Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Stepnaya, O. A.; Tsfasman, I. M.; Logvina, I. A.; Ryazanova, L. P.; Muranova, T. A.; Kulaev, I. S.

doi:10.1007/s10541-005-0221-1

Cited by 21 publications

(10 citation statements)

References 8 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, endopeptidase L1 does not hydrolyze the native cells of Gram-negative bacteria but is capable of degrading their autoclaved cells and the peptidoglycan isolated from them. In this substrate the enzyme hydrolyzes the bond between diaminopimelic acid and alanine [Stepnaya et al, 2005].…”

Section: Discussionmentioning

confidence: 99%

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

Vasilyeva¹,

Shishkova²,

Marinin³

et al. 2014

Microb Physiol

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

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

Vasilyeva¹,

Shishkova²,

Marinin³

et al. 2014

Microb Physiol

View full text Add to dashboard Cite

show abstract

Section: Introductionmentioning

confidence: 99%

“…Bacterial cell walls have a com plex chemical structure; consequently, lysis can be brought about by various enzymes, mostly hydrolases, in particular, glycosidases and proteases [1]. The sources of bacteriolytic enzymes are animals, plants, fungi, microorganisms, and bacteriophages [1][2][3][4][5][6]. Today there are a great many publications devoted to bacteriolytic enzymes [1,[4][5][6][7], which is explained by their wide application in genetic engineering, medicine, and various branches of industry.…”

Section: Introductionmentioning

confidence: 99%

“…The sources of bacteriolytic enzymes are animals, plants, fungi, microorganisms, and bacteriophages [1][2][3][4][5][6]. Today there are a great many publications devoted to bacteriolytic enzymes [1,[4][5][6][7], which is explained by their wide application in genetic engineering, medicine, and various branches of industry. The recent outbreak of infectious diseases in Europe has shown the urgency of developing alternative methods of diagnosis of, and therapy for, diseases of various etiology, in particular, diseases caused by gram negative microorganisms [8].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Bacteriolytic enzymes from the blood plasma of the sheep

et al. 2012

View full text Add to dashboard Cite

In the present work the studies ofbacteriolytic factors from sheep blood plasma have been performed. Three novel enzymes have been identified and characterized. Two of them have a molecular weight 15 +/- 2 kDa and able to lyse the gram-negative Escherichia coli bacteria. The third enzyme has a molecular weight 34 +/- 4 kDa and is able to lyse both gram-negative Escherichia coli and gram-positive Micrococcus luteus bacteria. The bacteriolytic reactions have been studied for all three enzymes; particularly, pH-optima have been identified with respect to the substrate. To identify the enzymes trypsinolysis and consequent MALDI-TOF mass spectrometry studies were performed. The results were compared to data from publicly available databases, such as Swiss-Prot, NCBI, MSDB.

show abstract

“…The bacteriolytic enzymes of the lysoamidase preparation are represented by three endopeptidases, L1, L4, and L5, as well as N-acetylmuramoyl-L-alanine amidase L2 and muramidase L3 (42,45,47,51). It is obvious that the occurrence of lytic enzymes specific to different bonds in peptidoglycan determines a broad range of lysoamidase antibacterial activities.…”

mentioning

confidence: 99%

Cloning and Expression Analysis of Genes Encoding Lytic Endopeptidases L1 and L5 from Lysobacter sp. Strain XL1

Lapteva

Zolova

Shlyapnikov

et al. 2012

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

c Lytic enzymes are the group of hydrolases that break down structural polymers of the cell walls of various microorganisms. In this work, we determined the nucleotide sequences of the Lysobacter sp. strain XL1 alpA and alpB genes, which code for, respectively, secreted lytic endopeptidases L1 (AlpA) and L5 (AlpB). In silico analysis of their amino acid sequences showed these endopeptidases to be homologous proteins synthesized as precursors similar in structural organization: the mature enzyme sequence is preceded by an N-terminal signal peptide and a pro region. On the basis of phylogenetic analysis, endopeptidases AlpA and AlpB were assigned to the S1E family [clan PA(S)] of serine peptidases. Expression of the alpA and alpB open reading frames (ORFs) in Escherichia coli confirmed that they code for functionally active lytic enzymes. Each ORF was predicted to have the Shine-Dalgarno sequence located at a canonical distance from the start codon and a potential Rho-independent transcription terminator immediately after the stop codon. The alpA and alpB mRNAs were experimentally found to be monocistronic; transcription start points were determined for both mRNAs. The synthesis of the alpA and alpB mRNAs was shown to occur predominantly in the late logarithmic growth phase. The amount of alpA mRNA in cells of Lysobacter sp. strain XL1 was much higher, which correlates with greater production of endopeptidase L1 than of L5.

show abstract

Isolation and Characterization of a New Extracellular Bacteriolytic Endopeptidase of Lysobacter sp. XL1

Cited by 21 publications

References 8 publications

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

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

Bacteriolytic enzymes from the blood plasma of the sheep

Cloning and Expression Analysis of Genes Encoding Lytic Endopeptidases L1 and L5 from Lysobacter sp. Strain XL1

Contact Info

Product

Resources

About