論文 - 詳細
| RRC ID | 27699 |
|---|---|
| 著者 | Sugimoto S, Iwamoto T, Takada K, Okuda K, Tajima A, Iwase T, Mizunoe Y. |
| タイトル | Staphylococcus epidermidis Esp degrades specific proteins associated with Staphylococcus aureus biofilm formation and host-pathogen interaction. |
| ジャーナル | J Bacteriol |
| Abstract |
Staphylococcus aureus exhibits a strong capacity to attach to abiotic or biotic surfaces and form biofilms, which lead to chronic infections. We have recently shown that Esp, a serine protease secreted by commensal Staphylococcus epidermidis, disassembles preformed biofilms of S. aureus and inhibits its colonization. Esp was expected to degrade protein determinants of the adhesive and cohesive strength of S. aureus biofilms. The aim of this study was to elucidate the substrate specificity and target proteins of Esp and thereby determine the mechanism by which Esp disassembles S. aureus biofilms. We used a mutant Esp protein (Esp(S235A)) with defective proteolytic activity; this protein did not disassemble the biofilm formed by a clinically isolated methicillin-resistant S. aureus (MRSA) strain, thereby indicating that the proteolytic activity of Esp is essential for biofilm disassembly. Esp degraded specific proteins in the biofilm matrix and cell wall fractions, in contrast to proteinase K, which is frequently used for testing biofilm robustness and showed no preference for proteolysis. Proteomic and immunological analyses showed that Esp degrades at least 75 proteins, including 11 biofilm formation- and colonization-associated proteins, such as the extracellular adherence protein, the extracellular matrix protein-binding protein, fibronectin-binding protein A, and protein A. In addition, Esp selectively degraded several human receptor proteins of S. aureus (e.g., fibronectin, fibrinogen, and vitronectin) that are involved in its colonization or infection. These results suggest that Esp inhibits S. aureus colonization and biofilm formation by degrading specific proteins that are crucial for biofilm construction and host-pathogen interaction. |
| 巻・号 | 195(8) |
| ページ | 1645-55 |
| 公開日 | 2013-4-1 |
| DOI | 10.1128/JB.01672-12 |
| PII | JB.01672-12 |
| PMID | 23316041 |
| PMC | PMC3624567 |
| MeSH | Bacterial Proteins / chemistry Bacterial Proteins / genetics Bacterial Proteins / metabolism* Biofilms / growth & development* Blood Proteins / chemistry Cell Wall Extracellular Matrix / chemistry Host-Pathogen Interactions Humans Membrane Proteins / metabolism Microscopy, Fluorescence Serine Proteases / chemistry Serine Proteases / genetics Serine Proteases / metabolism* Sodium Chloride Staphylococcus aureus / physiology* Staphylococcus aureus / ultrastructure Staphylococcus epidermidis / enzymology Staphylococcus epidermidis / genetics Staphylococcus epidermidis / metabolism* Substrate Specificity |
| IF | 3.006 |
| 引用数 | 93 |
| WOS 分野 | MICROBIOLOGY |
| オルトメトリクス指標 |
オルトメトリクス指標項目
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| 最多言及媒体 | Patent(IFI CLAIMS) |
| 各媒体での言及数の合計 | 16 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 一般微生物 | JCM 2874 |