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PubMed1977

Bacteriocin typing by leakage of ultraviolet light-absorbing material.

A rapid and reproducible method of bacteriocin typing is described based on leakage of ultraviolet light-absorbing material (UVAM), detectable in supernatants of bacteriocin-sensitive cultures, by means of a spectrophotometer. The prerequisites for reproducible results, with nonsignificant fluctuations in standard error of the mean, are: a set of standardized bacteriocins, produced under defined conditions and of determined strength. These must interact with the unknown bacterial culture in suspension and at a given ratio in order to achieve an optimal multiplicity of interaction. Pyocin and colicin typing by the "scrape and streak" technique of Gillies (J. Hyg. 62:1-10, 1963) was compared with the UVAM leakage method in 275 tests; the two tests were found to be in good agreement for the strains tested.

Bacteria↗

PubMed1978

Isolation and characterization of a Streptococcus mutans bacteriocin inhibitor from Streptococcus pyogenes.

An inhibitor of Streptococcus mutans strain GS5 bacteriocin was released from a bacteriocin-sensitive strain of S. pyogenes by sonic treatment and partly purified by gel filtration on a Sepharose 6B column. The inhibitory factor was sensitive to heat, trypsin, and periodate and possessed a molecular weight of approximately 93,000. This factor may be the receptor for the S. mutans bacteriocin.

Bacterial Proteins↗

PubMed1980

Single bacteriocin typing scheme for the vibrio group of organisms.

A total of 743 strains of O-I "agglutinable" and 293 strains of O I "inagglutinable" Vibrio cholerae were subjected to bacteriocin typing based on deferred antagonism of eight indicator bacteria, including two strains of V. cholerae, by the method of Chakrabarty et al. (Infect. Immun. 1:293-299, 1970). A minor modification that was effected in the typing medium was replacement of iodoacetic acid by ammonium chloride (at a final concentration of 0.003%) which appeared to regulate bacteriocin production more accurately and increase the stability of the types. Of the agglutinable strains, 94% were found to be bacteriocinogenic and could be fitted into 11 of the earlier-reported types (Chakrabarty et al., Infect. Immun. 1:293-299, 1970), and 6 newer types were recognized. Likewise, 285 (90.7%) of the inagglutinable strains were found to be bacteriocinogenic and could be accommodated within 10 original and 8 newer types identified for the inagglutinable vibrios. Thirteen types were common to the two groups of vibrios. The single bacteriocin typing scheme appeared to be simple and adequate for both groups of organisms, and the producer as well as the indicator bacteria behaved remarkably stably in this typing scheme over many years.

Bacteriocins↗

PubMed1987

A bacteriocin of Actinobacillus actinomycetemcomitans.

An inhibitory factor from Actinobacillus actinomycetemcomitans Y4 was isolated, and its properties indicated that it was a bacteriocin (actinobacillicin). The bacteriocin was active against Streptococcus sanguis strains, Streptococcus uberis (FDC1), and Actinomyces viscosus T14 as well as other strains of A. actinomycetemcomitans, but not against other crevicular bacteria, including other streptococci and actinomycetes. The activity of this bacteriocin was inhibited by pronase, trypsin, and heat (45 min at 56 degrees C) but not by DNase, RNase, phospholipase, exposure to UV light, or low pH (1.0 to 6.5). Although actinobacillicin markedly inhibited glycolysis in S. sanguis, the primary mechanism of its bactericidal action appears to be alterations in cell permeability, with the resultant leakage of RNA, DNA, and other essential intracellular macromolecules. These findings provide an ecologic explanation for the reciprocal growth relationship between A. actinomycetemcomitans and S. sanguis/Actinomyces viscosus observed in localized juvenile periodontitis.

Actinobacillus↗

PubMed2006

Cloning and expression of the Erwinia carotovora subsp. carotovora gene encoding the low-molecular-weight bacteriocin carocin S1.

