1 research outputs found
The hydrolase LpqI primes mycobacterial peptidoglycan recycling
Growth and division by most bacteria requires remodeling 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, respecticely.
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-N31 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 peptidoglyca