Literature DB >> 24434599

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

Natalia V Vasilyeva1, Nina A Shishkova, Leonid I Marinin, Larisa A Ledova, Irina M Tsfasman, Tatyana A Muranova, Olga A Stepnaya, Igor S Kulaev.   

Abstract

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.
© 2014 S. Karger AG, Basel.

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Year:  2014        PMID: 24434599     DOI: 10.1159/000356838

Source DB:  PubMed          Journal:  J Mol Microbiol Biotechnol        ISSN: 1464-1801


  6 in total

1.  Structural Studies of Component of Lysoamidase Bacteriolytic Complex from Lysobacter sp. XL1.

Authors:  Svetlana Tishchenko; Azat Gabdulkhakov; Bogdan Melnik; Irina Kudryakova; Oleg Latypov; Natalya Vasilyeva; Alexey Leontievsky
Journal:  Protein J       Date:  2016-02       Impact factor: 2.371

2.  The First Homologous Expression System for the β-Lytic Protease of Lysobacter capsici VKM B-2533T, a Promising Antimicrobial Agent.

Authors:  Irina Kudryakova; Alexey Afoshin; Elena Leontyevskaya; Natalia Leontyevskaya Vasilyeva
Journal:  Int J Mol Sci       Date:  2022-05-20       Impact factor: 6.208

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

Authors:  A S Afoshin; I V Kudryakova; A O Borovikova; N E Suzina; I Yu Toropygin; N A Shishkova; N V Vasilyeva
Journal:  Sci Rep       Date:  2020-06-19       Impact factor: 4.379

4.  Comparative genomics provides insights into the potential biocontrol mechanism of two Lysobacter enzymogenes strains with distinct antagonistic activities.

Authors:  Shuai Xu; Ziyu Zhang; Xuewen Xie; Yanxia Shi; Ali Chai; Tengfei Fan; Baoju Li; Lei Li
Journal:  Front Microbiol       Date:  2022-08-11       Impact factor: 6.064

5.  Whole-Genome Sequencing of Lysobacter capsici VKM B-2533T and Lysobacter gummosus 10.1.1, Promising Producers of Lytic Agents.

Authors:  Sergey V Tarlachkov; Irina V Kudryakova; Alexey S Afoshin; Elena A Leontyevskaya; Natalia V Leontyevskaya Vasilyeva
Journal:  Microbiol Resour Announc       Date:  2022-08-03

6.  Diversity and Activity of Lysobacter Species from Disease Suppressive Soils.

Authors:  Ruth Gómez Expósito; Joeke Postma; Jos M Raaijmakers; Irene De Bruijn
Journal:  Front Microbiol       Date:  2015-11-16       Impact factor: 5.640

  6 in total

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