The purpose of this study was to clone the carocin S1 gene and express it in a non-carocin-producing strain of Erwinia carotovora. A mutant, TH22-10, which produced a high-molecular-weight bacteriocin but not a low-molecular-weight bacteriocin, was obtained by Tn5 insertional mutagenesis using H-rif-8-2 (a spontaneous rifampin-resistant mutant of Erwinia carotovora subsp. carotovora 89-H-4). Using thermal asymmetric interlaced PCR, the DNA sequence from the Tn5 insertion site and the DNA sequence of the contiguous 2,280-bp region were determined. Two complete open reading frames (ORF), designated ORF2 and ORF3, were identified within the sequence fragment. ORF2 and ORF3 were identified with the carocin S1 genes, caroS1K (ORF2) and caroS1I (ORF3), which, respectively, encode a killing protein (CaroS1K) and an immunity protein (CaroS1I). These genes were homologous to the pyocin S3 gene and the pyocin AP41 gene. Carocin S1 was expressed in E. carotovora subsp. carotovora Ea1068 and replicated in TH22-10 but could not be expressed in Escherichia coli (JM101) because a consensus sequence resembling an SOS box was absent. A putative sequence similar to the consensus sequence for the E. coli cyclic AMP receptor protein binding site (-312 bp) was found upstream of the start codon. Production of this bacteriocin was also induced by glucose and lactose. The homology search results indicated that the carocin S1 gene (between bp 1078 and bp 1704) was homologous to the pyocin S3 and pyocin AP41 genes in Pseudomonas aeruginosa. These genes encode proteins with nuclease activity (domain 4). This study found that carocin S1 also has nuclease activity.

Amino Acid Sequence↗

PubMed1970

Characterization of a Staphylococcus aureus bacteriocin.

The bacteriocin produced by a strain of Staphylococcus aureus has been isolated and designated staphylococcin (414), and a study was made of its chemical, physical, and biological properties. The staphylococcin is released in appreciable quantities after breakage of the cells and can be purified through differential centrifugation and column chromatography. In the native state, it appears to be a lipoprotein-carbohydrate complex with a molecular weight in excess of 200,000. The complex can be dissociated by sodium dodecyl sulfate into smaller subunits which retain activity. The gross chemical and physical properties of the bacteriocin closely resemble those ascribed to certain preparations of cell membranes. Staphylococcin (414) is not a lytic enzyme like lysostaphin and does not have the same spectrum of activity. Like other bacteriocins from gram-positive microorganisms, it does not inhibit any gram-negative bacteria, but does inhibit several other genera.

Acridines↗

PubMed1985

Bacteriocin small of fast-growing rhizobia is chloroform soluble and is not required for effective nodulation.

Small bacteriocin is a low-molecular-weight bacteriocin which is common in fast-growing rhizobia. As its activity could not be detected in chloroform-sterilized culture supernatants (P.R. Hirsch, J. Gen. Microbiol. 113:219-228, 1979), the bacteriocin could not be purified in order to study its mechanism of action. We report here that small is soluble in chloroform, an observation which led to effective and simple (partial) purification. Other properties of small are its low molecular weight, which is estimated to be between 700 and 1,500, its resistance to proteolytic enzymes, pectinase, and lysozyme, and its heat stability at pH 5.5 but not at pH 7.0. Its bactericidal action on exponentially growing sensitive cells was not detected until 11 h after its addition. The bactericidal action was preceded by inhibition of cell division. To determine whether small activity is required for nodulation or nitrogen fixation, a transposon Tn5-induced small-negative mutant was isolated. The observation that this strain formed normal, acetylene-reducing root nodules showed that small production is not a prerequisite for the formation of effective nodules.

Bacteriocins↗

PubMed1986

Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481.

Lactobacillus helveticus 481 produced an antimicrobial agent active against five closely related species. The sensitive indicators included L. helveticus 1846 and 1244, L. bulgaricus 1373 and 1489, and L. lactis 970. The antimicrobial compound was active at neutral pH under aerobic or anaerobic conditions, was sensitive to proteolytic enzymes and heat (30 min at 100 degrees C), and demonstrated a bactericidal mode of action against sensitive indicators. These data confirmed that antimicrobial activity of L. helveticus 481 was mediated by a bacteriocin, designated helveticin J. Production of helveticin J was maximized in an anaerobic fermentor held at a constant pH of 5.5. Ultrafiltration experiments on culture supernatants containing the bacteriocin revealed that helveticin J was present as an aggregate with a molecular weight in excess of 300,000. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of helveticin J purified through Sephadex chromatography resolved a 37,000-dalton protein band with bacteriocin activity. L. helveticus 481 was shown to harbor a single 8-megadalton plasmid (pMJ1008). Isolates cured of pMJ1008 were phenotypically identical to plasmid-bearing cells in fermentation patterns, helveticin J activity, and immunity spectra. The data provided evidence for a chromosomal location of helveticin J and host immunity determinants.

