Bacterial proteins with thiol groups

Bacterial proteins with thiol groups represent a broad and essential class of therapeutic targets for various antimicrobial agents, including heavy metals, reactive sulfur species, and certain natural products. Thiol groups (-SH), located on cysteine residues, are vital for the catalytic function of numerous enzymes, the structural stability of proteins via disulfide bridges, and the maintenance of cellular redox balance (NIH, 2018). Drugs such as silver ions (e.g., silver nitrate) and organomercurials (e.g., thimerosal) exert their bactericidal effects by binding covalently to these sulfhydryl groups, causing protein denaturation and systemic metabolic failure within the bacterial cell (Goodman & Gilman, 2018). This multi-target approach is highly effective against a wide range of pathogens and significantly reduces the likelihood of resistance development compared to single-target antibiotics. However, the presence of similar thiol groups in human proteins often limits the use of these agents to topical applications or environmental disinfection due to the risk of host toxicity. Understanding the interaction between drugs and the bacterial thiol proteome remains a key area for developing novel redox-based antimicrobial therapies (ResearchGate, 2022).

Other names

Bacterial sulfhydryl-containing proteinsBacterial cysteine-containing proteinsBacterial thiol-dependent enzymesBacterial thiol proteome

Covalent modification of cysteine sulfhydryl groups, leading to enzyme inhibition, protein denaturation, and disruption of bacterial metabolism and redox balance.