Structural Investigations and Identification of the Extracellular Bacteriolytic Endopeptidase L1 from Lysobacter sp. XL1

Muranova, T. A.; Krasovskaya, L. A.; Tsfasman, I. M.; Stepnaya, O. A.; Kulaev, I. S.

doi:10.1023/b:biry.0000029847.40511.26

Cited by 16 publications

(10 citation statements)

References 11 publications

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“…The most investigated among these enzymes are lytic proteases L1 and L5. The gene structures of these proteins ( alp A and alp B) suggest them to be synthesized as pre-pro-proteins, as has been shown for the alpha-lytic protease of Lysobacter enzymogenes , which is homologous to them [Granovsky et al, 2010[Granovsky et al, , 2011Lapteva et al, 2012;Muranova et al, 2004]. In accordance with this, it could be assumed that secretion of enzymes L1 and L5 from the cytosol into the environment should proceed by the same protocol, in two stages.…”

Section: Introductionmentioning

confidence: 95%

“…Enzymes L1 and L5 are synthesized in the bacterial cytosol as pre-pro-proteins, which suggests secretion through the cytoplasmic membrane via a Sec-export mechanism [Granovsky et al, 2010[Granovsky et al, , 2011Muranova et al, 2004;Lapteva et al, 2012]. For Lysobacter , there has been no data defining the existence of a similar mechanism.…”

Section: Formation Of Vesicles In Lysobacter Sp and Their Role In Sementioning

confidence: 99%

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The Role of Membrane Vesicles in Secretion of Lysobacter sp. Bacteriolytic Enzymes

et al. 2013

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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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Section: Introductionmentioning

confidence: 95%

Section: Formation Of Vesicles In Lysobacter Sp and Their Role In Sementioning

confidence: 99%

The Role of Membrane Vesicles in Secretion of Lysobacter sp. Bacteriolytic Enzymes

et al. 2013

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“…The enzyme L5 is homologous to endopeptidase L1 of Lysobacter sp. XL1 and α-lytic protease of Lysobacter enzymogenes [Muranova et al, 2004], both known to digest the Gly-Gly and mur-D -Ala bonds in the peptidoglycan of S. aureus . Therefore, we have investigated the action of enzyme L5 on the peptidoglycan of S. aureus 209Р with and without teichoic acids.…”

Section: Action Of Enzyme L5 On Bacterial Cell Wall Componentsmentioning

confidence: 99%

“…Earlier, four lytic enzymes L1-L4 were isolated from the culture liquid of Lysobacter sp. XL1 and characterized [Muranova et al, 2004;Stepnaya et al, 1992Stepnaya et al, , 1996aStepnaya et al, , b, 2005]. An additional protein fraction possessing lytic activity against the autoclaved cells of Staphylococcus aureus 209P was found during optimization of the scheme of lytic enzymes purification.…”

Section: Introductionmentioning

confidence: 99%

Lytic Peptidase L5 of Lysobacter sp. XL1 with Broad Antimicrobial Spectrum

Vasilyeva¹,

Shishkova²,

Marinin³

et al. 2014

Microb Physiol

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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.

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“…AlpA and AlpB are homologous proteins that are close in size, and their pre-pro-protein sequences are 62% identical [Granovsky et al, 2010[Granovsky et al, , 2011. These enzymes also exhibit a homology with the well-investigated α-lytic protease from L. enzymogenes [Epstein and Wensink, 1988;Muranova et al, 2004], for which its pro part has been found to be involved in its folding and to be autocatalytically split off after the enzyme takes a native conformation [Fujishige et al, 1992;Silen et al, 1989].…”

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confidence: 99%

Gene Expression of Lytic Endopeptidases AlpA and AlpB from Lysobacter sp. XL1 in Pseudomonads

Tsfasman

Lapteva²,

Krasovskaya³

et al. 2015

Microb Physiol

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Development of an efficient expression system for (especially secreted) bacterial lytic enzymes is a complicated task due to the specificity of their action. The substrate for such enzymes is peptidoglycan, the main structural component of bacterial cell walls. For this reason, expression of recombinant lytic proteins is often accompanied with lysis of the producing bacterium. This paper presents data on the construction of an inducible system for expression of the lytic peptidases AlpA and AlpB from Lysobacter sp. XL1 in Pseudomonas fluorescens Q2-87, which provides for the successful secretion of these proteins into the culture liquid. In this system, the endopeptidase gene under control of the T7lac promoter was integrated into the bacterial chromosome, as well as the Escherichia coli lactose operon repressor protein gene. The T7 pol gene under lac promoter control, which encodes the phage T7 RNA polymerase, is maintained in Pseudomonas cells on the plasmids. Media and cultivation conditions for the recombinant strains were selected to enable the production of AlpA and AlpB by a simple purification protocol. Production of recombinant lytic enzymes should contribute to the development of new-generation antimicrobial drugs whose application will not be accompanied by selection of resistant microorganisms.

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Structural Investigations and Identification of the Extracellular Bacteriolytic Endopeptidase L1 from Lysobacter sp. XL1

Cited by 16 publications

References 11 publications

The Role of Membrane Vesicles in Secretion of <b><i>Lysobacter</i></b> sp. Bacteriolytic Enzymes

The Role of Membrane Vesicles in Secretion of <b><i>Lysobacter</i></b> sp. Bacteriolytic Enzymes

Lytic Peptidase L5 of <b><i>Lysobacter </i></b>sp. XL1 with Broad Antimicrobial Spectrum

Gene Expression of Lytic Endopeptidases AlpA and AlpB from <b><i>Lysobacter </i></b>sp. XL1 in Pseudomonads

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