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Lysophosphatidic acid inhibition of the accumulation of Pseudomonas aeruginosa PAO1 alginate, pyoverdin, elastase and LasA

Department of Cell and Molecular Biology, University of Rhode Island, Kingston, RI 02881, USA¹
Biocentrum, Bldg 301, Technical University of Denmark, DK-2800 Lyngby, Denmark²
Department of Pathology and Laboratory Medicine, Medical University of South Carolina, Charleston, SC 29425, USA³
Department of Gastrointestinal Infections, Statens Serum Institut, DK 2300 Copenhagen, Denmark⁴
Department of Microbiology, University of Virginia, Health Sciences Center, Charlottesville, VA 22908, USA⁵

Author for correspondence: Paul S. Cohen. Tel: +1 401 874 5920. Fax: +1 401 874 2202. e-mail: pco1697u{at}postoffice.uri.edu

The pathogenesis of Pseudomonas aeruginosa is at least partially attributable to its ability to synthesize and secrete the siderophore pyoverdin and the two zinc metalloproteases elastase and LasA, and its ability to form biofilms in which bacterial cells are embedded in an alginate matrix. In the present study, a lysophospholipid, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphate [also called monopalmitoylphosphatidic acid (MPPA)], which accumulates in inflammatory exudates, was shown to inhibit the extracellular accumulation of P. aeruginosa PAO1 alginate, elastase, LasA protease and the siderophore pyoverdin. MPPA also inhibited biofilm formation. The inhibitory effects of MPPA occur independently of rpoS expression and without affecting the accumulation of the autoinducers N-(3-oxododecanoyl) homoserine lactone and N-butyryl-L-homoserine lactone, and may be due, at least in part, to the ability of MPPA to bind divalent cations.

Keywords: monopalmitoylphosphatidic acid, cystic fibrosis

Abbreviations: BHL, N-butanoyl homoserine lactone; GFP, green fluorescent protein; LB, Luria broth; LPS, lipopolysaccharide; MPPA, 1-palmitoyl-2-hydroxy-sn-glycero-3-phosphate (also known as monopalmitoylphosphatidic acid); OdDHL, N-(3-oxododecanoyl) homoserine lactone

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