Project description:Mycobacterium marinum is a pathogenic bacterium that causes infections in both fish and humans. The PE/PPE protein family is unique to mycobacteria and has been implicated in various aspects of mycobacterial pathogenicity. Understanding the presence and potential function of these proteins in M. marinum is essential for unraveling the mechanisms underlying its virulence. In this study, we conducted a proteomics analysis to investigate the secretion and potential role of the PE/PPE protein family in the culture filtrate of M. marinum. To investigate the presence of PE/PPE proteins in the culture filtrate, we employed a proteomics approach combining Asp-N and trypsin based digestion. Cultures of M. marinum were grown under laboratory conditions, and the culture filtrate was collected and subjected to digestion and LC-MS injection. Our proteomics analysis revealed the secretion of about half PE/PPE proteins in the culture filtrate of M. marinum. Majority of these proteins are confirmed to be involved in EspG5 interaction. The identification of these proteins in the culture filtrate suggests their secretion and potential role in M. marinum. Our proteomics analysis highlights the presence of PE/PPE proteins in the culture filtrate of M. marinum, suggesting their secretion and potential involvement in the pathogenicity of this bacterium.
Project description:In this study we investigate the molecular physiology of the main S. cerevisiae commercial strain (PE-2) used on Brazilian bioethanol process under two distinct conditions: typical (TF) and flocculated (co-aggregated - FL) fermentation. Transcriptional machinery of PE-2 was assessed by high throughput sequencing-based methods (RNA-seq) during industrial fed-batch fermentations. Data from comparative analysis revealed distinct transcriptional profiles among conditions, characterized mainly by a deep gene repression on FL process.
Project description:We observed through Western blot that Mycobacterium marinum secreted more highly abundant PE-PGRS proteins that are above 130 kDa when treated with compound 36 than mock-treated bacteria. We would like to explore which PE-PGRS proteins are more secreted in this condition and whether other proteins are also differentially secreted between two conditions.