Bacteriocins↗

PubMed1990

Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J.

Lactobacillus helveticus 481 produces a 37-kDa bacteriocin called helveticin J. Libraries of chromosomal DNA from L. helveticus were prepared in lambda gt11 and probed for phage-producing fusion proteins that could react with polyclonal helveticin J antibody. Two recombinant phage, HJ1 and HJ4, containing homologous inserts of 350 and 600 bp, respectively, produced proteins that reacted with antibody. These two phage clones specifically hybridized to L. helveticus 481 total genomic DNA but not to DNA from strains that did not produce helveticin J or strains producing unrelated bacteriocins. HJ1 and HJ4 lysogens produced beta-galactosidase fusion proteins that shared similar epitopes with each other and helveticin J. The intact helveticin J gene (hlv) was isolated by screening a library of L. helveticus chromosomal DNA in lambda EMBL3 with the insert DNA from phage HJ4 as a probe. The DNA sequence of a contiguous 3,364-bp region was determined. Two complete open reading frames (ORF), designated ORF2 and ORF3, were identified within the sequenced fragment. The 3' end of another open reading frame, ORF1, was located upstream of ORF2. A noncoding region and a putative promoter were located between ORF1 and ORF2. ORF2 could encode an 11,808-Da protein. The L. helveticus DNA inserts of the HJ1 and HJ4 clones reside within ORF3, which begins 30 bp downstream from the termination codon of ORF2. ORF3 could encode a 37,511-Da protein. Downstream from ORF3, the 5' end of another ORF (ORF4) was found. A Bg/II fragment containing ORF2 and ORF3 was cloned into pGK12, and the recombinant plasmid, pTRK135, was transformed into Lactobacillus acidophilus via electroporation. Transformants carrying pTRK135 produced a bacteriocin that was heat labile and exhibited an acitivity spectrum that was the same as that of helveticin J.

Amino Acid Sequence↗

PubMed1993

Membrane permeabilization of Listeria monocytogenes and mitochondria by the bacteriocin mesentericin Y105.

Mesentericin Y105, a bacteriocin produced by a Leuconostoc mesenteroides strain, dissipates the plasma membrane potential of Listeria monocytogenes and inhibits the transport of leucine and glutamic acid. It also induces an efflux of preaccumulated amino acids from cells. In addition, the bacteriocin uncouples mitochondria by increasing state 4 respiration and decreasing state 3 respiration. The bacteriocin inhibits ATP synthase and adenine nucleotide translocase of the organelle while the affinity of ADP for its carrier is not modified. The results suggest that mesentericin Y105 acts by inducing, directly or indirectly, pore formation in the energy-transducing membranes, especially those of its natural target.

Adenosine Triphosphate↗

PubMed1995

A signal peptide secretion-dependent bacteriocin from Carnobacterium divergens.

Divergicin A is a strongly hydrophobic, narrow-spectrum, nonlantibiotic bacteriocin produced by Carnobacterium divergens LV13. This strain of C. divergens contains a 3.4-kb plasmid that mediates production of, and immunity to, the bacteriocin. N-terminal amino acid sequencing of the purified divergicin A was used to locate the structural gene (dvnA). The structural gene encodes a prepeptide of 75 amino acids consisting of a 29-amino-acid N-terminal extension and a mature peptide of 46 amino acids. Directly downstream of dvnA there is a second open reading frame that encodes the immunity protein for divergicin A. Divergicin A has a calculated molecular mass of 4,223.89 Da. The molecular mass determined by mass spectrometry is 4,223.9 Da, indicating that there is no posttranslational modification of the peptide. The N-terminal extension of divergicin A has an Ala-Ser-Ala (positions -3 to -1) cleavage site and acts as a signal peptide that accesses the general export system of the cell (such as the sec pathway in Escherichia coli). This is the first bacteriocin of lactic acid bacteria to be reported that does not have dedicated maturation and secretion genes. Production of divergicin A was observed in heterologous hosts containing only the two genes associated with divergicin A production and immunity. Fusing alkaline phosphatase behind the signal peptide for divergicin resulted in the secretion of this enzyme in the periplasmic space and supernatant of E. coli.

