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J Biol Chem, Vol. 273, Issue 27, 16792-16797, July 3, 1998

Protease IV, a Unique Extracellular Protease and Virulence Factor from Pseudomonas aeruginosa

Lee S. Engel, James M. Hill^§, Armando R. Caballero, Linda C. Green^§, and Richard J. O'Callaghan^§

From the Departments of  Microbiology, Immunology, and Parasitology, and ^§ Ophthalmology, Louisiana State University Eye Center, Louisiana State University Medical Center, School of Medicine, New Orleans, Louisiana 70112

Comparisons of virulence between a Pseudomonas parent strain and an isogenic mutant devoid of protease IV have demonstrated a significant role for this enzyme during infection. We have characterized purified Pseudomonas aeruginosa protease IV in terms of its biochemical and enzymatic properties, and found it to be a unique extracellular protease. The N-terminal decapeptide sequence of protease IV is not homologous with any published protein sequence. Protease IV has a molecular mass of 26 kDa, an isoelectric point of 8.70, and optimum enzymatic activity at pH 10.0 and 45 °C. Purified protease IV demonstrates activity for the carboxyl side of lysine-containing peptides and can digest a number of biologically important proteins, including immunoglobulin, complement components, fibrinogen, and plasminogen. Protease IV is not inhibited by thiol-, carboxyl-, or metalloproteinase inhibitors. The total loss of enzyme activity in the presence of N-p-tosyl-L-chloromethyl ketone and the partial inhibition of enzyme activity by diisopropyl fluorophosphate or phenylmethylsulfonyl fluoride imply that protease IV is a serine protease. Inhibition by dithiothreitol and -mercaptoethanol suggests that intramolecular disulfide bonds are essential for enzyme activity. The characteristics of this enzyme suggest that inhibitors of serine proteases could be developed into a medication designed to arrest tissue damage during Pseudomonas infection.

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