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Enzymatic and Structural Characterization of a Phosphoglycolate Phosphatase Virulence Factor from Staphylococcus aureus
Author(s) -
Ramirez Sebastian,
Hill Jacqueline,
O'Handley Suzanne
Publication year - 2011
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.25.1_supplement.967.5
Subject(s) - virulence , staphylococcus aureus , virulence factor , microbiology and biotechnology , biology , phosphatase , gene , enzyme , biochemistry , bacteria , genetics
Staphylococcus aureus is a major cause of hospital acquired infection. The multi‐drug resistant nature of certain S. aureus strains makes the discovery of new S. aureus drug targets vital. A newly discovered virulence factor from S. aureus was described as a homolog of NAGD. We cloned the gene, expressed and purified the protein, and determined its activity. This virulence factor is not an ortholog of NAGD UMPase, but rather a phosphoglycolate phosphatase. A phosphoglycolate phosphatase from E. coli has been implicated with a role in DNA repair. If the S. aureus phosphoglycolate phosphatase is involved in both DNA repair and virulence, this would be a novel type of virulence factor, and a potential novel antibiotic target. We have subcloned this PGPase into a His‐tag vector and purified the protein using nickel affinity and size exclusion chromatography. We are currently screening crystals for use in determining the xray crystal structure.