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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, Vol. 277, No. 13, 13, 2002, p. 11042-11049.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Windhorst, S, Frank, E, Georgieva, DN, Genov, N, Buck, F, Borowski, P & Weber, W 2002, 'The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene.', J BIOL CHEM, vol. 277, no. 13, 13, pp. 11042-11049. <http://www.ncbi.nlm.nih.gov/pubmed/11796713?dopt=Citation>

APA

Windhorst, S., Frank, E., Georgieva, D. N., Genov, N., Buck, F., Borowski, P., & Weber, W. (2002). The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene. J BIOL CHEM, 277(13), 11042-11049. [13]. http://www.ncbi.nlm.nih.gov/pubmed/11796713?dopt=Citation

Vancouver

Windhorst S, Frank E, Georgieva DN, Genov N, Buck F, Borowski P et al. The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene. J BIOL CHEM. 2002;277(13):11042-11049. 13.

Bibtex

@article{ec9bbb13929044d5864879639333cc02,
title = "The major extracellular protease of the nosocomial pathogen Stenotrophomonas maltophilia: characterization of the protein and molecular cloning of the gene.",
abstract = "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.",
keywords = "Humans, Amino Acid Sequence, Molecular Sequence Data, Base Sequence, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular, Hydrolysis, Oxidation-Reduction, Cross Infection/*microbiology, Insulin/chemistry/metabolism, Serine Endopeptidases/chemistry/genetics/isolation & purification/*metabolism, Stenotrophomonas maltophilia/*enzymology/pathogenicity, Humans, Amino Acid Sequence, Molecular Sequence Data, Base Sequence, Electrophoresis, Polyacrylamide Gel, Cloning, Molecular, Hydrolysis, Oxidation-Reduction, Cross Infection/*microbiology, Insulin/chemistry/metabolism, Serine Endopeptidases/chemistry/genetics/isolation & purification/*metabolism, Stenotrophomonas maltophilia/*enzymology/pathogenicity",
author = "Sabine Windhorst and Eva Frank and Georgieva, {Dessislava N} and Nicolay Genov and Fritz Buck and Peter Borowski and Wolfgang Weber",
year = "2002",
language = "English",
volume = "277",
pages = "11042--11049",
journal = "J BIOL CHEM",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "13",

}

RIS

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 -