Skip to main content
NCBI home page
Microbiological Reviews logoLink to Microbiological Reviews
. 1995 Jun;59(2):171–200. doi: 10.1128/mr.59.2.171-200.1995

Bacteriocins of gram-positive bacteria.

R W Jack 1, J R Tagg 1, B Ray 1
PMCID: PMC239359  PMID: 7603408

Abstract

In recent years, a group of antibacterial proteins produced by gram-positive bacteria have attracted great interest in their potential use as food preservatives and as antibacterial agents to combat certain infections due to gram-positive pathogenic bacteria. They are ribosomally synthesized peptides of 30 to less than 60 amino acids, with a narrow to wide antibacterial spectrum against gram-positive bacteria; the antibacterial property is heat stable, and a producer strain displays a degree of specific self-protection against its own antibacterial peptide. In many respects, these proteins are quite different from the colicins and other bacteriocins produced by gram-negative bacteria, yet customarily they also are grouped as bacteriocins. Although a large number of these bacteriocins (or bacteriocin-like inhibitory substances) have been reported, only a few have been studied in detail for their mode of action, amino acid sequence, genetic characteristics, and biosynthesis mechanisms. Nevertheless, in general, they appear to be translated as inactive prepeptides containing an N-terminal leader sequence and a C-terminal propeptide component. During posttranslational modifications, the leader peptide is removed. In addition, depending on the particular type, some amino acids in the propeptide components may undergo either dehydration and thioether ring formation to produce lanthionine and beta-methyl lanthionine (as in lantibiotics) or thio ester ring formation to form cystine (as in thiolbiotics). Some of these steps, as well as the translocation of the molecules through the cytoplasmic membrane and producer self-protection against the homologous bacteriocin, are mediated through specific proteins (enzymes). Limited genetic studies have shown that the structural gene for such a bacteriocin and the genes encoding proteins associated with immunity, translocation, and processing are present in a cluster in either a plasmid, the chromosome, or a transposon. Following posttranslational modification and depending on the pH, the molecules may either be released into the environment or remain bound to the cell wall. The antibacterial action against a sensitive cell of a gram-positive strain is produced principally by destabilization of membrane functions. Under certain conditions, gram-negative bacterial cells can also be sensitive to some of these molecules. By application of site-specific mutagenesis, bacteriocin variants which may differ in their antimicrobial spectrum and physicochemical characteristics can be produced. Research activity in this field has grown remarkably but sometimes with an undisciplined regard for conformity in the definition, naming, and categorization of these molecules and their genetic effectors. Some suggestions for improved standardization of nomenclature are offered.

Full Text

The Full Text of this article is available as a PDF (1,000.2 KB).

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Abee T., Klaenhammer T. R., Letellier L. Kinetic studies of the action of lactacin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane. Appl Environ Microbiol. 1994 Mar;60(3):1006–1013. doi: 10.1128/aem.60.3.1006-1013.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Allgaier H., Jung G., Werner R. G., Schneider U., Zähner H. Epidermin: sequencing of a heterodetic tetracyclic 21-peptide amide antibiotic. Eur J Biochem. 1986 Oct 1;160(1):9–22. doi: 10.1111/j.1432-1033.1986.tb09933.x. [DOI] [PubMed] [Google Scholar]
