Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071
dc.contributor.author | Balla E. | |
dc.contributor.author | Dicks L.M.T. | |
dc.contributor.author | Du Toit M. | |
dc.contributor.author | Van Der Merwe M.J. | |
dc.contributor.author | Holzapfel W.H. | |
dc.date.accessioned | 2011-05-15T15:56:34Z | |
dc.date.available | 2011-05-15T15:56:34Z | |
dc.date.issued | 2000 | |
dc.description.abstract | The pH-neutral cell supernatant of Enterococcus faecalis BFE 1071, isolated from the feces of minipigs in Gottingen, 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 α and β peptides of lactococcin G, respectively. This is the first report of two new antimicrobial peptides representative of a fourth type of E. faecalis bacteriocin. | |
dc.description.version | Article | |
dc.identifier.citation | Applied and Environmental Microbiology | |
dc.identifier.citation | 66 | |
dc.identifier.citation | 4 | |
dc.identifier.issn | 992240 | |
dc.identifier.other | 10.1128/AEM.66.4.1298-1304.2000 | |
dc.identifier.uri | http://hdl.handle.net/10019.1/9919 | |
dc.subject | antiinfective agent | |
dc.subject | bacteriocin | |
dc.subject | enterocin 1071a | |
dc.subject | enterocin 1071b | |
dc.subject | lactococcin | |
dc.subject | peptide derivative | |
dc.subject | unclassified drug | |
dc.subject | amino acid sequence | |
dc.subject | article | |
dc.subject | bacterial growth | |
dc.subject | bacterium conjugation | |
dc.subject | drug isolation | |
dc.subject | Enterococcus faecalis | |
dc.subject | gene location | |
dc.subject | genetic analysis | |
dc.subject | heat tolerance | |
dc.subject | molecular cloning | |
dc.subject | nonhuman | |
dc.subject | nucleotide sequence | |
dc.subject | open reading frame | |
dc.subject | pH | |
dc.subject | plasmid | |
dc.subject | sequence homology | |
dc.subject | Amino Acid Sequence | |
dc.subject | Bacterial Proteins | |
dc.subject | Bacteriocins | |
dc.subject | Base Sequence | |
dc.subject | Cloning, Molecular | |
dc.subject | Conjugation, Genetic | |
dc.subject | Enterococcus faecalis | |
dc.subject | Genes, Bacterial | |
dc.subject | Gram-Positive Bacteria | |
dc.subject | Heat | |
dc.subject | Hydrogen-Ion Concentration | |
dc.subject | Molecular Sequence Data | |
dc.subject | Peptide Hydrolases | |
dc.subject | Plasmids | |
dc.subject | Sequence Analysis, DNA | |
dc.subject | Bacteria (microorganisms) | |
dc.subject | Enterococcus faecalis | |
dc.subject | Posibacteria | |
dc.subject | Prokaryota | |
dc.title | Characterization and cloning of the genes encoding enterocin 1071A and enterocin 1071B, two antimicrobial peptides produced by Enterococcus faecalis BFE 1071 | |
dc.type | Article |