Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>

ABSTRACT Peptidoglycan (PG), a polymer cross-linked by d-amino acid-containing peptides, is an essential component of the bacterial cell wall. We found that a fluorescent d-alanine analog (FDAA) incorporates chiefly at one of the two poles in Mycobacterium smegmatis but that polar dominance varies a...

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Autores principales:	Helene Botella, Guangli Yang, Ouathek Ouerfelli, Sabine Ehrt, Carl F. Nathan, Julien Vaubourgeix
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2017
Materias:	cell division infectious diseases microbiology mycobacteria peptidoglycan tuberculosis Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/fa96f2621a094f4e9df20bec19046749
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spelling	oai:doaj.org-article:fa96f2621a094f4e9df20bec190467492021-11-15T15:51:50ZDistinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>10.1128/mBio.01183-172150-7511https://doaj.org/article/fa96f2621a094f4e9df20bec190467492017-11-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01183-17https://doaj.org/toc/2150-7511ABSTRACT Peptidoglycan (PG), a polymer cross-linked by d-amino acid-containing peptides, is an essential component of the bacterial cell wall. We found that a fluorescent d-alanine analog (FDAA) incorporates chiefly at one of the two poles in Mycobacterium smegmatis but that polar dominance varies as a function of the cell cycle in Mycobacterium tuberculosis: immediately after cytokinesis, FDAAs are incorporated chiefly at one of the two poles, but just before cytokinesis, FDAAs are incorporated comparably at both. These observations suggest that mycobacterial PG-synthesizing enzymes are localized in functional compartments at the poles and septum and that the capacity for PG synthesis matures at the new pole in M. tuberculosis. Deeper knowledge of the biology of mycobacterial PG synthesis may help in discovering drugs that disable previously unappreciated steps in the process. IMPORTANCE People are dying all over the world because of the rise of antimicrobial resistance to medicines that could previously treat bacterial infections, including tuberculosis. Here, we used fluorescent d-alanine analogs (FDAAs) that incorporate into peptidoglycan (PG)—the synthesis of which is an attractive drug target—combined with high- and super-resolution microscopy to investigate the spatiotemporal dynamics of PG synthesis in M. smegmatis and M. tuberculosis. FDAA incorporation predominates at one of the two poles in M. smegmatis. In contrast, while FDAA incorporation into M. tuberculosis is also polar, there are striking variations in polar dominance as a function of the cell cycle. This suggests that enzymes involved in PG synthesis are localized in functional compartments in mycobacteria and that M. tuberculosis possesses a mechanism for maturation of the capacity for PG synthesis at the new pole. This may help in discovering drugs that cripple previously unappreciated steps in the process.Helene BotellaGuangli YangOuathek OuerfelliSabine EhrtCarl F. NathanJulien VaubourgeixAmerican Society for Microbiologyarticlecell divisioninfectious diseasesmicrobiologymycobacteriapeptidoglycantuberculosisMicrobiologyQR1-502ENmBio, Vol 8, Iss 5 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	cell division infectious diseases microbiology mycobacteria peptidoglycan tuberculosis Microbiology QR1-502
spellingShingle	cell division infectious diseases microbiology mycobacteria peptidoglycan tuberculosis Microbiology QR1-502 Helene Botella Guangli Yang Ouathek Ouerfelli Sabine Ehrt Carl F. Nathan Julien Vaubourgeix Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
description	ABSTRACT Peptidoglycan (PG), a polymer cross-linked by d-amino acid-containing peptides, is an essential component of the bacterial cell wall. We found that a fluorescent d-alanine analog (FDAA) incorporates chiefly at one of the two poles in Mycobacterium smegmatis but that polar dominance varies as a function of the cell cycle in Mycobacterium tuberculosis: immediately after cytokinesis, FDAAs are incorporated chiefly at one of the two poles, but just before cytokinesis, FDAAs are incorporated comparably at both. These observations suggest that mycobacterial PG-synthesizing enzymes are localized in functional compartments at the poles and septum and that the capacity for PG synthesis matures at the new pole in M. tuberculosis. Deeper knowledge of the biology of mycobacterial PG synthesis may help in discovering drugs that disable previously unappreciated steps in the process. IMPORTANCE People are dying all over the world because of the rise of antimicrobial resistance to medicines that could previously treat bacterial infections, including tuberculosis. Here, we used fluorescent d-alanine analogs (FDAAs) that incorporate into peptidoglycan (PG)—the synthesis of which is an attractive drug target—combined with high- and super-resolution microscopy to investigate the spatiotemporal dynamics of PG synthesis in M. smegmatis and M. tuberculosis. FDAA incorporation predominates at one of the two poles in M. smegmatis. In contrast, while FDAA incorporation into M. tuberculosis is also polar, there are striking variations in polar dominance as a function of the cell cycle. This suggests that enzymes involved in PG synthesis are localized in functional compartments in mycobacteria and that M. tuberculosis possesses a mechanism for maturation of the capacity for PG synthesis at the new pole. This may help in discovering drugs that cripple previously unappreciated steps in the process.
format	article
author	Helene Botella Guangli Yang Ouathek Ouerfelli Sabine Ehrt Carl F. Nathan Julien Vaubourgeix
author_facet	Helene Botella Guangli Yang Ouathek Ouerfelli Sabine Ehrt Carl F. Nathan Julien Vaubourgeix
author_sort	Helene Botella
title	Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
title_short	Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
title_full	Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
title_fullStr	Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
title_full_unstemmed	Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>
title_sort	distinct spatiotemporal dynamics of peptidoglycan synthesis between <italic toggle="yes">mycobacterium smegmatis</italic> and <italic toggle="yes">mycobacterium tuberculosis</italic>
publisher	American Society for Microbiology
publishDate	2017
url	https://doaj.org/article/fa96f2621a094f4e9df20bec19046749
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Distinct Spatiotemporal Dynamics of Peptidoglycan Synthesis between <italic toggle="yes">Mycobacterium smegmatis</italic> and <italic toggle="yes">Mycobacterium tuberculosis</italic>

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