1. Generation and characterization of thiol-deficient Mycobacterium tuberculosis mutants.
- Author
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Sao Emani C, Williams MJ, Van Helden PD, Taylor MJC, Carolis C, Wiid IJ, and Baker B
- Subjects
- Bacterial Proteins chemistry, Bacterial Proteins genetics, Mutation, Oxidative Stress genetics, Sulfhydryl Compounds, Cysteine deficiency, Cysteine genetics, Dipeptides deficiency, Dipeptides genetics, Ergothioneine deficiency, Ergothioneine genetics, Glycopeptides deficiency, Glycopeptides genetics, Inositol deficiency, Inositol genetics, Mycobacterium tuberculosis chemistry, Mycobacterium tuberculosis genetics, Mycobacterium tuberculosis isolation & purification
- Abstract
Mycothiol (MSH) and ergothioneine (ERG) are thiols able to compensate for each other to protect mycobacteria 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. High throughput screening (HTS) of off-patent drugs and natural compounds revealed few compounds that displayed a higher activity against the thiol-deficient mutants relative to the wild-type strain. The mode of action of these drugs was further investigated. Raw data displaying these results are described here.
- Published
- 2018
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