The hydrolase LpqI primes mycobacterial peptidoglycan recycling

Patrick J. Moynihan (), Ian T. Cadby, Natacha Veerapen, Monika Jankute, Marialuisa Crosatti, Galina V. Mukamolova, Andrew L. Lovering and Gurdyal S. Besra
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Patrick J. Moynihan: University of Birmingham
Ian T. Cadby: University of Birmingham
Natacha Veerapen: University of Birmingham
Monika Jankute: University of Birmingham
Marialuisa Crosatti: University of Leicester
Galina V. Mukamolova: University of Leicester
Andrew L. Lovering: University of Birmingham
Gurdyal S. Besra: University of Birmingham

Nature Communications, 2019, vol. 10, issue 1, 1-11

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-10586-2

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