Abstract
Methicillin Resistant Staphylococcus aureus (MRSA) is the bacteria responsible for staph infections; one of the most prevalent hospital acquired infections. Since its initial discovery, Staphylococcus aureus (S. aureus) has developed multidrug resistance making infection extremely difficult to treat. One avenue of pursuit in identifying new drug targets against staph infections might be found through the study of Haloacid Dehalogenase (HAD) superfamily phosphatases. A HAD phosphatase in S. aureus has been shown to serve as both a virulence factor and possess the ability to dephosphorylate 2‐phosphoglycolate. If not catabolized, 2‐phosphoglycolate accumulates in cells and inhibits triose phosphate isomerase (TPI). In S. aureus, TPI also serves as an adhesion molecule that can bind to host cells via sugar‐side chains. To confirm physiologically that the S. aureus HAD phosphatase is indeed a phosphoglycolate phosphatase (PGPase), the enzyme will be expressed in a PGPase Saccharomyces cerevisiae knockout. We have identified a potential growth phenotype for this PGPase knockout in response to hyperosmotic (1M NaCl) shock compared to wild‐type cells. We hypothesize that the S. aureus PGPase should be able to complement this growth phenotype if it is a true functional ortholog. Studies are currently underway to clone the S. aureus PGPase into a yeast expression vector for subsequent complementation work. This research was supported by an NIH AREA grant, RIT McNair Scholars Program, and RIT NTID and COS FEAD grants.
Published Version
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