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PubMed2004

Bacteriocin-like substance production by Bacillus licheniformis strain P40.

AIMS: To investigate the production of bacteriocin-like compounds by Bacillus spp. isolated from the Amazon basin. METHODS AND RESULTS: An antimicrobial substance produced by Bacillus licheniformis strain P40 was inhibitory to a broad range of indicator strains, such as Listeria monocytogenes, Bacillus cereus and clinical isolates of Streptococcus spp. The compound was stable at 100 degrees C, but lost its activity when treated at 121 degrees C/103.5 kPa for 15 min. It was resistant to the proteolytic action of trypsin and papain but sensitive to pronase E and was stable within a wide range of pH (3-11). The substance was bactericidal and bacteriolytic to L. monocytogenes. CONCLUSIONS: An antibacterial peptide produced by Bacillus licheniformis was characterized, presenting a broad spectrum of activity against pathogenic and spoilage organisms. SIGNIFICANCE AND IMPACT OF THE STUDY: The identification of a substance active against important pathogens addresses an important aspect of food safety.

Antibiosis↗
PubMed2004

Characterisation of autolytic enzymes in Lactobacillus pentosus.

AIMS: To characterize autolysis and autolytic system of the lactic acid bacterium Lactobacillus pentosus. METHODS AND RESULTS: Autolysis of nine Lact. pentosus strains was evaluated in buffer solution. Their peptidoglycan hydrolase profiles were examined by renaturing SDS-PAGE and revealed two major activity bands at 58 and 112 kDa. Specificity analysis indicated the presence of at least two different types of peptidoglycan hydrolase activities in Lact. pentosus 1091. CONCLUSIONS: Autolysis of Lact. pentosus was shown to be strain dependent and involvement of at least two different autolysins was evidenced. SIGNIFICANCE AND IMPACT OF THE STUDY: The autolytic system of Lact. pentosus was characterized for the first time and the data obtained could be used in the selection of strains of technological interest.

Bacteriolysis↗
PubMed2004

Isolation of bacteriophages from the oral cavity.

AIMS: To isolate bacteriophages lytic for oral pathogens from human saliva, dental plaque and mature biofilms constituted from saliva-derived bacteria. METHODS AND RESULTS: Saliva and dental plaque samples from healthy volunteers and from patients with gingivitis and periodontitis were examined for the presence of lytic bacteriophage using a panel of oral pathogens and bacteria isolated from the samples. Samples were also enriched for bacteriophage using static culture techniques and mature biofilms. A limited number of samples contained bacteriophage particles that were visualized using electron microscopy. Cultures yielded phage infecting non-oral bacteria (Proteus mirabilis) but no bacteriophage specific for recognized oral pathogens were found. Some micro-organisms from the oral microflora elaborated antibacterial substances that inhibited growth of other residents of the oral cavity. CONCLUSIONS: Unlike other ecosystems, the composition of the oral cavity does not appear to be heavily influenced by interactions between bacteriophages and their hosts. SIGNIFICANCE AND IMPACT OF THE STUDY: Bacteriophage for control of oral infections may need to be obtained from other sources. Antibacterial substances derived from some members of the oral microflora warrant investigation as potential antibiotics.

Actinomyces↗
PubMed2006

Isolation, characterization of bacteriophages specific to Microlunatus phosphovorus and their application for rapid host detection.

AIMS: To isolate and characterize lytic-bacteriophages specific to Microlunatus phosphovorus, and prepare fluorescently labelled phages (FLPs) for the rapid detection of the host bacterium in activated sludge. METHODS AND RESULTS: Isolation of bacteriophages lytic to M. phosphovorus was attempted by applying supernatants of activated sludge processes on the lawn of M. phosphovorus JCM9379 for plaque formation. Thirteen bacteriophage isolates were obtained. The restriction fragment length polymorphism analysis distinguished them into two different bacteriophages designated as phiMP1 and phiMP2. They were found to possess double-stranded DNA and host specificity. Morphological observations were done by electron microscopy. The bacteriophage particles stained by SYBR Green I was shown to be applicable to detect their host bacterial cells mixed with activated sludge. CONCLUSIONS: Two M. phosphovorus-specific bacteriophages were isolated and classified as Siphoviridae. FLPs of them were prepared, and successfully applied to detect the host bacterium added into the activated sludge. SIGNIFICANCE AND IMPACT OF THE STUDY: At least some of bacteria in activated sludge are susceptible to their related bacteriophages. Bacteriophages lytic to activated sludge bacteria could be affecting the bacterial population in activated sludge. The FLPs could be used for the easy-rapid detection of their host bacterium in activated sludge.

