Publication

Article Metrics

Citations


Online attention

The hydrolase LpqI primes mycobacterial peptidoglycan recycling

DOI: 10.1038/s41467-019-10586-2 DOI Help

Authors: 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)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 10 , PAGES 2647

State: Published (Approved)
Published: June 2019
Diamond Proposal Number(s): 14692

Open Access Open Access

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.

Journal Keywords: Amino sugars; Bacteria; Hydrolases; Pathogens

Subject Areas: Biology and Bio-materials, Medicine


Instruments: I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Documents:
s41467-019-10586-2.pdf