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B and Activator Protein-21
*
Department of Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Rochester, NY 14642;
The Center for Blood Research and Department of Pathology, Harvard Medical School, Boston, MA 02115;
Department of Molecular Oncology, Cancer Research Institute, Kanazawa University, Kanazawa, Japan; and
Cancer Center, University of Rochester, Rochester, NY 14642
The destructive pulmonary inflammation associated with
Pseudomonas aeruginosa colonization is caused, in part,
by the production of the chemokine IL-8, which recruits neutrophils
into the lung. The Pseudomonas autoinducer,
N-3-oxododecanoyl homoserine lactone (3-O-C12-HSL), is a
small lipid-soluble molecule that is essential in the regulation of
many P. aeruginosa virulence factors, but little is
known about how it affects eukaryotic cells. In this report we
demonstrate that 3-O-C12-HSL is a potent stimulator of both IL-8 mRNA
and protein from human fibroblasts and epithelial cells in vitro. The
IL-8 produced from these 3-O-C12-HSL-stimulated cells was found to be
functionally active by inducing the chemotaxis of neutrophils. To
determine a mechanism for this IL-8 induction, deletion constructs of
the IL-8 promoter were examined. It was found that the DNA region
between nucleotides -1481 and -546 and the transcription factor
NF-
B were essential for the maximal induction of IL-8 by
3-O-C12-HSL. This was confirmed by EMSAs, where 3-O-C12-HSL induced a
shift with both AP-2 and NF-B consensus DNA. The activation of
NF-B and subsequent production of IL-8 were found to be regulated by
a mitogen-activated protein kinase pathway. These findings support the
concept that the severe lung damage that accompanies P.
aeruginosa infections is caused by an exuberant neutrophil
response stimulated by 3-O-C12-HSL-induced IL-8. Understanding the
mechanisms of 3-O-C12-HSL activation of lung structural cells may
provide a means to help control lung damage during infections with
P. aeruginosa.
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