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Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis
Tuberculosis is a massive global burden and Mycobacterium tuberculosis is increasingly resistant to first- and second-line drugs. There is an acute need for new anti-mycobacterial drugs with novel targets. We previously evaluated a series of 2-aminothiazoles with activity against Mycobacterium tuber...
Autores principales: | , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Frontiers Media S.A.
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213970/ https://www.ncbi.nlm.nih.gov/pubmed/30416491 http://dx.doi.org/10.3389/fmicb.2018.02542 |
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author | Wescott, Heather H. Zuniga, Edison S. Bajpai, Anumita Trujillo, Carolina Ehrt, Sabine Schnappinger, Dirk Roberts, David M. Parish, Tanya |
author_facet | Wescott, Heather H. Zuniga, Edison S. Bajpai, Anumita Trujillo, Carolina Ehrt, Sabine Schnappinger, Dirk Roberts, David M. Parish, Tanya |
author_sort | Wescott, Heather H. |
collection | PubMed |
description | Tuberculosis is a massive global burden and Mycobacterium tuberculosis is increasingly resistant to first- and second-line drugs. There is an acute need for new anti-mycobacterial drugs with novel targets. We previously evaluated a series of 2-aminothiazoles with activity against Mycobacterium tuberculosis. In this study, we identify the glycolytic enzyme enolase as the target of these molecules using pull down studies. We demonstrate that modulation of the level of enolase expression affects sensitivity to 2-aminothiazoles; increased expression leads to resistance while decreased protein levels increase sensitivity. Exposure to 2-aminothiazoles results in increased levels of metabolites preceding the action of enolase in the glycolytic pathway and decreased ATP levels. We demonstrate that 2-aminothiazoles inhibit the activity of the human α-enolase, which could also account for the cytotoxicity of some of those molecules. If selectivity for the bacterial enzyme over the human enzyme could be achieved, enolase would represent an attractive target for M. tuberculosis drug discovery and development efforts. |
format | Online Article Text |
id | pubmed-6213970 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-62139702018-11-09 Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis Wescott, Heather H. Zuniga, Edison S. Bajpai, Anumita Trujillo, Carolina Ehrt, Sabine Schnappinger, Dirk Roberts, David M. Parish, Tanya Front Microbiol Microbiology Tuberculosis is a massive global burden and Mycobacterium tuberculosis is increasingly resistant to first- and second-line drugs. There is an acute need for new anti-mycobacterial drugs with novel targets. We previously evaluated a series of 2-aminothiazoles with activity against Mycobacterium tuberculosis. In this study, we identify the glycolytic enzyme enolase as the target of these molecules using pull down studies. We demonstrate that modulation of the level of enolase expression affects sensitivity to 2-aminothiazoles; increased expression leads to resistance while decreased protein levels increase sensitivity. Exposure to 2-aminothiazoles results in increased levels of metabolites preceding the action of enolase in the glycolytic pathway and decreased ATP levels. We demonstrate that 2-aminothiazoles inhibit the activity of the human α-enolase, which could also account for the cytotoxicity of some of those molecules. If selectivity for the bacterial enzyme over the human enzyme could be achieved, enolase would represent an attractive target for M. tuberculosis drug discovery and development efforts. Frontiers Media S.A. 2018-10-26 /pmc/articles/PMC6213970/ /pubmed/30416491 http://dx.doi.org/10.3389/fmicb.2018.02542 Text en Copyright © 2018 Wescott, Zuniga, Bajpai, Trujillo, Ehrt, Schnappinger, Roberts and Parish. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. |
spellingShingle | Microbiology Wescott, Heather H. Zuniga, Edison S. Bajpai, Anumita Trujillo, Carolina Ehrt, Sabine Schnappinger, Dirk Roberts, David M. Parish, Tanya Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title | Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title_full | Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title_fullStr | Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title_full_unstemmed | Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title_short | Identification of Enolase as the Target of 2-Aminothiazoles in Mycobacterium tuberculosis |
title_sort | identification of enolase as the target of 2-aminothiazoles in mycobacterium tuberculosis |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6213970/ https://www.ncbi.nlm.nih.gov/pubmed/30416491 http://dx.doi.org/10.3389/fmicb.2018.02542 |
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