Lytic peptidase L5 of Lysobacter sp. XL1 with broad antimicrobial spectrum. 2014

Natalia V Vasilyeva, and Nina A Shishkova, and Leonid I Marinin, and Larisa A Ledova, and Irina M Tsfasman, and Tatyana A Muranova, and Olga A Stepnaya, and Igor S Kulaev
Laboratory of Microbial Cell Surface Biochemistry, G.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Russian Academy of Sciences, Pushchino/Moscow, Russia.

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.

UI MeSH Term Description Entries
D006090 Gram-Negative Bacteria Bacteria which lose crystal violet stain but are stained pink when treated by Gram's method. Gram Negative Bacteria
D006094 Gram-Positive Bacteria Bacteria which retain the crystal violet stain when treated by Gram's method. Gram Positive Bacteria
D000890 Anti-Infective Agents Substances that prevent infectious agents or organisms from spreading or kill infectious agents in order to prevent the spread of infection. Anti-Infective Agent,Anti-Microbial Agent,Antimicrobial Agent,Microbicide,Microbicides,Anti-Microbial Agents,Antiinfective Agents,Antimicrobial Agents,Agent, Anti-Infective,Agent, Anti-Microbial,Agent, Antimicrobial,Agents, Anti-Infective,Agents, Anti-Microbial,Agents, Antiinfective,Agents, Antimicrobial,Anti Infective Agent,Anti Infective Agents,Anti Microbial Agent,Anti Microbial Agents
D001433 Bacteriolysis Rupture of bacterial cells due to mechanical force, chemical action, or the lytic growth of BACTERIOPHAGES. Bacteriolyses
D013379 Substrate Specificity A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts. Specificities, Substrate,Specificity, Substrate,Substrate Specificities
D053528 Lysobacter A genus of gram-negative, rod-shaped, gliding bacteria in the family XANTHOMONADACEAE. Strongly proteolytic, it is involved in lysing a variety of microorganisms.
D055252 Cell-Derived Microparticles Extracellular vesicles generated by the shedding of CELL MEMBRANE blebs. Cell Membrane Microparticles,Circulating Cell-Derived Microparticles,Ectosomes,Microparticles, Cell-Derived,Shedding Microvesicles,Cell Derived Microparticles,Cell Membrane Microparticle,Cell-Derived Microparticle,Cell-Derived Microparticle, Circulating,Cell-Derived Microparticles, Circulating,Circulating Cell Derived Microparticles,Circulating Cell-Derived Microparticle,Ectosome,Membrane Microparticle, Cell,Membrane Microparticles, Cell,Microparticle, Cell Membrane,Microparticle, Cell-Derived,Microparticle, Circulating Cell-Derived,Microparticles, Cell Derived,Microparticles, Cell Membrane,Microparticles, Circulating Cell-Derived,Microvesicle, Shedding,Microvesicles, Shedding,Shedding Microvesicle
D057057 Serine Proteases Peptide hydrolases that contain at the active site a SERINE residue involved in catalysis. Serine Proteinases,Serine Protease,Serine Protein Hydrolases,Serine Proteinase,Protease, Serine,Proteases, Serine,Protein Hydrolases, Serine,Proteinase, Serine,Proteinases, Serine

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