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

Muriana, Peter M.; Klaenhammer, Todd R.

doi:10.1128/jb.173.5.1779-1788.1991

Cited by 142 publications

(113 citation statements)

References 43 publications

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“…A novel excretion mechanism in this group of bacteria may account for these differences from the expected structure of signal peptides (14). The four amino acids adjacent to the clevage site in the C region (Val-ValGly-Gly) are identical to those of the leader peptide of the lacEF gene of Lactobacillus aCidophilus (29).…”

Section: Resultsmentioning

confidence: 99%

“…The structural gene encoding helveticin J produced by Lactobacillus helveticus 481 has been cloned, sequenced, and expressed in Lactobacillus acidophilus (19). Also, the structural gene encoding lactacin F produced by Lactobacillus acidophilus has been cloned; DNA sequence analysis elucidated a 75-amino-acid precursor bacteriocin consisting of a 57-residue bacteriocin and an 18-residue leader peptide (28,29).…”

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confidence: 99%

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Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum

et al. 1991

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Leucocin A-UAL 187 is a bacteriocin produced by Leuconostoc gelidum UAL 187, a lactic acid bacterium isolated from vacuum-packaged meat. The bacteriocin was purified by ammonium sulfate or acid (pH 2.5) precipitation, hydrophobic interaction chromatography, gel filtration, and reversed-phase high-performance liquid chromatography with a yield of 58% of the original activity. Leucocin A is stable at low pH and heat resistant, and the activity of the pure form is enhanced by the addition of bovine serum albumin. It is inactivated by a range of proteolytic enzymes. The molecular weight was determined by mass spectrometry to be 3,930.3 0.4. Leucocin A-UAL 187 contains 37 amino acids with a calculated molecular weight of 3,932.3. A mixed oligonucleotide (24-mer) homologous to the sequence of the already known N terminus of the bacteriocin hybridized to a 2.9-kb HpaII fragment of a 7.6-MDa plasmid from the producer strain. The fragment was cloned into pUC118 and then subcloned into a lactococcal shuttle vector, pNZ19. DNA sequencing revealed an operon consisting of a putative upstream promoter, a downstream terminator, and two open reading frames flanked by a putative upstream promoter and a downstream terminator. The first open reading frame downstream of the promoter contains 61 amino acids and is identified as the leucocin structural gene, consisting of a 37-amino-acid bacteriocin and a 24-residue N-terminal extension. No phenotypic expression of the bacteriocin was evident in several lactic acid bacteria that were electrotransformed with pNZ19 containing the 2.9-kb cloned fragment of the leucocin A plasmid.Bacteriocins are antimicrobial peptides or proteins formed by bacteria. The potential applications for bacteriocin-producing lactic acid bacteria in food preservation has stimulated interest in the characterization of these substances. However, maintaining activity during isolation and purification has proved difficult, and the full or partial amino acid sequences of only five such bacteriocins have been reported. The most extensively studied is nisin A (2, 3, 7, 34), a posttranslationally modified bacteriocin from Lactococcus lactis subsp. lactis. Nisin has been approved for use as a preservative in foods in over 45 countries (9). It is ribosomally synthesized (6, 10) and is one of a group of lantibiotics that possess lanthionine-or methyllanthionine-containing rings resulting from the attack of cysteine sulfhydryl groups on dehydroalanine or dehydrobutyrine residues (derived from serine or threonine). Partial characterization of lactacin 481 from L. lactis shows that it also contains lanthionine rings, but the full sequence has not yet been published (31). In contrast, lactocin S from Lactobacillus sake (27)

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Section: Resultsmentioning

confidence: 99%

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Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum

et al. 1991

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“…Hastings et al (1991) have cloned the gene for leucocin A-UAL 187 of Leuconostoc gelidum. The gene of Lactobacillus acidophilus encoding lactacin F has been sequenced by Muriana & Klaenhammer (1991). Two bacteriocins from Lb.…”

Section: Introductionmentioning

confidence: 99%

Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706

Holck¹,

Axelsson²,

Birkeland

et al. 1992

Journal of General Microbiology

195

134

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Sakacin A, a bacteriocin produced by Lactobacillus sake Lb706 and which inhibits the growth of Listeria monocytogenes, was purified to homogeneity by ammonium sulphate precipitation and ion-exchange, hydrophobicinteraction and reversed-phase chromatography. The complete amino acid sequence of sakacin A was determined by Edman degradation. The bacteriocin consisted of 41 amino acid residues and had a calculated Mc of 4308.7, which is in good agreement with the value determined by mass spectrometry. The structural gene encoding sakacin A (sakA) was cloned and sequenced. The gene encoded a primary translation product of 59 amino acid residues which was cleaved between amino acids 18 and 19 to yield the active sakacin A. Sakacin A shared some sequence similarities with other bacteriocins.

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“…This group of bacteria, including L. gasseri, which is found in the human intestine, has been classified on the basis of similarities in rRNA sequences and compositions of the cell walls into six subgroups (9,11,18). Many strains in this group have been shown to be bacteriocin producers (6,12,19,23).…”

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Structural and Functional Differences in Two Cyclic Bacteriocins with the Same Sequences Produced by Lactobacilli

Kawai

Ishii

Arakawa

et al. 2004

Appl Environ Microbiol

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Lactobacillus gasseri LA39 and L. reuteri LA6 isolated from feces of the same human infant were found to produce similar cyclic bacteriocins (named gassericin A and reutericin 6, respectively) that cannot be distinguished by molecular weights or primary amino acid sequences. However, reutericin 6 has a narrower spectrum than gassericin A. In this study, gassericin A inhibited the growth of L. reuteri LA6, but reutericin 6 did not inhibit the growth of L. gasseri LA39. Both bacteriocins caused potassium ion efflux from indicator cells and liposomes, but the amounts of efflux and patterns of action were different. Although circular dichroism spectra of purified bacteriocins revealed that both antibacterial peptides are composed mainly of ␣-helices, the spectra of the bacteriocins did not coincide. The results of D-and L-amino acid composition analysis showed that two residues and one residue of D-Ala were detected among 18 Ala residues of gassericin A and reutericin 6, respectively. These findings suggest that the different D-alanine contents of the bacteriocins may cause the differences in modes of action, amounts of potassium ion efflux, and secondary structures. This is the first report that characteristics of native bacteriocins produced by wild lactobacillus strains having the same structural genes are influenced by a difference in D-amino acid contents in the molecules.

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

Cited by 142 publications

References 43 publications

Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum

Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum

Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706

Structural and Functional Differences in Two Cyclic Bacteriocins with the Same Sequences Produced by Lactobacilli

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