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Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G
Protein kinase G (PknG) is a eukaryotic-like serine/threonine kinase that is expressed by Mycobacterium tuberculosis and promotes survival of mycobacteria in host macrophages by suppressing phagosome-lysosome fusion. Thus, compounds showing inhibitory activity against PknG are promising anti-mycobac...
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/PMC6052090/ https://www.ncbi.nlm.nih.gov/pubmed/30050511 http://dx.doi.org/10.3389/fmicb.2018.01517 |
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author | Kanehiro, Yuichi Tomioka, Haruaki Pieters, Jean Tatano, Yutaka Kim, Hyoji Iizasa, Hisashi Yoshiyama, Hironori |
author_facet | Kanehiro, Yuichi Tomioka, Haruaki Pieters, Jean Tatano, Yutaka Kim, Hyoji Iizasa, Hisashi Yoshiyama, Hironori |
author_sort | Kanehiro, Yuichi |
collection | PubMed |
description | Protein kinase G (PknG) is a eukaryotic-like serine/threonine kinase that is expressed by Mycobacterium tuberculosis and promotes survival of mycobacteria in host macrophages by suppressing phagosome-lysosome fusion. Thus, compounds showing inhibitory activity against PknG are promising anti-mycobacterial agents. We therefore aimed to develop anti-mycobacterial agents by identifying new PknG inhibitors. A luciferase-based PknG kinase assay was used to screen potential inhibitors of PknG. We found that four compounds, namely AZD7762, R406, R406-free base, and CYC116, inhibited PknG activities. AZD7762, R406, and R406-free base promoted transfer of mycobacteria to lysosomes. These compounds also inhibited survival of M. bovis Bacillus Calmette–Guérin (BCG) inside human macrophages. Furthermore, R406 and R406-free base showed bactericidal activity against BCG in infected human macrophages without cytotoxicity. The PknG inhibitors identified in this study by the luciferase-based PknG kinase assay may be promising leads for the development of anti-mycobacterial agents. |
format | Online Article Text |
id | pubmed-6052090 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Frontiers Media S.A. |
record_format | MEDLINE/PubMed |
spelling | pubmed-60520902018-07-26 Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G Kanehiro, Yuichi Tomioka, Haruaki Pieters, Jean Tatano, Yutaka Kim, Hyoji Iizasa, Hisashi Yoshiyama, Hironori Front Microbiol Microbiology Protein kinase G (PknG) is a eukaryotic-like serine/threonine kinase that is expressed by Mycobacterium tuberculosis and promotes survival of mycobacteria in host macrophages by suppressing phagosome-lysosome fusion. Thus, compounds showing inhibitory activity against PknG are promising anti-mycobacterial agents. We therefore aimed to develop anti-mycobacterial agents by identifying new PknG inhibitors. A luciferase-based PknG kinase assay was used to screen potential inhibitors of PknG. We found that four compounds, namely AZD7762, R406, R406-free base, and CYC116, inhibited PknG activities. AZD7762, R406, and R406-free base promoted transfer of mycobacteria to lysosomes. These compounds also inhibited survival of M. bovis Bacillus Calmette–Guérin (BCG) inside human macrophages. Furthermore, R406 and R406-free base showed bactericidal activity against BCG in infected human macrophages without cytotoxicity. The PknG inhibitors identified in this study by the luciferase-based PknG kinase assay may be promising leads for the development of anti-mycobacterial agents. Frontiers Media S.A. 2018-07-12 /pmc/articles/PMC6052090/ /pubmed/30050511 http://dx.doi.org/10.3389/fmicb.2018.01517 Text en Copyright © 2018 Kanehiro, Tomioka, Pieters, Tatano, Kim, Iizasa and Yoshiyama. 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 Kanehiro, Yuichi Tomioka, Haruaki Pieters, Jean Tatano, Yutaka Kim, Hyoji Iizasa, Hisashi Yoshiyama, Hironori Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title | Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title_full | Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title_fullStr | Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title_full_unstemmed | Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title_short | Identification of Novel Mycobacterial Inhibitors Against Mycobacterial Protein Kinase G |
title_sort | identification of novel mycobacterial inhibitors against mycobacterial protein kinase g |
topic | Microbiology |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6052090/ https://www.ncbi.nlm.nih.gov/pubmed/30050511 http://dx.doi.org/10.3389/fmicb.2018.01517 |
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