Amino Acid Sequence↗

PubMed1996

Induction of bacteriocin production in Lactobacillus sake by a secreted peptide.

Lactobacillus sake LTH673 is known to produce a bacteriocin called sakacin P. Production of and immunity to sakacin P were found to depend on the presence of a protease-sensitive component that is produced by L. sake LTH673 itself. This component (called inducing factor [IF]) was purified from culture supernatants and shown to be a basic, nonbacteriocin peptide consisting of 19 amino acids, which in principle is capable of forming a highly amphiphilic helical structure. Circular dichroism studies showed that IF indeed could adopt a helical structure, but only in membrane-mimicking environments. Both purified IF and chemically synthesized IF induced expression of the structural gene for sakacin P and concomitant secretion of the gene product. In addition, IF induced its own production and immunity to sakacin P and related bacteriocins. These results indicate that bacteriocin production by L. sake LTH673 is controlled by an autoinduction pathway in which IF may function as a cell density signal.

Amino Acid Sequence↗

PubMed1999

Genes of the sbo-alb locus of Bacillus subtilis are required for production of the antilisterial bacteriocin subtilosin.

Bacillus subtilis JH642 and a wild strain of B. subtilis called 22a both produce an antilisterial peptide that can be purified by anion-exchange and gel filtration chromatography. Amino acid analysis confirmed that the substance was the cyclic bacteriocin subtilosin. A mutant defective in production of the substance was isolated from a plasmid gene disruption library. The plasmid insertion conferring the antilisterial-peptide-negative phenotype was located in a seven-gene operon (alb, for antilisterial bacteriocin) residing immediately downstream from the sbo gene, which encodes the precursor of subtilosin. An insertion mutation in the sbo gene also conferred loss of antilisterial activity. Comparison of the presubtilosin and mature subtilosin sequences suggested that certain residues undergo unusual posttranslational modifications unlike those occurring during the synthesis of class I (lantibiotic) or some class II bacteriocins. The putative products of the genes of the operon identified show similarities to peptidases and transport proteins that may function in processing and export. Two alb gene products resemble proteins that function in pyrroloquinoline quinone biosynthesis. The use of lacZ-alb and lacZ-sbo gene fusions, along with primer extension analysis, revealed that the sbo-alb genes are transcribed from a major promoter, residing upstream of sbo, that is very likely utilized by the sigma(A) form of RNA polymerase. The sbo and alb genes are negatively regulated by the global transition state regulator AbrB and are also under positive autoregulation that is not mediated by the subtilosin peptide but instead requires one or more of the alb gene products.

Amino Acid Sequence↗

PubMed2004

Heterologous expression and purification of active divercin V41, a class IIa bacteriocin encoded by a synthetic gene in Escherichia coli.

Divercin V41, a class IIa bacteriocin with strong antilisterial activity, is produced by Carnobacterium divergens V41. To express a recombinant version of divercin V41, we constructed a synthetic gene that encodes the mature divercin V41 peptide and then overexpressed the gene in pET-32b by using the T7 RNA polymerase promoter in the Escherichia coli Origami (DE3)(pLysS) strain. The DvnRV41 peptide was expressed as a translational fusion protein with thioredoxin and accumulated in the cell cytoplasm in a soluble anti-Listeria active form. The fusion protein was then purified and cleaved to obtain pure, soluble, folded DvnRV41 (462 microg per 20 ml of culture). This paper describes the first design of a synthetic bacteriocin gene and the first bacteriocin expressed in the E. coli cytoplasm.

Amino Acid Sequence↗

PubMed1979

Yersinia intermedia: temperature-dependent bacteriocin production.

