A Proteomic Approach to Assessment of Bacterial MTN as an Antibiotic Target
The significance of bacterial 5’-methylthioadenosine nucleosidase (MTN) as an antibiotic target may be deciphered through the analysis and comparison of the proteomic data from wild-type (WT) and MTN gene-knockout (KO) E. coli samples. The MTN gene encodes an enzyme present only in prokaryotic organisms that hydrolizes 5’-methylthioadenosine (MTA), S-adenosylhomocysteine (SAH), and 5’deoxyadenosine (5’-dADO) to adenine and the corresponding sugar. These reactions are vital to several metabolic pathways within a large majority of pathogenic bacteria species. Proteomic comparison of the WT versus KO strains revealed a number of important differences that suggest how antibiotics inhibiting bacterial MTN might work. These include significant changes to methionine salvage enzyme expression, polyamine synthesis, and other pathways; and suggest new antibiotic possibilities. The final goal of this research is to develop a broad-spectrum antimicrobial treatment that would be more effective than current drug therapies, especially in the face of growing antibiotic resistance.