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Pseudomonas aeruginosa is a gram-negative bacterium that is ubiquitous in our environment. The bacterium causes chronic infections, however, it is of particular burden in cystic fibrosis and chronic obstructive pulmonary disease patients and is a major source of wound, burn, and hospital-acquired infections. P. aeruginosa uses many virulence factors, biofilms, and increased antibiotic resistance to contribute to disease.
A number of P. aeruginosa enzymes use molybdenum cofactor (MoCo), including nitrate reductase important for anaerobic growth and biofilm development. P. aeruginosa mutants unable to make MoCo have diminished biofilm development and reduced virulence in assays such as the Caenorhabditis elegans fast-kill assay, lettuce leaf model, and burned mouse model compared to the wild-type (Filiatrault et al. 2013. PLoS ONE. 8(2): e55594). Production of MoCo relies on a series of proteins to construct, assemble, and chaperone the cofactor to its conjugate enzymes.
Currently in my lab, we are investigating the cellular localization of the proteins involved in MoCo biosynthesis via bacterial mutant construction and a green fluorescent protein (GFP) fragment complementation assay to determine protein interactions. Students will have the opportunity to learn techniques such as bacterial culturing, basic bioinformatic analysis, PCR, general cloning methods, and fluorescence/confocal microscopy. In addition, we are also investigating P. aeruginosa mutants in different infection models to determine proteins involved in virulence or disease.