Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 101, Issue 7, Pages 2135-2139Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0307308101
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Funding
- NCI NIH HHS [N01-CO-56000] Funding Source: Medline
- NIAID NIH HHS [R01 AI026289] Funding Source: Medline
- NIDCR NIH HHS [P01 DE013499, P01-DE13499] Funding Source: Medline
- NIDDK NIH HHS [DK60583, K01 DK060583-04] Funding Source: Medline
- NIGMS NIH HHS [GM38765, R01 GM038765, R37 GM038765] Funding Source: Medline
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In mammals, lipoxygenases play key roles in inflammation by initiating the transformation of arachidonic acid into potent bioactive lipid mediators such as leukotrienes and lipoxins. In general, most bacteria are believed to lack lipoxygenases and their polyunsaturated fatty acid substrates. It is therefore of interest that an ORF (PA1169) with high homology to eukaryotic lipoxygenases was discovered by analysis of the whole-genome sequence of the opportunistic bacterial pathogen Pseudomonas aeruginosa. Using TLC and liquid chromatography-UV-tandem mass spectrometry (LC-UV-MS-MS), we demonstrate that PA1169 encodes a bacterial lipoxygenase (LoxA) that converts arachidonic acid into 15-hydroxyeicosatetraenoic acid (15-HETE). Although mammalian Iipoxygenases are cytoplasmic enzymes, A aeruginosa LoxA activity is secreted. Taken together, these results suggest a mechanism by which a pathogen-secreted lipoxygenase may modulate host defense and inflammation via alteration of the biosynthesis of local chemical mediators.
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