Lytic potential of Lysobacter capsici VKM B-2533T: bacteriolytic enzymes and outer membrane vesicles.

ABSTRACT: 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 ?- and ?-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 ?-lytic protease digested live methicillin-resistant staphylococcal cells with high efficiency (minimal inhibitory concentration, 2.85??g/mL). This property makes the enzyme deserving special attention. A recombinant ?-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.

SUBMITTER: Afoshin AS 

PROVIDER: S-EPMC7305183 | biostudies-literature | 2020 Jun

REPOSITORIES: biostudies-literature