The Role of Membrane Vesicles in Secretion of &lt;b&gt;&lt;i&gt;Lysobacter&lt;/i&gt;&lt;/b&gt; sp. Bacteriolytic Enzymes

Vasilyeva, Natalia V.; Tsfasman, I. M.; Kudryakova, Irina V.; Suzina, N. E.; Shishkova, N.A.; Kulaev, I. S.; Stepnaya, O. A.

doi:10.1159/000346550

Cited by 13 publications

(10 citation statements)

References 64 publications

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“…Vesicles containing this enzyme possess a lytic activity against the autoclaved cells of S. aureus 209P and the living cells of E. caratovora B15 [Vasilyeva et al, 2008[Vasilyeva et al, , 2013. In the present work, the lytic action of Lysobacter sp.…”

Section: Antimicrobial Spectrum Of Lysobacter Sp Xl1 Vesicles Contaimentioning

confidence: 51%

“…We found that the lytic action of Lysobacter sp. XL1 vesicles is due to the action of not autolytic but extracellular lytic enzymes [Vasilyeva et al, 2008[Vasilyeva et al, , 2013. The lytic action of vesicles on Grampositive bacteria was much stronger than on Gram-negative ones.…”

Section: Discussionmentioning

confidence: 99%

“…Vesicles were obtained from the culture liquid of Lysobacter sp. XL1 [Vasilyeva et al, 2008[Vasilyeva et al, , 2013.…”

Section: Methodsmentioning

confidence: 99%

“…Enzyme L5 was found in extracellular membrane vesicles formed by Lysobacter sp. XL1 and possessing lytic activity against the living cells of Erwinia caratovora B15 and the autoclaved cells of S. aureus 209P [Vasilyeva et al, 2008[Vasilyeva et al, , 2013. The goal of this work was to isolate and characterize the enzyme L5 of Lysobacter sp.…”

Section: Introductionmentioning

confidence: 99%

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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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Section: Antimicrobial Spectrum Of Lysobacter Sp Xl1 Vesicles Contaimentioning

confidence: 51%

Section: Discussionmentioning

confidence: 99%

“…Vesicles were obtained from the culture liquid of Lysobacter sp. XL1 [Vasilyeva et al, 2008[Vasilyeva et al, , 2013.…”

Section: Methodsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

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

Vasilyeva¹,

Shishkova²,

Marinin³

et al. 2014

Microb Physiol

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“…However, bacteria are known which appear to possess membranous nuclear envelopes superficially resembling eukaryotic nuclei [Fuerst and Sagulenko, 2013]. Further, outer membrane vesicles of Gram-negative bacteria are now known to function in communication, protection and pathogenesis although such vesicular structures were thought to be largely limited to eukaryotes just a few years ago [Manning and Kuehn, 2013; Schertzer and Whiteley, 2013; Vasilyeva et al, 2013]. Finally, some intracellular organelles such as acidocalcisomes are ubiquitous, being present in bacteria, archaea and eukaryotes [Caetano-Anolles and Seufferheld, 2013].…”

Section: Introductionmentioning

confidence: 99%

Microcompartments and Protein Machines in Prokaryotes

Saier

2013

Microb Physiol

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The prokaryotic cell was once thought of as a ‘bag of enzymes' with little or no intracellular compartmentalization. In this view, most reactions essential for life occurred as a consequence of random molecular collisions involving substrates, cofactors and cytoplasmic enzymes. Our current conception of a prokaryote is far from this view. We now consider a bacterium or an archaeon as a highly structured, nonrandom collection of functional membrane-embedded and proteinaceous molecular machines, each of which serves a specialized function. In this article we shall present an overview of such microcompartments including (1) the bacterial cytoskeleton and the apparati allowing DNA segregation during cell division; (2) energy transduction apparati involving light-driven proton pumping and ion gradient-driven ATP synthesis; (3) prokaryotic motility and taxis machines that mediate cell movements in response to gradients of chemicals and physical forces; (4) machines of protein folding, secretion and degradation; (5) metabolosomes carrying out specific chemical reactions; (6) 24-hour clocks allowing bacteria to coordinate their metabolic activities with the daily solar cycle, and (7) proteinaceous membrane compartmentalized structures such as sulfur granules and gas vacuoles. Membrane-bound prokaryotic organelles were considered in a recent Journal of Molecular Microbiology and Biotechnology written symposium concerned with membranous compartmentalization in bacteria [J Mol Microbiol Biotechnol 2013;23:1-192]. By contrast, in this symposium, we focus on proteinaceous microcompartments. These two symposia, taken together, provide the interested reader with an objective view of the remarkable complexity of what was once thought of as a simple noncompartmentalized cell.

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Outer membrane vesicles as platform vaccine technology

Pol

Stork

Ley

2015

Biotechnology Journal

288

241

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Outer membrane vesicles (OMVs) are released spontaneously during growth by many Gram‐negative bacteria. They present a range of surface antigens in a native conformation and have natural properties like immunogenicity, self‐adjuvation and uptake by immune cells which make them attractive for application as vaccines against pathogenic bacteria. In particular with Neisseria meningitidis, they have been investigated extensively and an OMV‐containing meningococcal vaccine has recently been approved by regulatory agencies. Genetic engineering of the OMV‐producing bacteria can be used to improve and expand their usefulness as vaccines. Recent work on meningitis B vaccines shows that OMVs can be modified, such as for lipopolysaccharide reactogenicity, to yield an OMV product that is safe and effective. The overexpression of crucial antigens or simultaneous expression of multiple antigenic variants as well as the expression of heterologous antigens enable expansion of their range of applications. In addition, modifications may increase the yield of OMV production and can be combined with specific production processes to obtain high amounts of well‐defined, stable and uniform OMV particle vaccine products. Further improvement can facilitate the development of OMVs as platform vaccine product for multiple applications.

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

Cited by 13 publications

References 64 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

Microcompartments and Protein Machines in Prokaryotes

Outer membrane vesicles as platform vaccine technology

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