Purification, partial characterisation and mode of action of enterococcin EFS2, an antilisterial bacteriocin produced by a strain of Enterococcus faecalis isolated from a cheese

Maisnier‐Patin, Sophie; Forni, Emilia; Richard, Jean

doi:10.1016/0168-1605(96)00950-6

Cited by 80 publications

(46 citation statements)

References 31 publications

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“…Similarly, refrigeration temperatures also gave rise to a reduction in antibacterial activity. The reduced activity at low temperatures could be attributed to changes in fatty acid composition and fluidity of bacterial cell membranes (35) or to changes in AMP solubility (36). Regarding the effects of sodium and calcium salts, their addition to the medium at concentrations of up to 3% completely abolished the antibacterial activity of the ␣ s2 -casein f(193-207) peptide.…”

Section: Discussionmentioning

confidence: 99%

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Álvarez‐Ordóñez

Begley

Clifford

et al. 2013

Appl Environ Microbiol

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Section: Discussionmentioning

confidence: 99%

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Álvarez‐Ordóñez

Begley

Clifford

et al. 2013

Appl Environ Microbiol

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“…In other cases, the size of the pores may increase, thus allowing the subsequent release of larger molecules such as amino acids and even ATP (Gonza! lez et al, 1996 ;Zajdel et al, 1985 ;Maisnier-Patin et al, 1996).…”

Section: Introductionmentioning

confidence: 99%

Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci

2000

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Addition of lactococcin 972 to exponentially growing sensitive cultures of Lactococcus lactis resulted in cell elongation and widening. Thin sections revealed that septum invagination was blocked. Cell growth progressed until most cells showed equatorial constriction and even initial deposition of material at the septum ring, although cell division did not proceed any further. The increase in the incorporation of labelled precursors into the cell wall shifted from an exponential to a linear mode in treated cultures, subsequently being arrested. Gross degeneration of the cells was observed prior to cell death, followed by slow lysis of the culture. In contrast, stationary-phase cultures remained unaffected.

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“…Class II bacteriocins are unmodified, heat-stable, low-molecular-mass (Ͻ10-kDa), membrane-active peptides, usually characterized by a G-G-Xaa where Xaa is any amino acid, processing site, in the bacteriocin precursor. The class II bacteriocins are divided into three subgroups; IIa comprises peptides that contain a Y-G-N-G-V-Xaa-C motif near their N termini (Listeria-active peptides), e.g., pediocin PA-1 (22) and sakacin A (12); IIb comprises twopeptide bacteriocins, e.g., lactococcin G (25) and brochocin-C (23); and IIc comprises thiol-activated peptides, which require reduced cysteine residues for activity, e.g., lactococcin B (39).To date, six bacteriocins of Enterococcus faecalis have been described (7,10,17,19,34,35,40), of which only three types have been biochemically and genetically characterized. A hemolysin/bacteriocin, encoded on a 58-kbp conjugative plasmid (pAD1) and originally isolated from Enterococcus faecalis subsp.…”

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confidence: 99%

Characterization and Cloning of the Genes Encoding Enterocin 1071A and Enterocin 1071B, Two Antimicrobial Peptides Produced by Enterococcus faecalis BFE 1071

Balla¹,

Dicks²,

Toit³

et al. 2000

Appl Environ Microbiol

112

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The pH-neutral cell supernatant of Enterococcus faecalis BFE 1071, isolated from the feces of minipigs in Göttingen, inhibited the growth of Enterococcus spp. and a few other gram-positive bacteria. Ammonium sulfate precipitation and cation-exchange chromatography of the cell supernatant, followed by mass spectrometry analysis, yielded two bacteriocin-like peptides of similar molecular mass: enterocin 1071A (4.285 kDa) and enterocin 1071B (3.899 kDa). Both peptides are always isolated together. The peptides are heat resistant (100°C, 60 min; 50% of activity remained after 15 min at 121°C), remain active after 30 min of incubation at pH 3 to 12, and are sensitive to treatment with proteolytic enzymes. Curing experiments indicated that the genes encoding enterocins 1071A and 1071B are located on a 50-kbp plasmid (pEF1071). Conjugation of plasmid pEF1071 to E. faecalis strains FA2-2 and OGX1 resulted in the expression of two active peptides with sizes identical to those of enterocins 1071A and 1071B. Sequencing of a DNA insert of 9 to 10 kbp revealed two open reading frames, ent1071A and ent1071B, which coded for 39-and 34-amino-acid peptides, respectively. The deduced amino acid sequence of the mature Ent1071A and Ent1071B peptides showed 64 and 61% homology with the ␣ and ␤ peptides of lactococcin G, respectively. This is the first report of two new antimicrobial peptides representative of a fourth type of E. faecalis bacteriocin.Bacteriocins are ribosomally synthesized bacteriostatic or bactericidal proteins and peptides which are produced by a number of gram-positive and gram-negative bacteria. By definition these proteins exhibit a relatively narrow spectrum of antimicrobial activity and are in general active only against bacteria closely related to the producer strain (18). The bacteriocins of lactic acid bacteria were classified by Klaenhammer (18) into four groups. Most of the bacteriocins isolated so far belong to class I or class II. Class I bacteriocins, named lantibiotics, are small (Ͻ5-kDa) membrane-active peptides which contain posttranslationally modified amino acid residues. Nisin is the best-studied lantibiotic (31). Class II bacteriocins are unmodified, heat-stable, low-molecular-mass (Ͻ10-kDa), membrane-active peptides, usually characterized by a G-G-Xaa where Xaa is any amino acid, processing site, in the bacteriocin precursor. The class II bacteriocins are divided into three subgroups; IIa comprises peptides that contain a Y-G-N-G-V-Xaa-C motif near their N termini (Listeria-active peptides), e.g., pediocin PA-1 (22) and sakacin A (12); IIb comprises twopeptide bacteriocins, e.g., lactococcin G (25) and brochocin-C (23); and IIc comprises thiol-activated peptides, which require reduced cysteine residues for activity, e.g., lactococcin B (39).To date, six bacteriocins of Enterococcus faecalis have been described (7,10,17,19,34,35,40), of which only three types have been biochemically and genetically characterized. A hemolysin/bacteriocin, encoded on a 58-kbp conjugative plasmid (pAD1) and origin...

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Purification, partial characterisation and mode of action of enterococcin EFS2, an antilisterial bacteriocin produced by a strain of Enterococcus faecalis isolated from a cheese

Cited by 80 publications

References 31 publications

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci

Characterization and Cloning of the Genes Encoding Enterocin 1071A and Enterocin 1071B, Two Antimicrobial Peptides Produced by Enterococcus faecalis BFE 1071

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Purification, partial characterisation and mode of action of enterococcin EFS2, an antilisterial bacteriocin produced by a strain of Enterococcus faecalis isolated from a cheese

Cited by 80 publications

References 31 publications

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α s2 -Casein f(183–207)

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α s2 -Casein f(183–207)

Lactococcin 972, a bacteriocin that inhibits septum formation in lactococci

Characterization and Cloning of the Genes Encoding Enterocin 1071A and Enterocin 1071B, Two Antimicrobial Peptides Produced by Enterococcus faecalis BFE 1071

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Product

Resources

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Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)

Structure-Activity Relationship of Synthetic Variants of the Milk-Derived Antimicrobial Peptide α _s2 -Casein f(183–207)