Yersinia enterocolitica and related Yersinia species share many temperature-dependent biological attributes. The present report documents temperature-dependent production of a bacteriocin-like substance only among Yersinia strains which ferment L-rhamnose, raffinose, and melibiose and which have been tentatively designed Y. intermedia. When tested by the "lawn-spotting" technique at 25 and 37 degrees C, 7 of 15 Y. intermedia strains produced a bacteriocin only at 25 degrees C with a uniform spectrum of activity against 2 strains of Y. enterocolitica, 1 rhamnose-positive, raffinose-negative, melibiose-negative strain tentatively designated Y. frederiksenii, 8 Y. intermedia, and 3 sucrose- and acetylmethylcarbinol-negative yersinial isolates tested. Bacteriocin-like activity was not detected among the Y. enterocolitica, Y. frederiksenii, or sucrose-negative yersinial strains tested. The exclusive activity of the Y. intermedia antibacterial substance only against yersiniae and not against other representative Enterobacteriaceae tested supports the placement of these microorganisms within the genus Yersinia and further establishes the singularity of Y. intermedia.

Bacteriocins↗

PubMed1983

Comparison of two methods for bacteriocin typing of Serratia marcescens.

Two methods of bacteriocin susceptibility typing for Serratia marcescens were compared. A total of 80 epidemiologically unrelated isolates from patients in a single hospital were typed by the cross-streaking method and the mitomycin C-induced (spotting) method. The cross-streaking method was found to be more discriminatory than the spotting method. Using the cross-streaking method, it was possible to differentiate 50 bacteriocin groups out of the 80 isolates, whereas only 31 groups could be obtained with the spotting method. The reproducibility and percentage typability of the cross-streaking method (82.5 and 93.75%, respectively) were found to be as good as, if not better than, those of the spotting method (78.75 and 90.0%, respectively). Other factors, such as lower economic cost, technical simplicity, and the relative ease in the scoring of results, indicate a preference for the cross-streaking method. The findings of this study support the choice of the cross-streaking method for the bacteriocin typing of S. marcescens in epidemiological studies.

Bacteriocins↗

PubMed1984

Production of bacteriocin-like inhibitors by group A streptococci of nephritogenic M types.

Application of a bacteriocin-typing scheme that had been designed to minimize the inhibitory effects of hydrogen peroxide and acidic metabolites demonstrated a high incidence (72%) of bacteriocin-like inhibitors belonging to 5 different production (P) types in 61 strains of group A streptococci isolated in association with the development of acute glomerulonephritis. By contrast, only 4 of 16 (25%) rheumatic fever-associated strains were inhibitor positive, and 3 of these strains were P type 604, a P type not detected in any of the nephritis isolates. The P type designation was found to be identical for all inhibitor-positive strains within each particular M serotype, regardless of whether the source was a nephritis patient or an individual having an uncomplicated streptococcal infection. The incidence of inhibitor-positive strains was particularly high in strains of M types 2, 4, 12, 25, 57, and 60; it was moderately high in M types 49, 52, and 55 and absent in M1 and M3. Although the results indicate that the bacteriocin-like inhibitors detected in this study are probably unlikely to have a direct pathogenetic role in either rheumatic fever or acute glomerulonephritis, it does seem that the present P-typing scheme is a useful epidemiological tool, particularly for the presumptive identification of and differentiation among group A streptococcus strains of nephritogenic serotypes.

Aerobiosis↗

PubMed1976

Isolation and characterization of a bacteriocin produced by Bacillus stearothermophilus strain NU-10.

Broth-grown cultures of Bacillus stearothermophilus strain NU-10 produce a bacteriocin which exerts lethal activity on other strains of the bacterium. Optimal production occurs during late maximum stationary phase of growth, at neutral pH, and 55-65 degrees C. The bacteriocin can be substantially purified by a combination of precipitations, centrifugations, and gel filtrations. The thermocin is composed of protein and carbohydrate. It is partially destroyed by proteolytic enzymes but is resistant to DNase, RNase, and various chemical treatments. The bacteriocin has a small molecular weight and exhibits considerable thermostability.

Bacterial Proteins↗