The Effect of the Extracellular Bacteriolytic Enzymes of Lysobacter sp. on Gram-Negative Bacteria

Begunova, E. A.; Stepnaya, O. A.; Tsfasman, I. M.; Kulaev, I. S.

doi:10.1023/b:mici.0000032235.06143.5e

Cited by 13 publications

(8 citation statements)

References 12 publications

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“…It was shown earlier that lysoamidase did not affect the survival rate of P. vulgaris and P. mirabilis cells at the stationary phase of growth [12]. For this reason, cells at the logarithmic phase of growth were used as a substrate in subsequent experiments.…”

Section: Resultsmentioning

confidence: 99%

Effect of the Proteolytic Enzymes of Bacillus licheniformis and the Lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis Cells

Ryazanova

Ledova

Tsurikova

et al. 2005

Appl Biochem Microbiol

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Preparations of culture liquid of three Bacullus licheniformis strains (S, 103, and 60.4) and the enzymatic preparation lysoamidase from culture liquid of Lysobacter sp. strain XL1 actively lysed pre-autoclaved cells of the gram-negative bacteria Proteus vulgaris and P. mirabilis. Living Proteus cells treated with these enzymatic preparations were lysed during their subsequent autoclaving. Inoculation of enzyme-treated Proteus cells, taken either separately or in combination with one another and polymyxin B, into a rich medium led to cell repair and restoration of the culture viability.

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Section: Resultsmentioning

confidence: 99%

Effect of the Proteolytic Enzymes of Bacillus licheniformis and the Lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis Cells

Ryazanova

Ledova

Tsurikova

et al. 2005

Appl Biochem Microbiol

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“…The authors showed that secretion into the extracellular medium is due to outer membrane leakage initiated by the accumulation of the enzyme in the cell. We have shown previously that E. coli peptidoglycan is digested by endopeptidases AlpA and AlpB [Begunova et al, 2004]. Therefore, accumulation of lytic enzymes in the periplasm of E. coli cells may cause their lysis.…”

Section: Discussionmentioning

confidence: 99%

Gene Expression of Lytic Endopeptidases AlpA and AlpB from <b><i>Lysobacter </i></b>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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“…Measurement of the permeability alterations of the Gramnegative bacterial OM serves many purposes in the study and development of antimicrobial agents [22]. The molecular basis of the integrity of the OM lies in its LPS.…”

Section: Discussionmentioning

confidence: 99%

Potentiometric assessment of Gram-negative bacterial permeabilization of tobramycin

El-Kosasy

2006

Journal of Pharmaceutical and Biomedical Analysis

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The Effect of the Extracellular Bacteriolytic Enzymes of Lysobacter sp. on Gram-Negative Bacteria

Cited by 13 publications

References 12 publications

Effect of the Proteolytic Enzymes of Bacillus licheniformis and the Lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis Cells

Effect of the Proteolytic Enzymes of Bacillus licheniformis and the Lysoamidase of Lysobacter sp. XL1 on Proteus vulgaris and Proteus mirabilis Cells

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

Potentiometric assessment of Gram-negative bacterial permeabilization of tobramycin

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