  3. Allison G. E., Fremaux C., Klaenhammer T. R. Expansion of bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J Bacteriol. 1994 Apr;176(8):2235–2241. doi: 10.1128/jb.176.8.2235-2241.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Amemura M., Makino K., Shinagawa H., Kobayashi A., Nakata A. Nucleotide sequence of the genes involved in phosphate transport and regulation of the phosphate regulon in Escherichia coli. J Mol Biol. 1985 Jul 20;184(2):241–250. doi: 10.1016/0022-2836(85)90377-8. [DOI] [PubMed] [Google Scholar]
  5. Amemura M., Makino K., Shinagawa H., Nakata A. Nucleotide sequence of the phoM region of Escherichia coli: four open reading frames may constitute an operon. J Bacteriol. 1986 Oct;168(1):294–302. doi: 10.1128/jb.168.1.294-302.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Augustin J., Rosenstein R., Wieland B., Schneider U., Schnell N., Engelke G., Entian K. D., Götz F. Genetic analysis of epidermin biosynthetic genes and epidermin-negative mutants of Staphylococcus epidermidis. Eur J Biochem. 1992 Mar 15;204(3):1149–1154. doi: 10.1111/j.1432-1033.1992.tb16740.x. [DOI] [PubMed] [Google Scholar]
  7. Axelsson L., Holck A., Birkeland S. E., Aukrust T., Blom H. Cloning and nucleotide sequence of a gene from Lactobacillus sake Lb706 necessary for sakacin A production and immunity. Appl Environ Microbiol. 1993 Sep;59(9):2868–2875. doi: 10.1128/aem.59.9.2868-2875.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. BERRIDGE N. J., NEWTON G. G. F., ABRAHAM E. P. Purification and nature of the antibiotic nisin. Biochem J. 1952 Dec;52(4):529–535. doi: 10.1042/bj0520529. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Bailey F. J., Hurst A. Preparation of a highly active form of nisin from Streptococcus lactis. Can J Microbiol. 1971 Jan;17(1):61–67. doi: 10.1139/m71-010. [DOI] [PubMed] [Google Scholar]
  10. Banerjee S., Hansen J. N. Structure and expression of a gene encoding the precursor of subtilin, a small protein antibiotic. J Biol Chem. 1988 Jul 5;263(19):9508–9514. [PubMed] [Google Scholar]
  11. Benz R. Structure and function of porins from gram-negative bacteria. Annu Rev Microbiol. 1988;42:359–393. doi: 10.1146/annurev.mi.42.100188.002043. [DOI] [PubMed] [Google Scholar]
  12. Bhunia A. K., Johnson M. C., Ray B. Purification, characterization and antimicrobial spectrum of a bacteriocin produced by Pediococcus acidilactici. J Appl Bacteriol. 1988 Oct;65(4):261–268. doi: 10.1111/j.1365-2672.1988.tb01893.x. [DOI] [PubMed] [Google Scholar]
  13. Bierbaum G., Sahl H. G. Autolytic system of Staphylococcus simulans 22: influence of cationic peptides on activity of N-acetylmuramoyl-L-alanine amidase. J Bacteriol. 1987 Dec;169(12):5452–5458. doi: 10.1128/jb.169.12.5452-5458.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Bierbaum G., Sahl H. G. Induction of autolysis of staphylococci by the basic peptide antibiotics Pep 5 and nisin and their influence on the activity of autolytic enzymes. Arch Microbiol. 1985 Apr;141(3):249–254. doi: 10.1007/BF00408067. [DOI] [PubMed] [Google Scholar]
  15. Bierbaum G., Sahl H. G. Lantibiotics--unusually modified bacteriocin-like peptides from gram-positive bacteria. Zentralbl Bakteriol. 1993 Feb;278(1):1–22. doi: 10.1016/s0934-8840(11)80275-6. [DOI] [PubMed] [Google Scholar]