Bacteriolysis↗
PubMed2005

A novel mechanism of autolysis in Helicobacter pylori: possible involvement of peptidergic substances.

BACKGROUND: Helicobacter pylori survival in a hostile acidic environment is known to be caused by its production of urease, which is not released by known secretion pathways. It has been proposed that H. pylori cells undergo spontaneous autolysis during cultivation and that urease becomes surface-associated only concomitant with bacterial autolysis. The aim of this study was to elucidate mechanisms by which H. pylori cells undergo autolysis during cultivation. MATERIALS AND METHODS: Autolysis of H. pylori KZ109 cells was estimated by measuring the turbidity of the culture, by detection of cytoplasmic protein release into the culture supernatant and by scanning electron microscopic observation of H. pylori cells during cultivation. An autolysis-inducing factor (AIF) was partially purified from the culture supernatant by a partition method using ethyl acetate. RESULTS: Bacterial turbidity of KZ109 cells was drastically decreased after late-log phase accompanying release of urease and HspB into the extracellular space. Concomitantly, cell lytic activity was detected in the culture supernatant. Scanning electron microscopic observation suggested that partially purified AIF induced cell lysis. It was also shown that the AIF is different from other autolytic enzymes or substances so far reported. CONCLUSIONS: This study demonstrated the presence of the peptidergic autolytic substances in the culture supernatant of H. pylori KZ109 cells. The results of this study should be useful for further studies aimed at elucidation of the strategy of survival of H. pylori in the gastric environment and elucidation of the mechanisms of pathogenesis induced by H. pylori.

Bacterial Proteins↗
PubMed1979

Partial purification and characterization of a bacteriolytic enzyme secreted by Tetrahymena.

Tetrahymena pyriformis strain HSM secretes large quantities of acid hydrolases into the culture medium. An enzyme secreted by the ciliate and capable of degrading walls of streptococci was identified and purified to a considerable degree. The pH optimum of this enzyme was 3--4, and it was eluted after cytochrome c from Sephadex G-75 columns. Unlike lysozyme, the enzyme was thermolabile at pH 2.9, but relatively thermostable at pH 8.1. It degraded 14C-labeled cell walls of streptococci releasing reducing groups. Cell walls prepared from different strains of streptococci differed in susceptibility to this enzyme, the most sensitive strain tested being of group A, type T12. It was shown in immunologic studies that this hydrolase released the group-specific carbohydrate from the walls. Secretions of Tetrahymena from early stationary-phase cultures had more bacteriolytic activity than those from cells from late stationary-phase cultures. Further, cells from cultures grown in glucose-supplemented medium secreted less of the enzyme than ciliates of comparable age grown in unsupplemented proteose-peptone. The newly isolated bacteriolytic enzyme, presumably of lysosomal origin, may be helpful in characterizing streptococcal cell walls.

Animals↗
PubMed1997

Stazyme, a mycobacteriolytic preparation from a Staphylococcus strain, is able to break the permeability barrier in multiple drug resistant Mycobacterium avium.

