Pseudomonas aeruginosa elastase and elastolysis revisited: recent developments

Authors

  • D. R. Galloway

    Corresponding author
    1. Department of Microbiology, Ohio State University, 484 West 12th Avenue, Columbus, Ohio 43210–1292, USA.
    • *For correspondence. Tel. (614) 2923761; Fax (614) 292 1538.

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Summary

With the determination of the three-dimensional structure of elastase and the probable identification of the active site and key residues involved in proteolytic activity, our knowledge of the molecular details of this interesting protease is rapidly increasing. Pseudomonas elastase appears to be remarkably similar to the Bacillus metalloproteinase thermolysin. A further significant development has been the discovery of the lasA gene and the fact that Pseudomonas elastase and alkaline proteinase appear to act in concert with the LasA protein to display the notable elastolytic activity exhibited by isolates of this organism. Biochemical and genetic studies indicate that LasA is a second elastase which may be an important virulence factor that has been overlooked in previous studies.

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