The hydrolase LpqI primes mycobacterial peptidoglycan recycling

Research output: Contribution to journalArticle

Colleges, School and Institutes

External organisations

  • Leicester Tuberculosis Research group, Department of Respiratory Sciences, University of Leicester, Leicester, LE1 9HN, UK.

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.

Details

Original languageEnglish
Article number2647
JournalNature Communications
Volume10
Issue number1
Publication statusPublished - 14 Jun 2019