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The hydrolase LpqI primes mycobacterial peptidoglycan recycling
Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan (PG) fragments known as muropeptides, which are recycled in many model organisms. Bacteria and hosts can harness the unique nature of muropep...
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/PMC6572805/ https://www.ncbi.nlm.nih.gov/pubmed/31201321 http://dx.doi.org/10.1038/s41467-019-10586-2 |
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author | Moynihan, Patrick J. Cadby, Ian T. Veerapen, Natacha Jankute, Monika Crosatti, Marialuisa Mukamolova, Galina V. Lovering, Andrew L. Besra, Gurdyal S. |
author_facet | Moynihan, Patrick J. Cadby, Ian T. Veerapen, Natacha Jankute, Monika Crosatti, Marialuisa Mukamolova, Galina V. Lovering, Andrew L. Besra, Gurdyal S. |
author_sort | Moynihan, Patrick J. |
collection | PubMed |
description | Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan (PG) fragments known as muropeptides, which are recycled in many model organisms. Bacteria and hosts can harness the unique nature of muropeptides as a signal for cell wall damage and infection, respectively. Despite this critical role for muropeptides, it has long been thought that pathogenic mycobacteria such as Mycobacterium tuberculosis do not recycle their PG. Herein we show that M. tuberculosis and Mycobacterium bovis BCG are able to recycle components of their PG. We demonstrate that the core mycobacterial gene lpqI, encodes an authentic NagZ β-N-acetylglucosaminidase and that it is essential for PG-derived amino sugar recycling via an unusual pathway. Together these data provide a critical first step in understanding how mycobacteria recycle their peptidoglycan. |
format | Online Article Text |
id | pubmed-6572805 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-65728052019-06-24 The hydrolase LpqI primes mycobacterial peptidoglycan recycling Moynihan, Patrick J. Cadby, Ian T. Veerapen, Natacha Jankute, Monika Crosatti, Marialuisa Mukamolova, Galina V. Lovering, Andrew L. Besra, Gurdyal S. Nat Commun Article Growth and division by most bacteria requires remodelling and cleavage of their cell wall. A byproduct of this process is the generation of free peptidoglycan (PG) fragments known as muropeptides, which are recycled in many model organisms. Bacteria and hosts can harness the unique nature of muropeptides as a signal for cell wall damage and infection, respectively. Despite this critical role for muropeptides, it has long been thought that pathogenic mycobacteria such as Mycobacterium tuberculosis do not recycle their PG. Herein we show that M. tuberculosis and Mycobacterium bovis BCG are able to recycle components of their PG. We demonstrate that the core mycobacterial gene lpqI, encodes an authentic NagZ β-N-acetylglucosaminidase and that it is essential for PG-derived amino sugar recycling via an unusual pathway. Together these data provide a critical first step in understanding how mycobacteria recycle their peptidoglycan. Nature Publishing Group UK 2019-06-14 /pmc/articles/PMC6572805/ /pubmed/31201321 http://dx.doi.org/10.1038/s41467-019-10586-2 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 Moynihan, Patrick J. Cadby, Ian T. Veerapen, Natacha Jankute, Monika Crosatti, Marialuisa Mukamolova, Galina V. Lovering, Andrew L. Besra, Gurdyal S. The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title | The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title_full | The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title_fullStr | The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title_full_unstemmed | The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title_short | The hydrolase LpqI primes mycobacterial peptidoglycan recycling |
title_sort | hydrolase lpqi primes mycobacterial peptidoglycan recycling |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6572805/ https://www.ncbi.nlm.nih.gov/pubmed/31201321 http://dx.doi.org/10.1038/s41467-019-10586-2 |
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