Recent recurrent outbreaks of bacterial resistance to antibiotics have shown the critical need to identify new lytic agents to combat them. The species Lysobacter capsici VKM B-2533T possesses a potent antimicrobial action against a number of bacteria, fungi and yeasts. Its activity can be due to the impact of bacteriolytic enzymes, antibiotics and peptides. This work isolated four homogeneous bacteriolytic enzymes and a mixture of two proteins, which also had a bacteriolytic activity. The isolates included proteins identical to L. enzymogenes α- and β-lytic proteases and lysine-specific protease. The proteases of 26 kDa and 29 kDa and a protein identified as N-acetylglycosaminidase had not been isolated in Lysobacter earlier. The isolated β-lytic protease digested live methicillin-resistant staphylococcal cells with high efficiency (minimal inhibitory concentration, 2.85 μg/mL). This property makes the enzyme deserving special attention. A recombinant β-lytic protease was produced. The antimicrobial potential of the bacterium was contributed to by outer membrane vesicles (OMVs). L. capsici cells were found to form a group of OMVs responsible for antifungal activity. The data are indicative of a significant antimicrobial potential of this bacterium that requires thorough research.
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.
Outer membrane vesicles (OMVs) produced by Gram-negative bacteria have been intensively investigated in recent times. Vesicle formation models have been proposed, some factors affecting the process were established, and important roles vesicles play in vital activities of their producing cells were determined. Studies of pathogenic bacterial vesicles contribute to understanding the causes of acute infection and developing drugs on their basis. Despite intensive research, issues associated with the understanding of vesicle biogenesis, the mechanisms of bacterium-bacterium and pathogen-host interactions with participation of vesicles, still remain unresolved. This review discusses some results obtained in the research into OMVs of Lysobacter sp. XL1 VKM B-1576. This bacterium secretes into the environment a spectrum of bacteriolytic enzymes that hydrolyze peptidoglycan of competing bacteria, thus leading to their lysis. One of these enzymes, lytic endopeptidase L5, has been shown not only to be secreted by means of vesicles but also to be involved in their formation. As part of vesicles, the antimicrobial potential of L5 enzyme has been found to be considerably expanded. Vesicles have been shown to have a therapeutic effect in respect of anthrax infection and staphylococcal sepsis modelled in mice. The scientific basis for constructing liposomal antimicrobial preparations from vesicle phospholipids and recombinant bacteriolytic enzyme L5 has been formed.
Membrane vesicles produced by bacteria have been intensively studied in the recent years. Investigators have noted their roles in essential processes in the bacterial cell including secretion of proteins by the ‘eukaryotic' vesicular mechanism. To date, formation of vesicles is not considered to be a spontaneous event. Many believe it to be a programmed process that can be guided by several mechanisms. Vesicles are derivatives of the cell envelope, which in turn is a supramolecular structure where the functioning and biogenesis of all components are interrelated. Proteins secreted beyond the cell in their translocation are also part of the cell envelope. This also suggests their role in vesicle biogenesis. This review presents the results of vesicle studies in the Gram-negative bacterium Lysobacter sp. This bacterium is of interest as it secretes a number of proteins to the environment, including bacteriolytic enzymes. Bacteriolytic enzymes, on the one hand, are important for studies from a medical point of view as they can form the basis of new generation antimicrobial means. On the other hand, they are a convenient subject for studies of vesicle functions in the vital activities of the bacterial cell.
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