Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Turbant, Florian, Partouche, David, El Hamoui, Omar, Trépout, Sylvain, Legoubey, Théa, Wien, Frank, Arluison, Véronique
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
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
_version_ 1783671011482271744
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
work_keys_str_mv AT turbantflorian apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT partouchedavid apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT elhamouiomar apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT trepoutsylvain apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT legoubeythea apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT wienfrank apomorphinetargetsthepleiotropicbacterialregulatorhfq
AT arluisonveronique apomorphinetargetsthepleiotropicbacterialregulatorhfq