, we show that another compound that inhibits amyloid formation, apomorphine, may also serve as a new antibacterial. Our results provide an alternative in order to repurpose apomorphine, commonly used in the treatment of Parkinson’s disease, as an antibiotic to block bacterial adaptation to treat infections. |
format | Online Article Text |
id | pubmed-8000489 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-80004892021-03-28 Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq Turbant, Florian Partouche, David El Hamoui, Omar Trépout, Sylvain Legoubey, Théa Wien, Frank Arluison, Véronique Antibiotics (Basel) Article Hfq is a bacterial regulator with key roles in gene expression. The protein notably regulates translation efficiency and RNA decay in Gram-negative bacteria, thanks to its binding to small regulatory noncoding RNAs. This property is of primary importance for bacterial adaptation and survival in hosts. Small RNAs and Hfq are, for instance, involved in the response to antibiotics. Previous work has shown that the E. coli Hfq C-terminal region (Hfq-CTR) self-assembles into an amyloid structure. It was also demonstrated that the green tea compound EpiGallo Catechin Gallate (EGCG) binds to Hfq-CTR amyloid fibrils and remodels them into nonamyloid structures. Thus, compounds that target the amyloid region of Hfq may be used as antibacterial agents. Here, we show that another compound that inhibits amyloid formation, apomorphine, may also serve as a new antibacterial. Our results provide an alternative in order to repurpose apomorphine, commonly used in the treatment of Parkinson’s disease, as an antibiotic to block bacterial adaptation to treat infections. MDPI 2021-03-04 /pmc/articles/PMC8000489/ /pubmed/33806663 http://dx.doi.org/10.3390/antibiotics10030257 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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/ (https://creativecommons.org/licenses/by/4.0/) ). |
spellingShingle | Article Turbant, Florian Partouche, David El Hamoui, Omar Trépout, Sylvain Legoubey, Théa Wien, Frank Arluison, Véronique Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title | Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title_full | Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title_fullStr | Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title_full_unstemmed | Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title_short | Apomorphine Targets the Pleiotropic Bacterial Regulator Hfq |
title_sort | apomorphine targets the pleiotropic bacterial regulator hfq |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8000489/ https://www.ncbi.nlm.nih.gov/pubmed/33806663 http://dx.doi.org/10.3390/antibiotics10030257 |
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