The Effect of Oxidative Stress on Proteomics of Listeria monocytogenes PTCC 1297

Listeria monocytogenes is a ubiquitous Gram-positive food-borne human bacterial pathogen that can cause listeriosis. This disease is a fatal with a high rate of hospitalization (>90%). The aim of this study is to determine the effect of hydrogen peroxide (H2O2) on L. monocytogenes PTCC 1297 proteomics. Bacterial cells exposed to gradually increasing sub-lethal concentrations of oxidative stress: 0.06, 0.3, 0.6, and 1.5 % of H2O2. Changes in protein profile of cells exposed to H2O2 and control (non-adapted cells) were determined by isoelectric focusing (IEF) and sodium dodecyl sulfate–polyacrylamide gel electrophoresis (SDS-PAGE). Protein spots visualized by staining with colloidal Coomassie Brilliant Blue. Based on the obtained results, one thousand four hundred spots identified on the gels. Out of these points, 85 spots were reproducibly detected with the help of software and eye confirmation. After analyzing these points, 9 spots showed the most significant changes. These points had appropriate density and indicate the response of bacteria to stress conditions. It can be concluded that the structure of proteome of L. monocytogenes PTCC 1297 changes when faced with oxidative stress. Nine protein spots on the gel were found to have substantial variations after protein spot analysis. These sites show how bacteria react under stress. Some of these spots' expressions had increased, while others had decreased.