Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis

Previously, we showed that mutations in Mycobacterium tuberculosis panD, involved in coenzyme A biosynthesis, cause resistance against pyrazinoic acid, the bioactive component of the prodrug pyrazinamide. To identify additional resistance mechanisms, we isolated mutants resistant against pyrazinoic...

Descripción completa

Detalles Bibliográficos
Autores principales: Yee, Michelle, Gopal, Pooja, Dick, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Microbiology 2017
Materias:
Mechanisms of Resistance
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5278685/
https://www.ncbi.nlm.nih.gov/pubmed/27872068
http://dx.doi.org/10.1128/AAC.02342-16
_version_ 1782502677859532800
author Yee, Michelle
Gopal, Pooja
Dick, Thomas
author_facet Yee, Michelle
Gopal, Pooja
Dick, Thomas
author_sort Yee, Michelle
collection PubMed
description Previously, we showed that mutations in Mycobacterium tuberculosis panD, involved in coenzyme A biosynthesis, cause resistance against pyrazinoic acid, the bioactive component of the prodrug pyrazinamide. To identify additional resistance mechanisms, we isolated mutants resistant against pyrazinoic acid and subjected panD wild-type strains to whole-genome sequencing. Eight of the nine resistant strains harbored missense mutations in the unfoldase ClpC1 associated with the caseinolytic protease complex.
format Online
Article
Text
id pubmed-5278685
institution National Center for Biotechnology Information
language English
publishDate 2017
publisher American Society for Microbiology
record_format MEDLINE/PubMed
spelling pubmed-52786852017-02-06 Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis Yee, Michelle Gopal, Pooja Dick, Thomas Antimicrob Agents Chemother Mechanisms of Resistance Previously, we showed that mutations in Mycobacterium tuberculosis panD, involved in coenzyme A biosynthesis, cause resistance against pyrazinoic acid, the bioactive component of the prodrug pyrazinamide. To identify additional resistance mechanisms, we isolated mutants resistant against pyrazinoic acid and subjected panD wild-type strains to whole-genome sequencing. Eight of the nine resistant strains harbored missense mutations in the unfoldase ClpC1 associated with the caseinolytic protease complex. American Society for Microbiology 2017-01-24 /pmc/articles/PMC5278685/ /pubmed/27872068 http://dx.doi.org/10.1128/AAC.02342-16 Text en Copyright © 2017 Yee et al. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license (http://creativecommons.org/licenses/by/4.0/) .
spellingShingle Mechanisms of Resistance
Yee, Michelle
Gopal, Pooja
Dick, Thomas
Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title_full Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title_fullStr Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title_full_unstemmed Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title_short Missense Mutations in the Unfoldase ClpC1 of the Caseinolytic Protease Complex Are Associated with Pyrazinamide Resistance in Mycobacterium tuberculosis
title_sort missense mutations in the unfoldase clpc1 of the caseinolytic protease complex are associated with pyrazinamide resistance in mycobacterium tuberculosis
topic Mechanisms of Resistance
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5278685/
https://www.ncbi.nlm.nih.gov/pubmed/27872068
http://dx.doi.org/10.1128/AAC.02342-16
work_keys_str_mv AT yeemichelle missensemutationsintheunfoldaseclpc1ofthecaseinolyticproteasecomplexareassociatedwithpyrazinamideresistanceinmycobacteriumtuberculosis
AT gopalpooja missensemutationsintheunfoldaseclpc1ofthecaseinolyticproteasecomplexareassociatedwithpyrazinamideresistanceinmycobacteriumtuberculosis
AT dickthomas missensemutationsintheunfoldaseclpc1ofthecaseinolyticproteasecomplexareassociatedwithpyrazinamideresistanceinmycobacteriumtuberculosis

Ejemplares similares