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Genetics and Molecular Biology |
Anti-Infective Research (UP1345), SmithKline Beecham Pharmaceuticals, 1250 South Collegeville Road, PO Box 5089, Collegeville, PA19426-0989, USA1
Author for correspondence: Alison F. Chalker. Tel: +1 610 917 6366. Fax: +1 610 917 7901. e-mail: Alison_F_Chalker{at}sbphrd.com
Homologues of Escherichia coli bacA, encoding extremely hydrophobic proteins, were identified in the genomes of Staphylococcus aureus and Streptococcus pneumoniae. Allelic replacement mutagenesis demonstrated that the gene is not essential for in vitro growth in either organism, and the mutants showed no significant changes in growth rate or morphology. The Staph. aureus bacA mutant showed slightly reduced virulence in a mouse model of infection and an eightfold increase in bacitracin susceptibility. However, a Strep. pneumoniae bacA mutant was highly attenuated in a mouse model of infection, and demonstrated an increase in susceptibility to bacitracin of up to 160000-fold. These observations are consistent with the previously proposed role of BacA protein as undecaprenol kinase.
Keywords: bacitracin, bacA, undecaprenol kinase, Staphylococcus aureus, Streptococcus pneumoniae
Abbreviations: PN, pyelonephritis; RTI, respiratory tract infection; UP, undecaprenol monophosphate; UPP, undecaprenol pyrophosphate
The GenBank accession number for the sequence reported in this paper is AF228662.
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