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J. Biol. Chem., Vol. 277, Issue 13, 11042-11049, March 29, 2002

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The Major Extracellular Protease of the Nosocomial Pathogen Stenotrophomonas maltophilia
CHARACTERIZATION OF THE PROTEIN AND MOLECULAR CLONING OF THE GENE^*

Sabine Windhorst, Eva Frank, Dessislava N. Georgieva, Nicolay Genov^¶, Fritz Buck^§, Peter Borowski, and Wolfgang Weber^**

From the Universitätsklinikum Hamburg-Eppendorf, D-20246 Hamburg, Germany,  Institut für Medizinische Biochemie und Molekularbiologie and ^§ Institut für Zellbiochemie und Klinische Neurobiologie

Stenotrophomonas maltophilia is increasingly emerging as a multiresistant pathogen in the hospital environment. In immunosuppressed patients, these bacteria may cause severe infections associated with tissue lesions such as pulmonary hemorrhage. This suggests proteolysis as a possible pathogenic mechanism in these infections. This study describes a protease with broad specificity secreted by S. maltophilia. The gene, termed StmPr1, codes for a 63-kDa precursor that is processed to the mature protein of 47 kDa. The enzyme is an alkaline serine protease that, by sequence homology and enzymic properties, can be further classified as a new member of the family of subtilases. It differs from the classic subtilisins in molecular size, in substrate specificity, and probably in the architecture of the active site. The StmPr1 protease is able to degrade several human proteins from serum and connective tissue. Furthermore, pan-protease inhibitors such as ₁-antitrypsin and ₂-macroglobulin were unable to abolish the activity of the bacterial protease. The data support the interpretation that the extracellular protease of S. maltophilia functions as a pathogenic factor and thus could serve as a target for the development of therapeutic agents.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s) AJ291488.

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