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Microbiology. 2001 Mar;147(Pt 3):643-651. doi: 10.1099/00221287-147-3-643.

Plantaricin W from Lactobacillus plantarum belongs to a new family of two-peptide lantibiotics.

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Norwegian Dairies Association, Centre for Research and Development, Oslo, Norway2.
Laboratory of Microbial Gene Technology, Department of Chemistry and Biotechnology, Agricultural University of Norway, PO Box 5051, N-1432 Ås, Norway1.
Department of Food Science and Technology, 240 Wiegand Hall, Oregon State University, Corvallis, OR 97331, USA3.
Department of Immunology, Institute for Cell Biology, University of Tübingen, Auf der Morgenstelle 15, D-72076 Tübingen, Germany4.


Plantaricin W (Plw) is a new two-peptide bacteriocin, from Lactobacillus plantarum, which inhibits a large number of Gram-positive bacteria. The two peptides, Plwalpha (comprising 29 residues) and Plwbeta (comprising 32 residues), were isolated from the culture supernatants and characterized. The individual peptides had low antimicrobial activity but acted synergistically, and synergism was seen at all mixing ratios tested. The data indicate that the two peptides work in a 1:1 ratio. Chemical analyses showed that both peptides are lantibiotics, but two unmodified cysteines and one serine residue were present in Plwalpha, and Plwbeta contained one cysteine residue. The Plw structural genes were sequenced and shown to encode prepeptides with sequence similarities to two other two-peptide lantibiotics, namely staphylococcin C55 and lacticin 3147. The conserved residues are mainly serines, threonines and cysteines that can be involved in intramolecular thioether bond formation in the C-terminal parts of the molecules. This indicates that these bacteriocins are members of a new family of lantibiotics with common bridging patterns, and that the ring structures play an important functional role. Based on the data a structural model is presented in which each peptide has a central lanthionine and two overlapping thioether bridges close to their C-termini.

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