Bacteriocins of gram-positive bacteria.

Jack, Ralph W.; Tagg, John; Ray, Bibek

doi:10.1128/mmbr.59.2.171-200.1995

Cited by 1,118 publications

(725 citation statements)

References 161 publications

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“…Recent work showed that de-energized S. bovis cells that had been loaded with potassium and diluted into a bu¡er lacking potassium had a slow rate of potassium e¥ux, indicating that the potassium/proton symporters did not act reversibly to catalyze a rapid rate of potassium e¥ux [10]. However, it has long been recognized that potassium e¥ux from bacterial cells can be facilitated by ionophores like valinomycin, nigericin and monensin [11] or by bacteriocins [7].…”

Section: Discussionmentioning

confidence: 99%

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The binding and degradation of nisin by mixed ruminal bacteria

Lee¹

2002

FEMS Microbiology Ecology

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We found that nisin catalyzed potassium efflux from glycolyzing Streptococcus bovis JB1 cell suspensions and that the steady state concentration of residual potassium was dependent upon the amount of nisin added. The relationship between nisin concentration and potassium depletion was a saturation function that had considerable cooperativity. By pre-incubating mixed ruminal bacteria with nisin and removing them prior to S. bovis JB1 addition, it was possible to estimate the ability of mixed ruminal bacteria to bind or degrade nisin. Low concentrations of mixed ruminal bacteria did not bind or degrade all of the nisin in 6 h, but little nisin remained if the mixed ruminal bacteria were present at more than 50 microg protein ml(-1). Because cell-free ruminal fluid (10% v/v) inactivated the nisin in less than 2 h, and this inactivation could be counteracted by autoclaving, ultra-filtration or proteinase inhibitor, it appeared that there was an enzymatic degradation of nisin. Mixed ruminal bacteria degraded nisin rapidly, but this degradation did not prevent potassium depletion from mixed ruminal bacteria. These latter results indicated that nisin binding was faster than nisin degradation. The idea that nisin binding could protect nisin from degradation was supported by the observation that intact nisin could be extracted from mixed ruminal bacteria. These observations support the hypothesis that bacteriocins can be used to modify ruminal fermentation, but further work will be needed to see if these peptides can be produced economically.

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Section: Discussionmentioning

confidence: 99%

“…Ruminal bacteriocins have been proposed as an alternative to feed additives like monensin [5], but the stability of these bacteriocins in a mixed ruminal culture has yet to be determined. Some ruminal bacteria produce peptidases and proteinases [6], and these enzymes have the potential to degrade and inactivate bacteriocins [7].…”

Section: Introductionmentioning

confidence: 99%

The binding and degradation of nisin by mixed ruminal bacteria

Lee¹

2002

FEMS Microbiology Ecology

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“…Bacteriocins produced by Gram-negative bacteria include relatively large proteins; for example, colicins range in size from 449 to 629 amino acids (Riley and Wertz, 2002a). Most bacteriocins from Gram-positive are peptides with typically less than 70 amino acids (Jack et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Diversity and dynamics of bacteriocins from human microbiome

Zheng

Gänzle

Lin

et al. 2014

Environmental Microbiology

106

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Human commensal microbiota are an important determinant of health and disease of the host. Different human body sites harbour different bacterial microbiota, bacterial communities that maintain a stable balance. However, many of the factors influencing the stabilities of bacterial communities associated with humans remain unknown. In this study, we identified putative bacteriocins produced by human commensal microbiota. Bacteriocins are peptides or proteins with antimicrobial activity that contribute to the stability and dynamics of microbial communities. We employed bioinformatic analyses to identify putative bacteriocin sequences in metagenomic sequences obtained from different human body sites. Prevailing bacterial taxa of the putative bacteriocins producers matched the most abundant organisms in each human body site. Remarkably, we found that samples from different body sites contain different density of putative bacteriocin genes, with the highest in samples from the vagina, the airway, and the oral cavity and the lowest in those from gut. Inherent differences of different body sites thus influence the density and types of bacteriocins produced by commensal bacteria. Our results suggest that bacteriocins play important roles to allow different bacteria to occupy several human body sites, and to establish a long-term commensal relationship with human hosts.

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“…Cationic antimicrobial peptides have now been isolated from a wide variety of sources including bacteria, invertebrates, vertebrates and plants [1][2][3][4][5][6][7]. Although their structure and chemical nature differ markedly, their function appears to involve protection of the producing organism from competing or pathogenic micro-organisms, and their activity may be directed towards a variety of bacteria, protozoa, fungi and/or viruses.…”

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confidence: 99%

Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3

Chen

Leung

Thakur

et al. 2003

European Journal of Biochemistry

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Different pathways of bilayer disruption by the structurally related antimicrobial peptides cecropin B, B1 and B3, revealed by surface plasma resonance analysis of immobilized liposomes, differential scanning calorimetry of peptidelarge unilamellar vesicle interactions, and light microscopic analysis of peptide-treated giant unilamellar vesicles, have been identified in this study. Natural cecropin B (CB) has one amphipathic and one hydrophobic a-helix, whereas cecropins B1 (CB1) and B3 (CB3), which are custom-designed, chimaeric analogues of CB, possess either two amphipathic or two hydrophobic a-helices, respectively. Surface plasma resonance analysis of unilamellar vesicles immobilized through a biotin-avidin interaction showed that both CB and CB1 bind to the lipid bilayers at high concentration (>10 lM); in contrast, CB3 induces disintegration of the vesicles at all concentrations tested. Differential scanning calorimetry showed the concentration-dependent effect of bilayer disruption, based on the different thermotrophic phase behaviours and the shapes of the thermal phasetransition curves obtained. The kinetics of the lysis of giant unilamellar vesicles observed by microscopy demonstrated that both CB and CB1 effect a continuous process involving loss of integrity followed by coalescence and resolution into smaller vesicles, whereas CB3 induces rapid formation of irregular-shaped, nonlamellar structures which rapidly disintegrate into twisted, microtubule-containing debris before being completely destroyed. On the basis of these observations, models by which CB, CB1 and CB3 induce lysis of lipid bilayers are discussed.

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Bacteriocins of gram-positive bacteria.

Cited by 1,118 publications

References 161 publications

The binding and degradation of nisin by mixed ruminal bacteria

The binding and degradation of nisin by mixed ruminal bacteria

Diversity and dynamics of bacteriocins from human microbiome

Distinguishing between different pathways of bilayer disruption by the related antimicrobial peptides cecropin B, B1 and B3

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