Antibiosis among Lactobacilli

Klerk, H. C. De; Coetzee, J. N.

doi:10.1038/192340a0

Cited by 58 publications

(23 citation statements)

References 3 publications

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“…Similar to lactocin 27 (24,25) and the L. fermenti bacteriocin (3)(4)(5), activity was restricted to members of the family Lactobacilliaceae. Purified lactacin B showed activity against L. leichmannii, L. helveticus, L. lactis, and L. bulgaricus.…”

Section: Resultsmentioning

confidence: 99%

“…Although numerous bacteriocins from other bacterial genera have been isolated and characterized (10,18,20,27), few have been studied extensively in the lactobacilli. 4,5) and Upreti and Hinsdill (24,25) identified and characterized bacteriocins produced by Lactobacillusfermentum and L. helveticus, respectively. In crude form both compounds were nondialyzable, heat stable, insensitive to catalase, sensitive to proteolytic enzymes, and inhibited only members of the family Lactobacilliaceae.…”

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confidence: 99%

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Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B

Barefoot¹,

Klaenhammer²

1984

Antimicrob Agents Chemother

221

148

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Parameters for production and purification of a bacteriocin produced by Lactobacillus acidophilus N2 are described. Production of lactatin B was pH dependent, with maximum activity detected in broth cultures maintained at pH 6. Lactacin B was purified by ion-exchange chromatography, ultrafiltration, and successive gel filtrations in the presence of 8 M urea and then 0.1% sodium dodecyl sulfate. The molecular weight of lactacin B was ca. 6,000 to 6,500, and the purified compound showed maximum absorbance at 211 nm. The activity of purified lactacin B was bactericidal to sensitive cells and restricted to members of the family Lactobacilliaceae, L. keichmannii, L. bulgaricus, L. helveticus, and L. lactis. Characteristics identified for lactacin B indicated that it was a peptide and confirmed its identity as a bacteriocin.Bacteriocins are antagonistic proteins or peptides that show bactericidal activity against closely related species (23). Although numerous bacteriocins from other bacterial genera have been isolated and characterized (10,18,20,27), few have been studied extensively in the lactobacilli. 4,5) and Upreti and Hinsdill (24,25) identified and characterized bacteriocins produced by Lactobacillusfermentum and L. helveticus, respectively. In crude form both compounds were nondialyzable, heat stable, insensitive to catalase, sensitive to proteolytic enzymes, and inhibited only members of the family Lactobacilliaceae. Upon subsequent purification, both bacteriocins were identified as large lipopolysaccharide protein complexes of ca. 200,000 in molecular weight. Because the L. fermenti bacteriocin could not be dissociated without loss of activity, DeKlerk and Smit (5) concluded that the complex molecule was essential for activity. Chromatography of the L. helveticus bacteriocin in the presence of sodium dodecyl sulfate (SDS) showed that the active moiety was a glycoprotein with a molecular weight of 12,400 (24).We reported previously that a bacteriocin-like antagonist was produced when L. acidophilus N2 was propagated anaerobically in agar cultures (1). Crude preparations of lactacin B were stable at 100°C for 60 min, insensitive to catalase, sensitive to protease, and bactericidal to sensitive species. In contrast to recent reports of bacteriocin-type compounds that are produced by lactobacilli and antagonize Clostridium (13), Neisseria (16) compound showed that lactacin B was a peptide with 'actericidal activity against the four indicator species. MATERIALS AND METHODSCultures and media. The bacteriocin producer L. acidophilus N2, the sensitive indicator L. leichmannii 4797, and all other cultures used in this study were described previously (1). Lactobacilli were maintained as frozen stocks at -76°C (9) and propagated twice (1% inoculum) through MRS broth (Difco Laboratories, Detroit, Mich.) for 14 to 16 h at 37°C before experimental use.Liquid media used were either MRS broth or a semidefined medium. The basal semi-defined medium included (per liter of solution) Casitone (Difco), 10 g; sodium acetate, 5 g;...

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Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B

Barefoot¹,

Klaenhammer²

1984

Antimicrob Agents Chemother

221

148

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“…Previous investigators have described an antibacterial substance elaborated by certain L. acidophilus strains (4,7,11,15,16,18). Although incompletely characterized, this substance seems to be active principally against other lactobacilli.…”

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confidence: 99%

Antimicrobial substance from a human Lactobacillus strain

Silva¹,

Jacobus²,

Deneke³

et al. 1987

Antimicrob Agents Chemother

500

260

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Lactobacillus sp. strain GG, which was isolated from the feces of a normal person, produced a substance with potent inhibitory activity against a wide range of bacterial species. It inhibited anaerobic bacteria (Clostridium spp., Bacteroides spp., Bifidobacterium spp.), members of the family Enterobacteriaceae, Pseudomonas spp. Staphylococcus spp., and Streptococcus spp., as demonstrated by a microbiological assay; however, it did not inhibit other lactobacilli. The inhibitory activity occurred between pH 3 and 5 and was heat stable. Bactericidal activity against Escherichia coli was demonstrated at a dilution of 1:128. The inhibitory substance was distinct from lactic and acetic acids. It had a low molecular weight (less than 1,000) and was soluble in acetone-water (10:1). Because of these characteristics, the inhibitory material could not be considered a bacteriocin; it most closely resembled a microcin, which has been associated previously with members of the family Enterobacteriaceae.

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“…Among the gram-positive bacteria, bacteriocins are produced by many lactic acid bacteria (LAB) used in food fermentations and dairy products, including lactobacilli, lactococci, and pediococci (29). Lactobacilli are especially known for their bacteriocinogenic properties (4,11,41). Barefoot and Klaenhammer (4) reported that 63% of the Lactobacillus acidophilus strains they examined produced bacteriocins.…”

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Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp

1991

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Lactacin F is a heat-stable bacteriocin produced by Lactobacillus acidophilus 11088. A 63-mer oligonucleotide probe deduced from the N-terminal lactacin F amino acid sequence was used to clone the putative laf structural gene from plasmid DNA of a lactacin F-producing transconjugant, L. acidophilus T143. One clone, NCK360, harbored a recombinant plasmid, pTRK160, which contained a 2.2-kb EcoRI fragment of the size expected from hybridization experiments. An Escherichia coli-L. acidophilus shuttle vector was constructed, and a subclone (pTRK162) containing the 2.2-kb EcoRI fragment was introduced by electroporation into two lactacin F-negative strains, L. acidophilus 89 and 88-C. Lactobacillus transformants containing pTRK162 expressed lactacin F activity and immunity. Bacteriocin produced by the transformants exhibited an inhibitory spectrum and heat stability identical to those of the wild-type bacteriocin. An 873-bp region of the 2.2-kb fragment was sequenced by using a 20-mer degenerate lactacin F-specific primer to initiate sequencing from within the lactacin F structural gene. Analysis of the resulting sequence identified an open reading frame which could encode a protein of 75 amino acids. The 25 N-terminal amino acids for lactacin F were identified within the open reading frame along with an N-terminal extension, possibly a signal sequence. The lactacin F N-terminal sequence, through the remainder of the open reading frame (57 amino acids; 6.3 kDa), correlated extremely well with composition analyses of purified lactacin F which also predicted a size of 51 to 56 amino acid residues. Molecular characterization of lactacin F identified a small hydrophobic peptide that may be representative of a common bacteriocin class in lactic acid bacteria.

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Antibiosis among Lactobacilli

Cited by 58 publications

References 3 publications

Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B

Purification and characterization of the Lactobacillus acidophilus bacteriocin lactacin B

Antimicrobial substance from a human Lactobacillus strain

Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp

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