The success of Mycobacterium tuberculosis (Mtb) as a pathogen depends on
the redundant and complex mechanisms it has evolved for resisting
nitrosative and oxidative stresses inflicted by host immunity. Improving
our understanding of these defense pathways can reveal vulnerable
points in Mtb pathogenesis. In this study, we combined genetic, structural,
computational, biochemical, and biophysical approaches to identify
a novel enzyme class represented by Rv2466c. We show that Rv2466c
is a mycothiol-dependent nitroreductase of Mtb and can reduce the
nitro group of a novel mycobactericidal compound using mycothiol as
a cofactor. In addition to its function as a nitroreductase, Rv2466c
confers partial protection to menadione stress.
The alarming increase of antimicrobial-resistance urges rapid diagnosis and pathogen specific infection management. This work reports a rapid screening assay for pathogenic bacteria resistant to lactam antibiotics. We designed a...
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