The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene.
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The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene. / Windhorst, Sabine; Frank, Eva; Georgieva, Dessislava N; Genov, Nicolay; Buck, Fritz; Borowski, Peter; Weber, Wolfgang.
in: J BIOL CHEM, Jahrgang 277, Nr. 13, 13, 2002, S. 11042-11049.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene.
AU - Windhorst, Sabine
AU - Frank, Eva
AU - Georgieva, Dessislava N
AU - Genov, Nicolay
AU - Buck, Fritz
AU - Borowski, Peter
AU - Weber, Wolfgang
PY - 2002
Y1 - 2002
N2 - 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 alpha(1)-antitrypsin and alpha(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.
AB - 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 alpha(1)-antitrypsin and alpha(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.
KW - Humans
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Base Sequence
KW - Electrophoresis, Polyacrylamide Gel
KW - Cloning, Molecular
KW - Hydrolysis
KW - Oxidation-Reduction
KW - Cross Infection/microbiology
KW - Insulin/chemistry/metabolism
KW - Serine Endopeptidases/chemistry/genetics/isolation & purification/metabolism
KW - Stenotrophomonas maltophilia/enzymology/pathogenicity
KW - Humans
KW - Amino Acid Sequence
KW - Molecular Sequence Data
KW - Base Sequence
KW - Electrophoresis, Polyacrylamide Gel
KW - Cloning, Molecular
KW - Hydrolysis
KW - Oxidation-Reduction
KW - Cross Infection/microbiology
KW - Insulin/chemistry/metabolism
KW - Serine Endopeptidases/chemistry/genetics/isolation & purification/metabolism
KW - Stenotrophomonas maltophilia/enzymology/pathogenicity
M3 - SCORING: Journal article
VL - 277
SP - 11042
EP - 11049
JO - J BIOL CHEM
JF - J BIOL CHEM
SN - 0021-9258
IS - 13
M1 - 13
ER -