Generation and characterization of thiol-deficient Mycobacterium tuberculosis mutants

Mycothiol (MSH) and ergothioneine (ERG) are thiols able to compensate for each other to protect mycobacteria such as Mycobacterium smegmatis against oxidative stress. Gamma-glutamylcysteine (GGC), another thiol and an intermediate in ERG biosynthesis has detoxification abilities. Five enzymes are involved in ERG biosynthesis, namely EgtA, EgtB, EgtC, EgtD and EgtE. The role of these enzymes in the production of ERG had been unclear. On the other hand, the enzyme MshA is known to be essential for MSH biosynthesis. In this manuscript, we describe the raw data of the generation and characterization of Mycobacterium tuberculosis (M.tb) mutants harbouring a deletion of the gene coding for each of these enzymes, and the raw data of the phenotypic characterization of the obtained thiol-deficient M.tb mutants. Through a high throughput screening approach, compounds not previously used in a tuberculosis (TB) regimen were identified. Raw data depicting the effect of these compounds on the generated thiol-deficient M.tb mutants, on the production of reactive oxygen species (ROS) and thiols in the M.tb wild type strain are described in this study.