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American Journal of Respiratory Cell and Molecular Biology. Vol. 28, pp. 528-537, 2003
© 2003 American Thoracic Society
DOI: 10.1165/rcmb.2002-0141OC

Pseudomonas aeruginosa Elastase Degrades Surfactant Proteins A and D

William I. Mariencheck*, John F. Alcorn*, Scott M. Palmer and Jo Rae Wright

Departments of Medicine and Cell Biology, Duke University Medical Center, Durham, North Carolina

Address correspondence to: Jo Rae Wright, Ph.D., Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710. E-mail: J.Wright{at}cellbio.duke.edu

Both in vitro and in vivo studies provide evidence that surfactant protein (SP)-A and SP-D have an important role in the innate immune response to Pseudomonas aeruginosa. In preliminary experiments characterizing the binding of SP-A to this bacteria, we observed the appearance of apparent degradation products of SP-A, and therefore we hypothesized that P. aeruginosa produces an enzyme that degrades SP-A. Incubation of SP-A with P. aeruginosa organisms from several clinical isolates resulted in concentration- and temperature-dependent degradation of SP-A that was inhibited by a metalloproteinase inhibitor, phosphoramidon. The degradative enzyme was purified by anion exchange chromatography and identified by ion trap mass spectroscopy as Pseudomonas elastase, which was shown to directly degrade SP-A and SP-D. Incubation of P. aeruginosa or purified elastase with cell-free bronchoalveolar lavage (BAL) resulted in degradation of SP-A. Furthermore, SP-A degradation fragments were detectable in BAL from lung transplant patients with cystic fibrosis. We speculate that degradation of SP-A and SP-D is a virulence mechanism in the pathogenesis of chronic P. aeruginosa infection.

Abbreviations: bronchoalveolar lavage, BAL • cystic fibrosis, CF • colony-forming units, cfu • collagenase-resistant fragment, CRF • high-performance liquid chromatography, HPLC • surfactant protein, SP • Tris-buffered saline, TBS




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