As a strategy to augment the potential of existing drugs against Mycobacterium avium we investigated a mycobacteriolytic preparation (stazyme) from the Staphylococcus strain Clavelis, which results in significant mycobacterial growth inhibition. A total of 10 specific protein bands were characterized in the stazyme preparation: three bands within a major 40-60 kDa fraction, five bands within the range of 30-90 kDa, and two bands of about 12 and 14 kDa respectively. Tested at concentrations of 50 and 200 microg ml(-1) of total protein, stazyme was highly bactericidal against M. smegmatis, and bacteriostatic against M. tuberculosis and M. avium. Stazyme was able to break the permeability barrier of M. avium isolates, significantly enhancing the activity of other antituberculous drugs (ethambutol, rifampicin, and amikacin), used at sub-MIC level. Stazyme essentially possessed a lytic activity as evidenced by its ability to lyse purified M. smegmatis cell walls. This lytic activity was also confirmed on intact M. smegmatis and M. avium bacilli by transmission electron microscopy. Precise identification of this mycobacteriolytic determinant(s) in stazyme may be helpful to define novel drug targets in mycobacteria.

Amikacin↗
PubMed2001

Bactericidal activity of normal cord serum (NCS) against Gram-negative rods with sialic acid-containing lipopolysaccharides (LPS).

Sialic acids, that are important constituents of animal tissue glycoconjugates, are also present in antigens of some bacterial strains. Capsular polysaccharides with sialic acid have been extensively studied whereas little is known on lipopolysaccharides which contain sialic acid. The susceptibility of Gram-negative strains with sialic acid-containing lipopolysaccharides to the bactericidal action of the sera of newborns was examined. The strains investigated showed variable sensitivity to the bactericidal action of normal cord serum.

Bacteriolysis↗
PubMed2002

Isolation and characterisation of a 13.8-kDa bacteriolytic enzyme from house dust mite extracts: homology with prokaryotic proteins suggests that the enzyme could be bacterially derived.

Bacteriolytic activity was detected in extracts of whole mite and spent growth medium (SGM) from the clinically important Dermatophagoides pteronyssinus and Dermatophagoides farinae mites and was most abundant in whole mite extract. Gram-positive organisms Micrococcus lysodeikticus, Bacillus megaterium and Listeria monocytogenes were preferentially lysed and the lytic activity was enhanced by thiols, destroyed by mite proteases, inhibited by HgCl2 and high concentrations of NaCl but was resistant to heat and acid treatment. Substrate SDS-PAGE analysis indicated the presence of several lytic enzymes, two of which were isolated from D. pteronyssinus spent growth medium extract by hydroxyapatite chromatography. The N-terminal amino acid sequence of one of them was then used in PCR-based cloning studies. The complete amino acid sequence of this protein was determined and cDNA found to encode a 130-amino acid residue mature protein with a 20-amino acid leader sequence. The deduced protein demonstrated sequence similarity with the C-terminal regions of a group of bacterial proteins belonging to the P60 superfamily. These data suggest that the enzyme is derived from bacteria within the mites rather than from mites per se.

Amino Acid Sequence↗
PubMed2002

The role of licA phase variation in the pathogenesis of invasive disease by Haemophilus influenzae type b.

LicA encodes the enzyme phosphorylcholine kinase which catalyses the incorporation of phosphorylcholine (ChoP) into H. influenzae LPS. Expression of this gene is subject to phase variation, resulting in the spontaneous loss, or gain of phosphorylcholine (ChoP)-decorated LPS structures. To investigate the role of this phenomenon in the pathogenesis of invasive disease an H. influenzae mutant was constructed which lacked the ability to phase vary licA. This was achieved by introducing an in-frame deletion of the 5'-CAAT-3' repeats into licA using polymerase chain reaction. The resultant mutant, licADelta5'-CAAT-3', was unable to switch off expression of licA and constitutively expressed ChoP-decorated LPS structures, as judged by colony immunoblotting with Mabs 12D9 and HAS. This resulted in increased synthesis of high molecular mass LPS structures and the absence of non-ChoP-decorated LPS species as determined by T-SDS-PAGE analysis. Inability to switch off the expression of licA reduced the virulence of H. influenzae in an infant rat model of invasive disease and resulted in increased sensitivity to the bactericidal activity of serum in the presence of CRP. The ability to switch off the expression of licA through phase variation is therefore concluded to enhance the systemic survival of H. influenzae.

Animals↗
PubMed1993

Extracellular proteolytic activation of bacteriolytic peptidoglycan hydrolases of Staphylococcus simulans biovar staphylolyticus.

