Bacteriocins: mechanism of membrane insertion and pore formation

Moll, Gert N.; Konings, Wil N.; Driessen, Arnold J.M.

doi:10.1007/978-94-017-2027-4_8

Cited by 115 publications

(166 citation statements)

References 40 publications

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“…Moreover synergistic effects were reported when the interactions between pairs of bacteriocins from lactic acid bacteria were tested which are in accordance with the results obtained by MulletPowell et al (1998) One possible explanation for the different effectiveness of bacteriocin pairs would be that the bacteriocins used in this study belonged to different classes, which vary considerably in the nature and sequence of amino acid residues as earlier suggested by Moll et al (1999). The synergistic action of combinations of two different bacteriocins with different structures produced by the same strain has also been reported in agar medium by Limonet et al (2004).…”

Section: Kinetics Of Cell Growth Inhibition By Bacteriocinssupporting

confidence: 92%

Antibacterial efficacy of nisin, pediocin 34 and enterocin FH99 against L. monocytogenes, E. faecium and E. faecalis and bacteriocin cross resistance and antibiotic susceptibility of their bacteriocin resistant variants

et al. 2011

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The bacteriocin susceptibility of Listeria monocytogenes MTCC 657, Enterococcus faecium DSMZ 20477, E. faecium VRE, and E. faecalis ATCC 29212 and their corresponding bacteriocin resistant variants was assessed. The single and combined effect of nisin and pediocin 34 and enterocin FH99 bacteriocins produced by Pediococcus pentosaceus 34, and E. faecium FH99, respectively, was determined. Pediocin34 proved to be more effective in inhibiting L. monocytogenes MTCC 657. A greater antibacterial effect was observed against E. faecium DSMZ 20477 and E. faecium (VRE) when the a combination of nisin, pediocin 34 and enterocin FH99 were used whereas in case of L. monocytogenes MTCC 657 a combination of pediocin 34 and enterocin FH99 was more effective in reducing the survival of pathogen. Bacteriocin cross-resistance and the antibiotic susceptibility of wild type and their corresponding resistant variants were assessed and results showed that resistance to a bacteriocin may extend to other bacteriocins within the same class and also the acquired resistance to bacteriocins can modify the antibiotic susceptibility/resistance profile of the bacterial species used in the study. According to the hydrophobicity nisin resistant variant of L. monocytogenes was more hydrophobic (p<0.001), whereas the pediocin 34 and enterocin FH99 resistant variants were less hydrophobic than the wild type strain. Nisin, pediocin 34 and enterocin FH99 resistant variants of E. faecium DSMZ 20477 and E. faecium VRE were less hydrophobic than their wild type counterparts. Nisin resistant E. faecalis ATCC 29212 was less hydrophobic than its wild type counterpart.

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Section: Kinetics Of Cell Growth Inhibition By Bacteriocinssupporting

confidence: 92%

Antibacterial efficacy of nisin, pediocin 34 and enterocin FH99 against L. monocytogenes, E. faecium and E. faecalis and bacteriocin cross resistance and antibiotic susceptibility of their bacteriocin resistant variants

et al. 2011

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“…As one of the major action mechanisms, hydrophobic and low-molecular-weight bacteriocins cause efflux of low-molecular-weight components such as ATP and cations by pore formation in the cytoplasmic membrane, resulting in depolarization of the cytoplasmic membrane to cause death of the indicator cell (21). No ATP efflux from the indicator cells of L. delbrueckii subsp.…”

Section: Vol 70 2004 Differences In Two Cyclic Bacteriocins 2909mentioning

confidence: 99%

“…These components from lactic acid bacteria (LAB) have been classified into four classes, I to IV (16,25). Recently, many class II bacteriocins, small hydrophobic peptides that do not contain modified amino acids such as lanthiothine, have been reported, and they have been divided into the categories IIa, IIb, IIc, and IId (21,25). These LAB bacteriocins and the producing strains isolated from humans and foods are expected to be food preservatives and probiotics for preventing the growth of harmful bacteria in food and the human intestine.…”

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confidence: 99%

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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“…A dominant and important group of these bacteriocins consists of the pediocin-like bacteriocins produced by lactic acid bacteria (LAB) (12,22,26). The pediocin-like bacteriocins are cationic, display antilisteria activity, and kill target cells by permeabilizing the cell membrane (8,21). They all contain between 37 and 48 residues, and they have very similar primary structures.…”

mentioning

confidence: 99%

Structure-Function Analysis of Immunity Proteins of Pediocin-Like Bacteriocins: C-Terminal Parts of Immunity Proteins Are Involved in Specific Recognition of Cognate Bacteriocins

Johnsen

Fimland

Mantzilas

et al. 2004

Appl Environ Microbiol

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The immunity proteins of pediocin-like bacteriocins show a high degree of specificity with respect to the pediocin-like bacteriocin they recognize and confer immunity to. The aim of this study was to identify regions of the immunity proteins that are involved in this specific recognition. Six different hybrid immunity proteins were constructed from three different pediocin-like bacteriocin immunity proteins that have similar sequences but confer resistance to different bacteriocins. These hybrid immunity proteins were then tested for their ability to confer immunity to various pediocin-like bacteriocins. The specificities of the hybrid immunity proteins proved to be similar to those of the immunity proteins from which the C-terminal halves were derived, thus revealing that the C-terminal half of immunity proteins for pediocin-like bacteriocins contains a domain that is involved in specific recognition of the bacteriocins they confer immunity to. Moreover, the results also revealed that the effectiveness of an immunity protein is strain dependent and that its functionality thus depends in part on interplay with strain-dependent factors. To further investigate the structure-function relationship of these immunity proteins, the enterocin A and leucocin A immunity proteins (EntA-im and LeuA-im) were purified to homogeneity and structurally analyzed under various conditions by Circular dichroism (CD) spectroscopy. The results revealed that both immunity proteins are ␣-helical and well structured in an aqueous environment, the denaturing temperature being 78.5°C for EntA-im and 58.0°C for LeuA-im. The CD spectra also revealed that there was no further increase in the structuring or ␣-helical content when the immunity proteins were exposed to dodecylphosphocholine micelles or dioleoyl-L-␣-phosphatidyl-DL-glycerol (DOPG) liposomes, indicating that the immunity proteins, in contrast to the bacteriocins, do not interact extensively with membranes. They may nevertheless be loosely associated with the membrane, possibly as peripheral membrane proteins, thus enabling them to interact with their cognate bacteriocin.

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Bacteriocins: mechanism of membrane insertion and pore formation

Cited by 115 publications

References 40 publications

Antibacterial efficacy of nisin, pediocin 34 and enterocin FH99 against L. monocytogenes, E. faecium and E. faecalis and bacteriocin cross resistance and antibiotic susceptibility of their bacteriocin resistant variants

Antibacterial efficacy of nisin, pediocin 34 and enterocin FH99 against L. monocytogenes, E. faecium and E. faecalis and bacteriocin cross resistance and antibiotic susceptibility of their bacteriocin resistant variants

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

Structure-Function Analysis of Immunity Proteins of Pediocin-Like Bacteriocins: C-Terminal Parts of Immunity Proteins Are Involved in Specific Recognition of Cognate Bacteriocins

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