  16. Biswas S. R., Ray P., Johnson M. C., Ray B. Influence of Growth Conditions on the Production of a Bacteriocin, Pediocin AcH, by Pediococcus acidilactici H. Appl Environ Microbiol. 1991 Apr;57(4):1265–1267. doi: 10.1128/aem.57.4.1265-1267.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Boulnois G. J., Paton J. C., Mitchell T. J., Andrew P. W. Structure and function of pneumolysin, the multifunctional, thiol-activated toxin of Streptococcus pneumoniae. Mol Microbiol. 1991 Nov;5(11):2611–2616. doi: 10.1111/j.1365-2958.1991.tb01969.x. [DOI] [PubMed] [Google Scholar]
  18. Bradley D. E. Ultrastructure of bacteriophage and bacteriocins. Bacteriol Rev. 1967 Dec;31(4):230–314. doi: 10.1128/br.31.4.230-314.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Bruno M. E., Montville T. J. Common mechanistic action of bacteriocins from lactic Acid bacteria. Appl Environ Microbiol. 1993 Sep;59(9):3003–3010. doi: 10.1128/aem.59.9.3003-3010.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Buchman G. W., Banerjee S., Hansen J. N. Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic. J Biol Chem. 1988 Nov 5;263(31):16260–16266. [PubMed] [Google Scholar]
  21. Bukhtiyarova M., Yang R., Ray B. Analysis of the pediocin AcH gene cluster from plasmid pSMB74 and its expression in a pediocin-negative Pediococcus acidilactici strain. Appl Environ Microbiol. 1994 Sep;60(9):3405–3408. doi: 10.1128/aem.60.9.3405-3408.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Chikindas M. L., García-Garcerá M. J., Driessen A. J., Ledeboer A. M., Nissen-Meyer J., Nes I. F., Abee T., Konings W. N., Venema G. Pediocin PA-1, a bacteriocin from Pediococcus acidilactici PAC1.0, forms hydrophilic pores in the cytoplasmic membrane of target cells. Appl Environ Microbiol. 1993 Nov;59(11):3577–3584. doi: 10.1128/aem.59.11.3577-3584.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Christensen D. P., Hutkins R. W. Collapse of the proton motive force in Listeria monocytogenes caused by a bacteriocin produced by Pediococcus acidilactici. Appl Environ Microbiol. 1992 Oct;58(10):3312–3315. doi: 10.1128/aem.58.10.3312-3315.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Chung Y. J., Hansen J. N. Determination of the sequence of spaE and identification of a promoter in the subtilin (spa) operon in Bacillus subtilis. J Bacteriol. 1992 Oct;174(20):6699–6702. doi: 10.1128/jb.174.20.6699-6702.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Daeschel M. A., Klaenhammer T. R. Association of a 13.6-Megadalton Plasmid in Pediococcus pentosaceus with Bacteriocin Activity. Appl Environ Microbiol. 1985 Dec;50(6):1538–1541. doi: 10.1128/aem.50.6.1538-1541.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Davey G. P. Plasmid associated with diplococcin production in Streptococcus. Appl Environ Microbiol. 1984 Oct;48(4):895–896. doi: 10.1128/aem.48.4.895-896.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. Davies J. What are antibiotics? Archaic functions for modern activities. Mol Microbiol. 1990 Aug;4(8):1227–1232. doi: 10.1111/j.1365-2958.1990.tb00701.x. [DOI] [PubMed] [Google Scholar]
  28. Dodd H. M., Horn N., Gasson M. J. Analysis of the genetic determinant for production of the peptide antibiotic nisin. J Gen Microbiol. 1990 Mar;136(3):555–566. doi: 10.1099/00221287-136-3-555. [DOI] [PubMed] [Google Scholar]
  29. Dufour A., Thuault D., Boulliou A., Bourgeois C. M., Le Pennec J. P. Plasmid-encoded determinants for bacteriocin production and immunity in a Lactococcus lactis strain and purification of the inhibitory peptide. J Gen Microbiol. 1991 Oct;137(10):2423–2429. doi: 10.1099/00221287-137-10-2423. [DOI] [PubMed] [Google Scholar]