Staphylococcus simulans biovar staphylolyticus secreted two bacteriolytic peptidoglycan hydrolases as proproteins that were activated as they were processed by an extracellular sulphydryl protease. This processing resulted in the production of multiple molecular-mass forms of each enzyme. Cells from early exponential phase cultures were susceptible to lysis by the mature forms of each of the peptidoglycan hydrolases whereas stationary phase cells were resistant. Thus secretion of these bacteriolytic enzymes during early exponential growth as precursors that are activated later by the protease would provide time for the cells to become resistant.

Bacterial Proteins↗
PubMed1994

Lysis of Escherichia coli cells induced by bacteriophage T4.

Structural changes in the envelope of Escherichia coli cells accompanying their lysis from without by bacteriophage T4 have been studied. The hypothesis concerning the role of collapse of membrane potential and formation of periplasmic vesicles in the process of lysis from without has been advanced.

Bacteriolysis↗
PubMed1994

Role of autolysins in the EDTA-induced lysis of Pseudomonas aeruginosa.

Treatment of Pseudomonas aeruginosa with metal ion chelators, especially ethylenediaminetetraacetic acid (EDTA), causes both release of protein-lipopolysaccharide complexes and cell death. We have examined the effect of EDTA on P. aeruginosa and found that EDTA does not induce the rapid solubilization of the peptidoglycan sacculus and complete lysis as previously thought; the decrease in optical density of cultures incubated with EDTA is primarily due to the loss of the outer membrane. Of the other potential solubilizers examined, only ethylene-bis(oxyethylenenitrilo)tetraacetic acid (EGTA) resulted in some decrease in optical density. The lytic effect of EDTA on 12 strains of P. aeruginosa was examined and was found to vary greatly between strains; the sensitivity to EDTA varies from between 96% and 10% of the decrease in optical density resulting from incubation of cells with both EDTA and lysozyme. Sensitivity to EDTA is not constant during the growth of P. aeruginosa; in the early exponential phase of growth, cells treated with EDTA exhibit a 82% decrease in optical density after 30 min while in the stationary phase the optical density decreases by only 40%. Nucleic acids were observed to leak from cells following treatment with EDTA and this was greatly facilitated by DNase and RNase. The release of genetic material was much reduced when cells were incubated at 4 degrees C, supporting an enzymatic role in cell wall solubilization. We propose that only small areas of the sacculus become hydrolysed via specific peptidoglycan hydrolases, or autolysin(s), which are activated or de-regulated by EDTA.

Bacteriolysis↗
PubMed1995

Plasmid and chromosomal DNA recovery by electroextraction of cyanobacteria.

High voltage electroporation has been investigated as a method for rapid recovery of plasmid and chromosomal DNA from the cyanobacteria Nostoc PCC 7121, Synechococcus PCC 7002, and Anabaena PCC 7120. Pulses of 18 kV/cm and higher applied to concentrated Nostoc cells carrying a shuttle plasmid (pRL25) resulted in copious release of nucleic acids and phycobiliproteins into the suspending medium. Small portions of these supernatants, when electroporated with Escherichia coli, gave rise to hundreds of E. coli transformants which contained pRL25. Electroporation of Synechococcus carrying plasmid pAQE19 did not cause detectable release of macromolecules but did reveal a low-level, voltage independent 'leakage' of pAQE19 into the medium. Electroextraction of Nostoc or Anabaena followed by addition of E. coli and delivery of a second high-voltage pulse permitted direct, one-cuvette transfer of shuttle plasmids from these cyanobacteria into E. coli. Electroextraction of single cyanobacterial colonies, as shown for Nostoc, also released sufficient chromosomal DNA for amplification of specific sequences by the polymerase chain reaction.

Anabaena↗
PubMed1996

Drastically decreased transcription from CII-activated promoters is responsible for impaired lysogenization of the Escherichia coli rpoA341 mutant by bacteriophage lambda.

