Chemistry: natural resins or derivatives; peptides or proteins; – Peptides of 3 to 100 amino acid residues – 25 or more amino acid residues in defined sequence
Patent
1993-10-07
1997-01-14
Patterson, Jr., Charles L.
Chemistry: natural resins or derivatives; peptides or proteins;
Peptides of 3 to 100 amino acid residues
25 or more amino acid residues in defined sequence
435 713, C07K 14315
Patent
active
055941036
DESCRIPTION:
BRIEF SUMMARY
The invention relates primarily to a number of lantibiotics similar to nisin A, which differ from nisin A by substitution, deletion or insertion of one or more amino acids, and in particular to a naturally occurring but previously unknown analogue of nisin A, termed nisin Z. The invention also relates to lactic acid bacteria which produce these lantibiotics and to a method for constructing such lactic acid bacteria. The invention also relates to a method for preserving foodstuffs for humans and animals with the aid of the lantibiotics in question or of the lactic acid bacteria in question, which produce lantibiotics.
PRIOR ART
Nisin has been described by Mattick and Hirsch [The Lancet (ii) (1947) 5-7] as a group N inhibitory substance having a broad antimicrobial action, produced by Streptococcus lactic (later termed Lactococcus lactis subsp. lactis) strain 354. Further analysis showed that in a nisin preparation produced by this strain [Hirsch, J. Gen. Microbiol. 5 (1951) 208-221] various components, which can be isolated, were found to occur [Hirsch, Nature 67 (1951) 1031-1032] which in a later study were named nisin A-D [Berridge et al., Biochem. J. 52 (1952), 529-335]. The structure of the main component nisin A was determined [Gross and Morell, JACS 93 (1971) 4634-4635] and comprises a pentacyclic 34 amino acid peptide which contains the unusual amino acids lanthionine, .beta.-methyllanthionine, dehydroalanine and .beta.B-methyldehydroalanine. Nisin A, together with a number of other lanthionine-containing peptides, is considered as belonging to the group of lantibiotics [Schnell et al., Nature 333 (1988) 276-278]. It is suggested that nisin A is derived from a ribosomal synthesised precursor polypeptide which contains natural amino acids only and has a higher molecular weight and which is converted into nisin A via a number of post-translational modification reactions of the Ser, Thr and Cys residues [Gross (1977) in Protein cross-linking, pp 131-153, Plenum Press, New York]. This biosynthesis route was confirmed by the cloning and the sequence analysis of the gene for the peptide precursor of nisin A [PCT WO 90/00558; Buchman et al., J. Biol. Chem. 263, (1988) 16260-16266] from L. lactis ATCC 11454 [first named spaN and subsequently named nisA; Kaletta and Entian, J. Bacteriol. 171 (1989) 1597-1601]. It was found from this that the nisA gene codes for a precursor peptide which contains 57 amino acids and consists of two parts: the 23 amino acid N-terminal leader peptide and the 34 amino acid C-terminal structural part. The previously proposed structure for nisin A is in complete agreement with the amino acid sequence derived from the nucleotide sequence of the nisA gene and can be fully explained by post-translational modification reactions of the C-terminal structural part of the peptide precursor. It was found from a subsequent study that only one copy of the gene for nisin production was present in the ATCC 11454 strain used [Donkersloot and Thompson, J. Bacteriol. 172 (1990) 4122-4126]. It was found from this study and also from other analyses [Chan et al., FEBS Letters 252 (1989) 29-36] that the various forms of nisin which can be produced by a single L. lactic strain are degradation products of the main component nisin A or processing intermediates in the formation of nisin A, which may or may not have biological activity. The existence of such intermediates in the case of the biosynthesis of the related lantibiotic Pep5 has recently been demonstrated [Weil et al., Eur. J. Biochem. 194 (1990) 217-223]. The term "nisin" is understood to mean the peptide nisin A derived from the nisA gene and also the processing intermediates derived therefrom and obtained during the biosynthesis, and degradation products of nisin A. A nisA gene with a sequence identical to that described previously was also found to occur in three other L. lactis strains which produced nisin [Kaletta and Entian, see above; Dodd et al., J. Gen. Microbiol. 136 (1990) 555-566; Rauch and de Vos (1990), Third ASM Conference on St
REFERENCES:
patent: 5173297 (1992-12-01), Vedamuthu et al.
patent: 5231165 (1993-07-01), Vedamuthu et al.
N. Schnell et al., "Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings", Nature, vol. 333, May 19, 1988, London, England, pp. 276-278.
Weng C. Chan et al., "Isolation and characteriation of two degradation products derived from the peptide antibiotic nisin", FEBS Letters, vol. 252, No. 1,2, Jul. 1989, pp. 29-36.
E. Broadbent et al., "Genetic construction of nisin producing L. lactis subsp. cremoris and analysis of a rapid method for conjugation", Applied and Environmental Microbiology, vol. 57, No. 2, Feb. 1991, p. 517.
J. W. M. Mulders, "Identification and characterization of the lantibiotic nisin Z, a natural nisin variant", Eur. J. Biochem, vol. 201, No. 3, Nov. 1, 1991, pp. 581-584.
De Vos Willem M.
Kuipers Oscar P.
Siezen Roelant J.
Patterson Jr. Charles L.
Stichting Nederlands Instituut Voor Zuivelonderzoek (NIZO)
LandOfFree
Lantibiotics similar to nisin a does not yet have a rating. At this time, there are no reviews or comments for this patent.
If you have personal experience with Lantibiotics similar to nisin a, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Lantibiotics similar to nisin a will most certainly appreciate the feedback.
Profile ID: LFUS-PAI-O-1389194