Models and mechanisms for bacteriocin action and application

Montville, Thomas J.; Winkowski, Karen; Ludescher, Richard D.

doi:10.1016/0958-6946(95)00034-8

Cited by 69 publications

(39 citation statements)

References 72 publications

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“…There is increasing interest in the use of bacteriocins from lactic acid bacteria in foods (20,22). For example, the class I bacteriocin nisin was approved for use in 1969 and has been applied to several foods (6).…”

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confidence: 99%

Absence of a Putative Mannose-Specific Phosphotransferase System Enzyme IIAB Component in a Leucocin A-Resistant Strain of Listeria monocytogenes , as Shown by Two-Dimensional Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Ramnath

Beukes

Tamura

et al. 2000

Appl Environ Microbiol

117

102

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Leucocin A is a class IIa bacteriocin produced by Leuconostoc spp. that has previously been shown to inhibit the growth of Listeria monocytogenes. A spontaneous resistant mutant of L. monocytogenes was isolated and found to be resistant to leucocin A at levels in excess of 2 mg/ml. The mutant showed no significant cross-resistance to nontype IIa bacteriocins including nisaplin and ESF1-7GR. However, there were no inhibition zones found on a lawn of the mutant when challenged with an extract containing 51,200 AU of pediocin PA-2 per ml as determined by a simultaneous assay on the sensitive wild-type strain. DNA and protein analysis of the resistant and susceptible strains were carried out using silver-stained amplified fragment length polymorphism (ssAFLP) and one-and two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), respectively. Two-dimensional SDS-PAGE clearly showed a 35-kDa protein which was present in the sensitive but absent from the resistant strain. The N-terminal end of the 35-kDa protein was sequenced and found to have an 83% homology to the mannose-specific phosphotransferase system enzyme IIAB of Streptococcus salivarius.Bacteriocins are proteinaceous antimicrobial peptides synthesized by bacteria and are usually active against strains closely related to the producing organism (13, 21). There is increasing interest in the use of bacteriocins from lactic acid bacteria in foods (20,22). For example, the class I bacteriocin nisin was approved for use in 1969 and has been applied to several foods (6). Class II bacteriocins are characteristically small, heat-stable peptides (15), some of which contain the consensus motif YGNGV and include leucocin A and pediocin PA-2. These were isolated from food-related lactic acid bacteria and have potential as food preservatives. With the addition of nisin (and other bacteriocins) into the environment, there is a concomitant interest in resistance to these antimicrobial compounds (4,5,10,18,19,33). The mechanism of resistance has not been fully established, but has been attributed to cell membrane and S-layer changes.Leucocin A is produced by several Leuconostoc spp. It inhibits the growth of the important potential food-borne pathogen Listeria monocytogenes (11,24). Resistance to class IIa bacteriocins has been reported to be a stable phenomenon (8,30). Transposon-mediated inactivation of 54 in L. monocytogenes has rendered it resistant to mesentericin Y105 (a class IIa bacteriocin) (31). There is, however, very little known about the molecular basis of resistance in naturally isolated strains.In an attempt to discover resistance-associated phenomena at both the DNA and proteiomic levels, amplified fragment length polymorphism (AFLP) and two-dimensional (2-D) gel electrophoresis were employed, respectively. AFLP is a genome fingerprinting technique based on the selective amplification of a subset of DNA fragments generated by restriction enzyme digestion (34). 2-D gel electrophoresis is a powerful tool for the analysis of complex p...

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confidence: 99%

Absence of a Putative Mannose-Specific Phosphotransferase System Enzyme IIAB Component in a Leucocin A-Resistant Strain of Listeria monocytogenes , as Shown by Two-Dimensional Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Ramnath

Beukes

Tamura

et al. 2000

Appl Environ Microbiol

117

102

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“…Enterocin P is a pediocin-like bacteriocin (27) with an N-terminal signal peptide which may allow it to be secreted via the sec pathway (for a review, see reference 30). The enterocin P operon has been previously characterized (11), and it consists of the bacteriocin structural gene (entP) encoding a 71-amino-acid precursor with a 27-amino-acid signal peptide and has a second open reading frame (orf2) located immediately downstream of entP and potentially encoding the immunity protein.The increasing interest of consumers in minimally processed, naturally preserved foods has prompted the proposal to use bacteriocinogenic LAB or their bacteriocins as biopreservatives to increase microbiological safety (19,25,31). However, rational application of the bacteriocins requires an understanding of the mechanisms underlying their specificity and activity (24, 26), as well as knowledge of the structure-function relationships, to develop new compounds with an improved efficacy.…”

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confidence: 99%

Enterocin P Selectively Dissipates the Membrane Potential of Enterococcus faecium T136

