Abstract: An antimicrobial peptide produced by Bacillus subtilis 168 was isolated and characterized and named sublancin 168. The invention includes DNA encoding for the sublancin 168 peptides and peptides which are at least 80% identical to the sublancin 168 peptide. The peptides may be administered as anti-bacterials, or may be used in food preservation. The peptides may also be co-administered with other lantibiotics (such as nisin and subtilin), or with known antibiotics.

Abstract: A sublancin peptide variant (lantibody) having a spacer region and a subtilin leader peptide fused to the C-terminal end of the mature sublancin peptide provide an anchoring means for inserting and retaining the lantibody in a host cell wall without affecting the intracellular processing of the lantibody, host cell expression of the molecule on the cell surface or the biological activity of the mature sublancin peptide in extracellular, cell-wall-bound form. Target molecules that bind to the antibody and methods of engineering a peptide variant gene, plasmid and a host cell transformant are described as are methods for generating a lantibody display library and identifying new target molecules.

Abstract: The present invention is directed to compositions comprising nisin and sublancin in amounts that are effective to inhibit bacterial spore germination. Additionally, the present invention is directed towards methods of inhibiting bacterial spore germination for a variety of purposes.

Abstract: A sublancin peptide variant having a Gly-His peptide sequence fused to the C-terminal end of the mature sublancin peptide provides an affinity tag facilitating increased purification of the peptide variant from sample preparations without affecting the intracellular processing of the sublancin peptide variant, expression by a host cell or its biological activity in secreted form. This sublancin variant has specific inhibitory activity for spore outgrowth as for the native sublancin peptide. Production of the sublancin peptide variant on an industrial scale is set forth as are methods of decontaminating spore-infected areas. Methods for generating the peptide variant gene, plasmid and transformant are also described.

Abstract: A sublancin peptide variant (lantibody) having a spacer region and a subtilin leader peptide fused to the C-terminal end of the mature sublancin peptide provide an anchoring means for inserting and retaining the lantibody in a host cell wall without affecting the intracellular processing of the lantibody, host cell expression of the molecule on the cell surface or the biological activity of the mature sublancin peptide in extracellular, cell-wall-bound form. Target molecules that bind to the lantibody and methods of engineering a peptide variant gene, plasmid and a host cell transformant are described as are methods of using a lantibody to identify new target molecules.

Abstract: The present invention is directed to compositions comprising nisin and sublancin in amounts that are effective to inhibit bacterial spore germination. Additionally, the present invention is directed towards methods of inhibiting bacterial spore germination for a variety of purposes.

Abstract: An antimicrobial peptide produced by Bacillus subtilis 168 was isolated and characterized and named sublancin 168. The invention includes DNA encoding for the sublancin 168 peptides and peptides which are at least 80% identical to the sublancin 168 peptide. The peptides may be administered as anti-bacterials, or may be used in food preservation. The peptides may also be co-administered with other lantibiotics (such as nisin and subtilin), or with known antibiotics.

Abstract: An antimicrobial peptide produced by Bacillus subtilis 168 was isolated and characterized and named sublancin 168. The invention includes DNA encoding for the sublancin 168 peptides and peptides which are at least 80% identical to the sublancin 168 peptide. The peptides may be administered as anti-bacterials, or may be used in food preservation. The peptides may also be co-administered with other lantibiotics (such as nisin and subtilin), or with known antibiotics.

Abstract: A sublancin peptide variant having a Gly-His peptide sequence fused to the C-terminal end of the mature sublancin peptide provides an affinity tag facilitating increased purification of the peptide variant from sample preparations without affecting the intracellular processing of the sublancin peptide variant, expression by a host cell or its biological activity in secreted form. This sublancin variant has specific inhibitory activity for spore outgrowth as for the native sublancin peptide. Production of the sublancin peptide variant on an industrial scale is set forth as are methods of decontaminating spore-infected areas. Methods for generating the peptide variant gene, plasmid and transformant are also described.

Abstract: A sublancin peptide variant (lantibody) having a spacer region and a subtilin leader peptide fused to the C-terminal end of the mature sublancin peptide provide an anchoring means for inserting and retaining the lantibody in a host cell wall without affecting the intracellular processing of the lantibody, host cell expression of the molecule on the cell surface or the biological activity of the mature sublancin peptide in extracellular, cell-wall-bound form. Target molecules that bind to the antibody and methods of engineering a peptide variant gene, plasmid and a host cell transformant are described as are methods for generating a lantibody display library and identifying new target molecules.

Abstract: A sublancin peptide variant (lantibody) having a spacer region and a subtilin leader peptide fused to the C-terminal end of the mature sublancin peptide provide an anchoring means for inserting and retaining the lantibody in a host cell wall without affecting the intracellular processing of the lantibody, host cell expression of the molecule on the cell surface or the biological activity of the mature sublancin peptide in extracellular, cell-wall-bound form. Target molecules that bind to the lantibody and methods of engineering a peptide variant gene, plasmid and a host cell transformant are described as are methods of using a lantibody to identify new target molecules.

