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NAGD UMPase from Escherichia coli and virulence factor “NAGD” phosphoglycolate phosphatase from Staphylococcus aureus, two distinct members of the nitrophenyl phosphatase family of the HAD superfamily
Author(s) -
Hill Jacqueline,
Leiker Teressa,
Sitterly Amanda,
Tirrell Isaac,
Nguyen Ahn Tram,
Mentz Robert,
Slivka Eric
Publication year - 2007
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.21.6.a1001-b
Subject(s) - virulence , escherichia coli , virulence factor , staphylococcus aureus , biology , microbiology and biotechnology , phosphatase , gene , bacteria , enzyme , biochemistry , genetics
NAGD from E. coli is a novel UMPase of the HAD superfamily, a ubiquitous superfamily with a wide variety of hydrolases especially phosphatases. NAGD is the first UMPase of this superfamily, and may be involved in cell surface lipopolysaccharide (LPS) and cell wall biosynthesis through hydrolysis of UMP, an intermediate of both pathways. There are NAGD homologs in a number of pathogens including Salmonella and Yersinia pestis, thus making NAGD a potential antibiotic target. Staphylococcus aureus is a major cause of hospital acquired infection. Multi‐drug resistant S. aureus makes finding new drug targets vital. A new virulence factor from S. aureus was recently 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, but rather a phosphoglycolate phosphatase. Recently, 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. Supported by an NIH AREA grant.