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A Phosphoglycolate Phosphatase Virulence Factor From Staphylococcus aureus
Author(s) -
Moreno Isreal,
O'Handley Suzanne F
Publication year - 2016
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.30.1_supplement.606.3
Subject(s) - virulence , staphylococcus aureus , virulence factor , isomerase , biology , biochemistry , enzyme , microbiology and biotechnology , phosphatase , gene , bacteria , genetics
Staphylococcus aureus is a major cause of hospital‐acquired infections. 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 from E. coli , a member of the nitrophenyl phosphatase family of the HAD (Haloacid Dehalogenase) superfamily. We cloned the gene, expressed and purified the protein, and determined its activity. This virulence factor is not an ortholog of NagD UMPase from E. coli , but rather a phosphoglycolate phosphatase (PGPase). If phosphoglycolate accumulates in the cell, it will inhibit the glycolytic enzyme triose phosphate isomerase (TPI). In S. aureus , TPI also serves as an adhesion molecule that can bind to host cells via sugar‐side chains; phosphoglycolate would interfere with this adhesion process and thus make it harder for S. aureus to infect a new host cell. Thus, this S. aureus PGPase may act as a virulence factor by degrading the TPI inhibitor phosphoglycolate. We have subcloned this PGPase into a His‐tag vector, purified the protein using nickel affinity and size exclusion chromatography, and have characterized the enzyme's enzymatic activity, optimal conditions, and kinetics. Support or Funding Information Supported by NIH AREA grant GM066715 and RIT Graduate Student Research Grant