Dataset Information


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.


PROVIDER: S-EPMC7305183 | BioStudies | 2020-01-01

REPOSITORIES: biostudies

Similar Datasets

1000-01-01 | S-EPMC3979864 | BioStudies
2016-01-01 | S-EPMC4742617 | BioStudies
2015-01-01 | S-EPMC4657364 | BioStudies
2015-01-01 | S-EPMC4644931 | BioStudies
2014-01-01 | S-EPMC4238840 | BioStudies
2015-01-01 | S-EPMC4457069 | BioStudies
2016-01-01 | S-EPMC4960238 | BioStudies
2017-01-01 | S-EPMC5300149 | BioStudies
2015-01-01 | S-EPMC4499002 | BioStudies
2015-01-01 | S-EPMC4408182 | BioStudies