  30. Engelke G., Gutowski-Eckel Z., Hammelmann M., Entian K. D. Biosynthesis of the lantibiotic nisin: genomic organization and membrane localization of the NisB protein. Appl Environ Microbiol. 1992 Nov;58(11):3730–3743. doi: 10.1128/aem.58.11.3730-3743.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  31. Engelke G., Gutowski-Eckel Z., Kiesau P., Siegers K., Hammelmann M., Entian K. D. Regulation of nisin biosynthesis and immunity in Lactococcus lactis 6F3. Appl Environ Microbiol. 1994 Mar;60(3):814–825. doi: 10.1128/aem.60.3.814-825.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. FREDERICQ P. COLICINES ET AUTRES BACTERIOCINES. Ergeb Mikrobiol Immunitatsforsch Exp Ther. 1963;37:114–161. [PubMed] [Google Scholar]
  33. FREDERICQ P. Colicins. Annu Rev Microbiol. 1957;11:7–22. doi: 10.1146/annurev.mi.11.100157.000255. [DOI] [PubMed] [Google Scholar]
  34. Farkas-Himsley H., Zhang Y. S., Yuan M., Musclow C. E. Partially purified bacteriocin kills malignant cells by apoptosis: programmed cell death. Cell Mol Biol (Noisy-le-grand) 1992 Aug-Sep;38(5-6):643–651. [PubMed] [Google Scholar]
  35. Fremaux C., Ahn C., Klaenhammer T. R. Molecular analysis of the lactacin F operon. Appl Environ Microbiol. 1993 Nov;59(11):3906–3915. doi: 10.1128/aem.59.11.3906-3915.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Freund S., Jung G., Gutbrod O., Folkers G., Gibbons W. A., Allgaier H., Werner R. The solution structure of the lantibiotic gallidermin. Biopolymers. 1991 May;31(6):803–811. doi: 10.1002/bip.360310626. [DOI] [PubMed] [Google Scholar]
  37. Gao F. H., Abee T., Konings W. N. Mechanism of action of the peptide antibiotic nisin in liposomes and cytochrome c oxidase-containing proteoliposomes. Appl Environ Microbiol. 1991 Aug;57(8):2164–2170. doi: 10.1128/aem.57.8.2164-2170.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  38. Garcerá M. J., Elferink M. G., Driessen A. J., Konings W. N. In vitro pore-forming activity of the lantibiotic nisin. Role of protonmotive force and lipid composition. Eur J Biochem. 1993 Mar 1;212(2):417–422. doi: 10.1111/j.1432-1033.1993.tb17677.x. [DOI] [PubMed] [Google Scholar]
  39. Garnier T., Cole S. T. Characterization of a bacteriocinogenic plasmid from Clostridium perfringens and molecular genetic analysis of the bacteriocin-encoding gene. J Bacteriol. 1986 Dec;168(3):1189–1196. doi: 10.1128/jb.168.3.1189-1196.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  40. Gonzalez C. F., Kunka B. S. Plasmid-Associated Bacteriocin Production and Sucrose Fermentation in Pediococcus acidilactici. Appl Environ Microbiol. 1987 Oct;53(10):2534–2538. doi: 10.1128/aem.53.10.2534-2538.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  41. Gonzalez C. F., Kunka B. S. Transfer of Sucrose-Fermenting Ability and Nisin Production Phenotype among Lactic Streptococci. Appl Environ Microbiol. 1985 Mar;49(3):627–633. doi: 10.1128/aem.49.3.627-633.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. Graham D. C., McKay L. L. Plasmid DNA in Strains of Pediococcus cerevisiae and Pediococcus pentosaceus. Appl Environ Microbiol. 1985 Aug;50(2):532–534. doi: 10.1128/aem.50.2.532-534.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  43. Gross E., Kiltz H. H. The number and nature of , -unsaturated amino acids in subtilin. Biochem Biophys Res Commun. 1973 Jan 23;50(2):559–565. doi: 10.1016/0006-291x(73)90876-0. [DOI] [PubMed] [Google Scholar]
  44. Gross E., Morell J. L. The structure of nisin. J Am Chem Soc. 1971 Sep 8;93(18):4634–4635. doi: 10.1021/ja00747a073. [DOI] [PubMed] [Google Scholar]