It was demonstrated previously that a mutation, rpoA341, in the gene encoding the alpha subunit of Escherichia coli RNA polymerase prevents lysogenization by bacteriophage lambda. The rpoA341 allele is known to be responsible for impaired transcription of some positively regulated E. coli chromosomal operons. Here we demonstrate that the inhibition of lysogenization of the rpoA341 mutant is a result of drastically decreased transcription from positively regulated phage promoters. We were unable to detect any transcripts originating from the CII-activated pE, pI and paQ promoters (important for lysogenic development) in the phage-infected rpoA341 mutant, in contrast to an otherwise isogenic rpoA+ strain. The results are discussed in the light of other reports showing that activation of the pE promoter by CII protein in vitro is decreased only about fivefold when the native alpha subunit is replaced by truncated alpha polypeptides.

Bacteriolysis↗
PubMed1996

Isolation and properties of bacteriolytic enzyme-producing cocci from the human mouth.

One-hundred-and-one bacteriolytic enzyme producing organisms were isolated from various sites of the mouth. All were non-hemolytic, Gram-positive, and chain-forming cocci. Ninety-one strains, like the reference strains of Streptococcus defectivus and S. adjacens, were dependent on pyridoxal for growth and produced a chromophore. The Rapid ID32 STREP system speciated these isolates as S. defectivus, S. adjacens or Gemella morbillorum. The remaining 10 bacteriolytic isolates were pyridoxal-independent and 8 belonged to S. intermediate. Some pyridoxal-independent S. intermedius reference strains including ATCC27335T and all group D Enterococcus strains tested were also bacteriolytic. Thus, bacteriolytic enzyme production is common to nutritionally variant streptococci but not unique to S. defectives and S. adjacens. The nutritionally variant strains generally had arylamidases but not alkaline phosphatase. The S. defectivus strains produced alpha-and beta-galactosidases (biotype 1) whereas the S. adjacens strains generally produced N-acetyl-beta-glucosaminidase and some had beta-glucuronidase but others did not (biotypes 2 and 3). The C. morbillorum strains had no detectable activity of these glycosidases (biotype 4) but produced a chromophore and an arginine dihydrolase, exhibiting a physiological profile atypical of the Gemella species. This indicates the possible presence of an additional phenotypic group or a new species among the nutritionally variant streptococci.

Acetylglucosaminidase↗
PubMed1997

Characterization of Bacillus subtilis mutants resistant to cold shock-induced autolysis.

Bacillus subtilis vegetative cells undergo autolysis when exposed to cold shock treatment. A mutant (CA1) resistant to cold shock was isolated, and its DNA was used for the transformation of B. subtilis 168AR. The transformant (TR1) and CA1 had almost completely lost major vegetative autolysins (Cw1B and Cw1G) and motility, and showed a filamentous cell morphology during the exponential phase. Expression of the sigD-lacZ fusion was reduced in TR1. But the introduction of a SigD overproducing plasmid, pHYSigD, into TR1 led to a considerable increase in the amount of autolysin, a normal cell morphology (short rod), and the cold shock-sensitive phenotype. However, motility was not restored in the transformant. The roles of pleiotropic genes in cold shock-induced autolysis are discussed.

Bacillus subtilis↗
PubMed1997

Antibacterial and hemolytic activities of linenscin OC2, a hydrophobic substance produced by Brevibacterium linens OC2.

Linenscin OC2 is an antibacterial substance produced by the orange cheese coryneform bacterium Brevibacterium linens OC2. It inhibits the growth of Gram-positive bacteria but it is inactive against Gram-negative bacteria. The intact outer membrane of Gram-negative bacteria was shown to be an effective permeability barrier against linenscin OC2. At high dosage the effect of linenscin OC2 was bacteriolytic on Listeria innocua. Bacteriostasis was observed at low dosage and peptidoglycan biosynthesis was affected at an early step upstream of the UDP-N-acetylglucosamine. Hemolytic activity of this substance on sheep erythrocytes suggested a common mode of action on prokaryotic and eukaryotic cells. It also suggested that the cytoplasmic membrane might be the primary target of linenscin OC2.

Anti-Bacterial Agents↗