Cargando…

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Moynihan, Patrick J., Cadby, Ian T., Veerapen, Natacha, Jankute, Monika, Crosatti, Marialuisa, Mukamolova, Galina V., Lovering, Andrew L., Besra, Gurdyal S.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
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
_version_ 1783427721238413312
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
work_keys_str_mv AT moynihanpatrickj thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT cadbyiant thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT veerapennatacha thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT jankutemonika thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT crosattimarialuisa thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT mukamolovagalinav thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT loveringandrewl thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT besragurdyals thehydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT moynihanpatrickj hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT cadbyiant hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT veerapennatacha hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT jankutemonika hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT crosattimarialuisa hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT mukamolovagalinav hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT loveringandrewl hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling
AT besragurdyals hydrolaselpqiprimesmycobacterialpeptidoglycanrecycling