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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...
Autores principales: | , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2019
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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. |
format | Online Article Text |
id | pubmed-6365497 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
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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