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2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain

There is an urgent need to develop new drugs against tuberculosis. In particular, it is critical to target drug tolerant Mycobacterium tuberculosis (M. tuberculosis), responsible, in part, for the lengthy antibiotic regimen required for treatment. We previously postulated that the presence of in viv...

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Autores principales: Jeon, Albert Byungyun, Ackart, David F., Li, Wei, Jackson, Mary, Melander, Roberta J., Melander, Christian, Abramovitch, Robert B., Chicco, Adam J., Basaraba, Randall J., Obregón-Henao, Andrés
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365497/
https://www.ncbi.nlm.nih.gov/pubmed/30728417
http://dx.doi.org/10.1038/s41598-018-38064-7
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author Jeon, Albert Byungyun
Ackart, David F.
Li, Wei
Jackson, Mary
Melander, Roberta J.
Melander, Christian
Abramovitch, Robert B.
Chicco, Adam J.
Basaraba, Randall J.
Obregón-Henao, Andrés
author_facet Jeon, Albert Byungyun
Ackart, David F.
Li, Wei
Jackson, Mary
Melander, Roberta J.
Melander, Christian
Abramovitch, Robert B.
Chicco, Adam J.
Basaraba, Randall J.
Obregón-Henao, Andrés
author_sort Jeon, Albert Byungyun
collection PubMed
description There is an urgent need to develop new drugs against tuberculosis. In particular, it is critical to target drug tolerant Mycobacterium tuberculosis (M. tuberculosis), responsible, in part, for the lengthy antibiotic regimen required for treatment. We previously postulated that the presence of in vivo biofilm-like communities of M. tuberculosis could contribute to this drug tolerance. Consistent with this hypothesis, certain 2-aminoimidazole (2-AIs) molecules with anti-biofilm activity were shown to revert mycobacterial drug tolerance in an in vitro M. tuberculosis biofilm model. While exploring their mechanism of action, it was serendipitously observed that these 2-AI molecules also potentiated β-lactam antibiotics by affecting mycobacterial protein secretion and lipid export. As these two bacterial processes are energy-dependent, herein it was evaluated if 2-AI compounds affect mycobacterial bioenergetics. At low concentrations, 2B8, the lead 2-AI compound, collapsed both components of the proton motive force, similar to other cationic amphiphiles. Interestingly, however, the minimum inhibitory concentration of 2B8 against M. tuberculosis correlated with a higher drug concentration determined to interfere with the mycobacterial electron transport chain. Collectively, this study elucidates the mechanism of action of 2-AIs against M. tuberculosis, providing a tool to better understand mycobacterial bioenergetics and develop compounds with improved anti-mycobacterial activity.
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spelling pubmed-63654972019-02-08 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain Jeon, Albert Byungyun Ackart, David F. Li, Wei Jackson, Mary Melander, Roberta J. Melander, Christian Abramovitch, Robert B. Chicco, Adam J. Basaraba, Randall J. Obregón-Henao, Andrés Sci Rep Article There is an urgent need to develop new drugs against tuberculosis. In particular, it is critical to target drug tolerant Mycobacterium tuberculosis (M. tuberculosis), responsible, in part, for the lengthy antibiotic regimen required for treatment. We previously postulated that the presence of in vivo biofilm-like communities of M. tuberculosis could contribute to this drug tolerance. Consistent with this hypothesis, certain 2-aminoimidazole (2-AIs) molecules with anti-biofilm activity were shown to revert mycobacterial drug tolerance in an in vitro M. tuberculosis biofilm model. While exploring their mechanism of action, it was serendipitously observed that these 2-AI molecules also potentiated β-lactam antibiotics by affecting mycobacterial protein secretion and lipid export. As these two bacterial processes are energy-dependent, herein it was evaluated if 2-AI compounds affect mycobacterial bioenergetics. At low concentrations, 2B8, the lead 2-AI compound, collapsed both components of the proton motive force, similar to other cationic amphiphiles. Interestingly, however, the minimum inhibitory concentration of 2B8 against M. tuberculosis correlated with a higher drug concentration determined to interfere with the mycobacterial electron transport chain. Collectively, this study elucidates the mechanism of action of 2-AIs against M. tuberculosis, providing a tool to better understand mycobacterial bioenergetics and develop compounds with improved anti-mycobacterial activity. Nature Publishing Group UK 2019-02-06 /pmc/articles/PMC6365497/ /pubmed/30728417 http://dx.doi.org/10.1038/s41598-018-38064-7 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Jeon, Albert Byungyun
Ackart, David F.
Li, Wei
Jackson, Mary
Melander, Roberta J.
Melander, Christian
Abramovitch, Robert B.
Chicco, Adam J.
Basaraba, Randall J.
Obregón-Henao, Andrés
2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title_full 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title_fullStr 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title_full_unstemmed 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title_short 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
title_sort 2-aminoimidazoles collapse mycobacterial proton motive force and block the electron transport chain
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6365497/
https://www.ncbi.nlm.nih.gov/pubmed/30728417
http://dx.doi.org/10.1038/s41598-018-38064-7
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