Lytic Peptidase L5 of Lysobacter sp. XL1 with Broad Antimicrobial Spectrum
| Autor: | Tatyana A. Muranova, Natalia V. Vasilyeva, Leonid Ivanovicn Marinin, Igor S. Kulaev, Larisa A. Ledova, Nina A. Shishkova, I. M. Tsfasman, O. A. Stepnaya |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Serine protease biology Physiology Vesicle Cell Biology Erwinia biology.organism_classification Applied Microbiology and Biotechnology Biochemistry Microbiology Enzyme chemistry Lytic cycle Extracellular biology.protein Bacterial outer membrane Bacteria Biotechnology |
| Zdroj: | Microbial Physiology. 24:59-66 |
| ISSN: | 2673-1673 2673-1665 |
| Popis: | The Gram-negative bacterium Lysobacter sp. XL1 secretes lytic enzymes (L1-L5) into the culture medium. Enzyme L5 is the most recently found extracellular lytic enzyme of this bacterium. The paper presents the results of the isolation and characterization of some properties of this enzyme. Thus, enzyme L5 of Lysobacter sp. XL1 is a lytic serine protease. Earlier, the enzyme was shown to be secreted into the culture medium by means of outer membrane vesicles, which possess a lytic effect towards living cells of Erwinia caratovora B15 [Vasilyeva et al., FEBS J 2008;15:3827-3835]. This work shows the action of enzyme L5 either as a vesicle component or the homogeneous enzyme L5 on a broad range of Gram-positive and Gram-negative microorganisms. Moreover, the vesicles containing this enzyme were shown to lyze the selected test cultures more efficiently than the soluble enzyme L5. It appears to be one of the first precedents of a bacteriolytic effect mediated by the action of outer membrane vesicles filled with extracellular lytic enzymes. The results suggest that the enzyme L5 of Lysobacter sp. XL1 and the vesicles containing this enzyme can be used as an antimicrobial drug. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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