Growth phase-dependent production of a cell wall-associated elastinolytic cysteine proteinase by Staphylococcus epidermidis
| Autor: | Grzegorz Szmyd, Jonathan L. Moon, Agnieszka Banbula, Timothy J. Foster, Malgorzata Kubica, Ewa Golonka, Aneta Oleksy, Doron C. Greenbaum, Matthew Bogyo, James Travis, Jan Potempa |
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| Rok vydání: | 2004 |
| Předmět: |
Proteases
medicine.medical_treatment Clinical Biochemistry Molecular Sequence Data Virulence Cysteine Proteinase Inhibitors medicine.disease_cause Biochemistry Microbiology Substrate Specificity Bacterial Proteins Staphylococcus epidermidis Cell Wall Enzyme Stability medicine Staphopain Humans Amino Acid Sequence Molecular Biology Protease biology Sequence Homology Amino Acid Proteolytic enzymes Hydrogen-Ion Concentration biology.organism_classification Cysteine protease Elastin Cysteine Endopeptidases Staphylococcus aureus Reducing Agents |
| Zdroj: | Biological chemistry. 385(6) |
| ISSN: | 1431-6730 |
| Popis: | Staphylococcus epidermidis, a Gram-positive, coagu- lase-negative bacterium is a predominant inhabitant of human skin and mucous membranes. Recently, however, it has become one of the most important agents of hos- pital-acquired bacteriemia, as it has been found to be responsible for surgical wound infections developed in individuals with indwelling catheters or prosthetic devices, as well as in immunosupressed or neutropenic patients. Despite their medical significance, little is known about proteolytic enzymes of S. epidermidis and their possible contribution to the bacterium's pathoge- nicity; however, it is likely that they function as virulence factors in a manner similar to that proposed for the pro- teases of Staphylococcus aureus. Here we describe the purification of a cell wall-associated cysteine protease from S. epidermidis, its biochemical properties and spec- ificity. A homology search using N-terminal sequence data revealed similarity to staphopain A (ScpA) and sta- phopain B (SspB), cysteine proteases from S. aureus. Moreover, the gene encoding S. epidermidis cysteine protease (Ecp) and a downstream gene coding for a putative inhibitor of the protease form an operon struc- ture which resembles that of staphopain A in S. aureus. The active cysteine protease was detected on the bac- terial cell surface as well as in the culture media and is apparently produced in a growth phase-dependent man- ner, with initial expression occurring in the mid-logarith- mic phase. This enzyme, with elastinolytic properties, as well as the ability to cleave a1PI, fibrinogen and fibro- nectin, may possibly contribute to the invasiveness and pathogenic potential of S. epidermidis. |
| Databáze: | OpenAIRE |
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