Abstract: Nisin-subtilin mutant and chimeric prepeptides were constructed and expressed in a Bacillus subtilis strain that possesses all of the cellular machinery for making subtilin, except for the presubtilin gene. The chimera S.sub.L -Nis.sub.1-11 -Sub.sub.12-32 was prepared. The prepeptide has the subtilin leader sequence (S.sub.L), the N-terminal portion of the structural region was derived from nisin, and the C-terminal portion of the structural region derived from subtilin. This chimera was accurately and efficiently converted to the mature lantibiotic, as demonstrated by a variety of physical and biological activity assays. In contrast, a (S.sub.L -Sub.sub.1-11 -Nis.sub.12-34) chimera was processed into a heterogeneous mixture of products, none of which appeared to be the correct chimeric lantibiotic. The mixture did, however, contain an active minor component with a biological activity that exceeded nisin itself.

Abstract: The method by which polypeptides having residues other than the 20 common amino acids are made is established. A leader peptide sequence and its gene are identified which induce or assist post-translational modifications of Cys, Thr and Ser in prokaryotes. The leader sequence may be used to induce the presence of covalent bonding sites in polypeptides and can be expressed by either naturally occurring or artificial means. Further, a subtilin mutant substituting isoleucine for Glu.sub.4 of the native sequence exhibits a 57-fold improvement in stability, resisting modification of the dehydroalanine residue at position 5. This stable mutant exhibits 3-4 times the specific activity, in suppression of bacterial spore outgrowth, of the native bacteriocin. A method for site-specific mutagenesis, as well as the resulting mutant gene, plasmid and transformant is similarly set forth.

Abstract: The method by which polypeptides having residues other than the 20 common amino acids are made is established. A leader peptide sequence (SEQ ID NO: 7) and its gene are identified which induce or assist post-translational modifications of Cys, Thr and Ser in prokaryotes. The leader sequence may be used to induce the presence of covalent bonding sites in polypeptides and can be expressed by either naturally occurring or artificial means. Further, a subtilin mutant substituting isoleucine for Glu.sub.4 of the native sequence exhibits a 57-fold improvement in stability, resisting modification of the dehydroalanine residue at position 5. This stable mutant exhibits 3-4 times the specific activity, in suppression of bacterial spore outgrowth, of the native bacteriocin. A method for site-specific mutagenesis, as well as the resulting mutant gene, plasmid and transformant is similarly set forth.

Abstract: Nisin-subtilin mutant and chimeric pre-peptides were constructed and expressed in a Bacillus subtilis strain that possesses all of the cellular machinery for making subtilin, except for the pre-subtilin gene. The chimera S.sub.L -Nis.sub.1-11 -Sub.sub.12-32 was prepared. This pre-peptide has the subtilin leader sequence (S.sub.L), the N-terminal portion of the structural region derived from nisin and the C-terminal portion of the structural region derived from subtilin. This chimera was accurately and efficiently converted to the mature lantibiotic, as demonstrated by a variety of physical and biological activity assays. In contrast, a S.sub.L -Sub.sub.1-11 -Nis.sub.12-34 chimera was processed into a heterogeneous mixture of products, none of which appeared to be the correct chimeric lantibiotic. The mixture did, however, contain an active minor component with a biological activity that exceeded nisin itself.

Abstract: A subtilin mutant substituting isoleucine for Glu.sub.4 of the native sequence (SEQ ID NO:7) exhibits a 57-fold improvement in stability, resisting modification of the dehydroalanine residue at position 5. This stable mutant exhibits 3-4 times the specific activity, in suppression of bacterial spore outgrowth, of the native bacteriocin. A method for site-specific mutagenesis, as well as the resulting mutant gene, plasmid and transformant is similarly set forth.

Abstract: A subtilin mutant substituting isoleucine for Glu.sub.4 of the native sequence (SEQ ID NO: 7) exhibits a 57-fold improvement in stability, resisting modification of the dehydroalanine residue at position 5. This stable mutant exhibits 3-4 times the specific activity, in suppression of bacterial spore outgrowth, of the native bacteriocin. A method for site-specific mutagenesis, as well as the resulting mutant gene, plasmid and transformant is similarly set forth.

Abstract: The method by which polypeptides having residues other than the 20 common amino acids are made is established. A leader peptide sequence, and its gene, are identified which induce or assist post-translational modifications of Cys, Thr and Ser in prokaryotes. The leader sequence may be used to induce the presence of covalent bonding sites in polypeptides and can be expressed by either naturally occurring or artificial means.