Herranz

Chen

Chung

et al. 2001

Appl Environ Microbiol

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Enterocin P is a pediocin-like, broad-spectrum bacteriocin which displays a strong inhibitory activity against Listeria monocytogenes. The bacteriocin was purified from the culture supernatant of Enterococcus faecium P13, and its molecular mechanism of action against the sensitive strain E. faecium T136 was evaluated. Although enterocin P caused significant reduction of the membrane potential (⌬⌿) and the intracellular ATP pool of the indicator organism, the pH gradient (⌬pH) component of the proton motive force (⌬p) was not dissipated. By contrast, enterocin P caused carboxyfluorescein efflux from E. faecium T136-derived liposomes.Bacteriocins produced by bacteria are a heterogeneous group of ribosomally synthesized antimicrobial proteins, which display antimicrobial activity against other bacteria (16,18,29). The genus Enterococcus is among the lactic acid bacteria (LAB) associated with foods that produce bacteriocins (2,4,6,11,12). Enterococcus faecium P13 and other E. faecium strains isolated from dry-fermented sausages produce enterocin P, a bacteriocin with strong inhibitory activity against Listeria monocytogenes (11,14). Enterocin P is a pediocin-like bacteriocin (27) with an N-terminal signal peptide which may allow it to be secreted via the sec pathway (for a review, see reference 30). The enterocin P operon has been previously characterized (11), and it consists of the bacteriocin structural gene (entP) encoding a 71-amino-acid precursor with a 27-amino-acid signal peptide and has a second open reading frame (orf2) located immediately downstream of entP and potentially encoding the immunity protein.The increasing interest of consumers in minimally processed, naturally preserved foods has prompted the proposal to use bacteriocinogenic LAB or their bacteriocins as biopreservatives to increase microbiological safety (19,25,31). However, rational application of the bacteriocins requires an understanding of the mechanisms underlying their specificity and activity (24, 26), as well as knowledge of the structure-function relationships, to develop new compounds with an improved efficacy. In this context, the objective of this study was to examine the mechanistic action of enterocin P on the sensitive strain E. faecium T136. MATERIALS AND METHODSBacterial strains and growth conditions. E. faecium P13 (11) and E. faecium T136 (6) were propagated in MRS broth (Difco Laboratories, Detroit, Mich.) at 30°C and used as the enterocin P producer and indicator microorganisms for bacteriocin activity, respectively.Purification of enterocin P. The bacteriocin was purified from the supernatant of a 16-h E. faecium P13 culture by hydrophobic interaction and cation-exchange chromatographies, basically as described by Casaus et al. (6). Next, the sample was dialyzed against distilled water in dialysis tubing (Spectrum, Houston, Tex.; molecular weight cutoff, 1,000) and concentrated with polyethylene glycol to half of its original volume. This sample was further purified by preparative isoelectric focusing using a Rotofor cel...

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“…Common targets are the cell wall, the cell membrane, protein synthesis or cell division. Inhibition of β-glucan synthesis and inhibition of chitin synthetase are the main mechanisms of compounds that act on the fungal cell wall [41][42][43].…”

Section: Figure 3 Growth Inhibition Of Penicillium Candidum By Ppblsmentioning

confidence: 99%

Extending the Shelf Life of Camembert Cheese via Controlling Over-Ripening by Bacteriocin of Newly Lactic Acid Bacterial Isolate LAB100

Khider¹,

Elbanna²

2017

IJNFS

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Camembert cheese is a surface white mould ripened cheese; when full ripe the casein becomes liquefy as the intensive degradation occurs by proteinases from surface flora and results over-ripening and off flavor. To control this, partial purified bacteriocin like substances (PPBLS) from newly lactic acid bacterial isolate (LAB100) exhibited antifungal activity against Penicillium candidum (in vitro) were used. Inhibition (%) of P. candidum by PPBLS at concentrations of 2, 4, 8, 16 and 32 mg/ml was 34, 50, 79, 80 and 85%, respectively. Based on their superior antifungal potential activity; isolate LAB100 was phenotypically and genotypically characterized as newly Lactobacillus sp. For delaying the Camembert cheese over-ripening (in vivo), bacteriocin producing isolate LAB100 and its PPBLS were incorporated and applied in different camembert cheese treatments. Three treatments beside control were conducted; after brining all cheese treatments stored at 12±2°C to ripen for 12 days and then at 5±2°C for more 30 days to complete ripening. Organoleptic properties, pH values and nitrogen distribution were determined during ripening period. In addition, the proteolysis of treated Camembert cheese was monitored by gel electrophoresis. The cheese treatment (T2) made with bacteriocin producer isolate LAB 100 added as co-culture to main starter recorded the highest total score, followed by T3 and the lowest one was recorded for control (T1). The highest WSN/TN% was in T1; 5. 4, 22.87, 34.41 and 57.65% at 3, 10, 20, and 40 days after brining, respectively, while the lowest WSN/TN% was recorded for treatment that made with both bacteriocin producer strain LAB100 and sprayed by PPBLS solution after 3 days of brining (T3), where it was 5.05, 9.85, 13.82, and 31.74% at the same previous ages, respectively. These results were confirmed by gel electrophoresis, indicating that bacteriocin producer LAB100 and or its bacteriocin controlled the protein degradation. These results suggest that both bacteriocin producer strain and its PPBLS minimize the growth of P. candidum as a consequence the rate of proteolysis was controlled and hence extending the shelf life of Camembert cheese is occurred.

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Models and mechanisms for bacteriocin action and application

Cited by 69 publications

References 72 publications

Absence of a Putative Mannose-Specific Phosphotransferase System Enzyme IIAB Component in a Leucocin A-Resistant Strain of Listeria monocytogenes , as Shown by Two-Dimensional Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Absence of a Putative Mannose-Specific Phosphotransferase System Enzyme IIAB Component in a Leucocin A-Resistant Strain of Listeria monocytogenes , as Shown by Two-Dimensional Sodium Dodecyl Sulfate-Polyacrylamide Gel Electrophoresis

Enterocin P Selectively Dissipates the Membrane Potential of Enterococcus faecium T136

Extending the Shelf Life of Camembert Cheese via Controlling Over-Ripening by Bacteriocin of Newly Lactic Acid Bacterial Isolate LAB100

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