Co-transfer of two plasmids determining bacteriocin production and sucrose utilization in Streptococcus faecium

Reichelt, T.

doi:10.1016/0378-1097(84)90197-6

Cited by 4 publications

(4 citation statements)

References 9 publications

(14 reference statements)

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“…According to Bradley's (1976) classification of bacteriocins, the substance produced by strain CCM4231 may be considered to be a low molecular weight bacteriocin. Reichelt et al (1984) reported plasmidencoded bacteriocin production in Streptococcus (Enterococcus) faecium; however, it was a human isolate. Recently, a study was published also about plasmid-associated bacteriocin production in Lactobacillus sake (Mordvedt and Nes 1990).…”

Section: Resultsmentioning

confidence: 99%

Detection and antimicrobial spectrum of a bacteriocin-like substance produced by Enterococcus faecium CCM4231

Lauková

Mareková

Javorský

1993

Lett Appl Microbiol

102

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Section: Resultsmentioning

confidence: 99%

Detection and antimicrobial spectrum of a bacteriocin-like substance produced by Enterococcus faecium CCM4231

Lauková

Mareková

Javorský

1993

Lett Appl Microbiol

102

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“…The strain E. faecalis EJ97 (Sm s ) was used as a donor in mating experiments with the plasmid-free strain E. faecalis OG1X (Sm r ) by the filter method as described elsewhere (43). Transconjugants were selected on BHI agar plates containing streptomycin (final concentration, 500 g/ml) and tested for the ability to produce bacteriocin.…”

Section: Methodsmentioning

confidence: 99%

The Genes Coding for Enterocin EJ97 Production by Enterococcus faecalis EJ97 Are Located on a Conjugative Plasmid

Sánchez‐Hidalgo

Maqueda

Gálvez

et al. 2003

Appl Environ Microbiol

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Enterococcus faecalis EJ97 produces a cationic bacteriocin (enterocin EJ97) of low molecular mass (5,327.7 Da). The complete amino acid sequence of enterocin EJ97 was elucidated after automated microsequencing of oligopeptides generated by endoproteinase GluC digestion and cyanogen bromide treatment. Transfer of the 60-kb conjugative plasmid pEJ97 from the bacteriocinogenic strain E. faecalis EJ97 to E. faecalis OG1X conferred bacteriocin production and resistance on the recipient. The genetic determinants of enterocin EJ97 were located in an 11.3-kb EcoRI-BglII DNA fragment of pEJ97. This region was cloned and sequenced. It contains the ej97A structural gene plus three open reading frames (ORFs) (ej97B, ej97C, and ej97D) and three putative ORFs transcribed in the opposite direction (orfA, orfB, and orfC). The gene ej97A translated as a 44-amino-acid residue mature protein lacking a leader peptide with no homology to other bacteriocins described so far. The product of ej97B (Ej97B) shows strong homology in its C-terminal domain to the superfamily of bacterial ATP-binding cassette transporters. The products of ej97C (Ej97C) and ej97D (Ej97D) could be proteins with 71 and 64 residues, respectively, of unknown functions and with no significant similarity to known proteins. There are two additional ORFs (ORF1 and ORF6) flanking the ej97 module, which have been identified as a transposon-like structure (tnp). ORF1 shows similarities to transposase of the Lactococcus lactis element ISS1 and is up to 50% identical to IS1216. This is flanked by two 18-bp inverted repeats (IRs) that are almost identical to those of ISS1 and IS1216. ORF6 (resEJ97) shows strong homology to the resolvase of plasmid pAM373 and up to 40 to 50% homology with the recombinase of several multiresistant plasmids and transposons from Staphylococcus aureus and E. faecalis. These data suggest that EJ97 could represent a new class of bacteriocins with a novel secretion mechanism and that the whole structure could be a composite transposon. Furthermore, two additional gene clusters were found: one cluster is probably related to the region responsible for the replication of plasmid pEJ97, and the second cluster is related to the sex pheromone response. These regions showed a high homology to the corresponding regions of the conjugative plasmids pAM373, pPD1, and pAD1 of E. faecalis, suggesting that they have a common origin.

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“…Filter mating experiments were done as described by Reichelt et al (29). An overnight culture (0.25 ml) of E. faecalis BFE 1071 and FA2-2 was added to 4. was placed onto an MRS agar plate and incubated overnight at 37°C.…”

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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

109

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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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Co-transfer of two plasmids determining bacteriocin production and sucrose utilization in Streptococcus faecium

Cited by 4 publications

References 9 publications

Detection and antimicrobial spectrum of a bacteriocin-like substance produced by Enterococcus faecium CCM4231

Detection and antimicrobial spectrum of a bacteriocin-like substance produced by Enterococcus faecium CCM4231

The Genes Coding for Enterocin EJ97 Production by Enterococcus faecalis EJ97 Are Located on a Conjugative Plasmid

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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