Bacterial thiol-containing molecules and enzymes (null)

Bacterial thiol-containing molecules and enzymes are essential components of the microbial antioxidant defense system and redox homeostasis (Newton et al., 2008, MMBR). This group encompasses low-molecular-weight (LMW) thiols—such as glutathione (GSH), mycothiol (MSH), and bacillithiol (BSH)—and the enzymes that maintain them, including thioredoxin reductase (TrxR) and glutaredoxins (Fahey, 2013, Free Radic Biol Med). These systems protect bacteria from oxidative damage caused by reactive oxygen species (ROS) generated during metabolism or by the host immune response during infection (Antelmann & Helmann, 2011, Antioxid Redox Signal). Because many of these pathways are distinct from human redox systems—for instance, the specific use of mycothiol in Actinobacteria or the structural differences in bacterial TrxR—they represent promising targets for novel antimicrobial therapies (Harbut et al., 2015, PNAS). Drugs like auranofin target these systems by inhibiting thioredoxin reductase, leading to a lethal accumulation of ROS and the collapse of the bacterial redox network (Thangamani et al., 2016, Sci Rep). Targeting these thiol-dependent pathways is particularly relevant for treating multi-drug resistant infections where traditional antibiotic mechanisms have failed.

Other names

Bacterial redox systemsLow-molecular-weight thiolsLMWTsBacterial thiol-dependent enzymesMycothiol systemBacillithiol system

Inhibition of thioredoxin reductase, depletion of low-molecular-weight thiols, covalent modification of cysteine residues, induction of oxidative stress