  45. Gutowski-Eckel Z., Klein C., Siegers K., Bohm K., Hammelmann M., Entian K. D. Growth phase-dependent regulation and membrane localization of SpaB, a protein involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol. 1994 Jan;60(1):1–11. doi: 10.1128/aem.60.1.1-11.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Hansen J. N. Antibiotics synthesized by posttranslational modification. Annu Rev Microbiol. 1993;47:535–564. doi: 10.1146/annurev.mi.47.100193.002535. [DOI] [PubMed] [Google Scholar]
  47. Hastings J. W., Sailer M., Johnson K., Roy K. L., Vederas J. C., Stiles M. E. Characterization of leucocin A-UAL 187 and cloning of the bacteriocin gene from Leuconostoc gelidum. J Bacteriol. 1991 Dec;173(23):7491–7500. doi: 10.1128/jb.173.23.7491-7500.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  48. Henderson J. T., Chopko A. L., van Wassenaar P. D. Purification and primary structure of pediocin PA-1 produced by Pediococcus acidilactici PAC-1.0. Arch Biochem Biophys. 1992 May 15;295(1):5–12. doi: 10.1016/0003-9861(92)90480-k. [DOI] [PubMed] [Google Scholar]
  49. Holck A. L., Axelsson L., Hühne K., Kröckel L. Purification and cloning of sakacin 674, a bacteriocin from Lactobacillus sake Lb674. FEMS Microbiol Lett. 1994 Jan 15;115(2-3):143–149. doi: 10.1111/j.1574-6968.1994.tb06629.x. [DOI] [PubMed] [Google Scholar]
  50. Holck A. L., Axelsson L., Schillinger U. Purification and cloning of piscicolin 61, a bacteriocin from Carnobacterium piscicola LV61. Curr Microbiol. 1994 Aug;29(2):63–68. doi: 10.1007/BF01575750. [DOI] [PubMed] [Google Scholar]
  51. Holck A., Axelsson L., Birkeland S. E., Aukrust T., Blom H. Purification and amino acid sequence of sakacin A, a bacteriocin from Lactobacillus sake Lb706. J Gen Microbiol. 1992 Dec;138(12):2715–2720. doi: 10.1099/00221287-138-12-2715. [DOI] [PubMed] [Google Scholar]
  52. Holo H., Nilssen O., Nes I. F. Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J Bacteriol. 1991 Jun;173(12):3879–3887. doi: 10.1128/jb.173.12.3879-3887.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Horn N., Swindell S., Dodd H., Gasson M. Nisin biosynthesis genes are encoded by a novel conjugative transposon. Mol Gen Genet. 1991 Aug;228(1-2):129–135. doi: 10.1007/BF00282457. [DOI] [PubMed] [Google Scholar]
  54. Hynes W. L., Ferretti J. J., Tagg J. R. Cloning of the gene encoding Streptococcin A-FF22, a novel lantibiotic produced by Streptococcus pyogenes, and determination of its nucleotide sequence. Appl Environ Microbiol. 1993 Jun;59(6):1969–1971. doi: 10.1128/aem.59.6.1969-1971.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Héchard Y., Dérijard B., Letellier F., Cenatiempo Y. Characterization and purification of mesentericin Y105, an anti-Listeria bacteriocin from Leuconostoc mesenteroides. J Gen Microbiol. 1992 Dec;138(12):2725–2731. doi: 10.1099/00221287-138-12-2725. [DOI] [PubMed] [Google Scholar]
  56. Ingram L. C. Synthesis of the antibiotic nisin: formation of lanthionine and beta-methyl-lanthionine. Biochim Biophys Acta. 1969 Jun 17;184(1):216–219. doi: 10.1016/0304-4165(69)90121-4. [DOI] [PubMed] [Google Scholar]
  57. Ingram L. A ribosomal mechanism for synthesis of peptides related to nisin. Biochim Biophys Acta. 1970 Nov 12;224(1):263–265. doi: 10.1016/0005-2787(70)90642-8. [DOI] [PubMed] [Google Scholar]
  58. JACOB F., LWOFF A., SIMINOVITCH A., WOLLMAN E. Définition de quelques termes relatifs a la lysogénie. Ann Inst Pasteur (Paris) 1953 Jan;84(1):222–224. [PubMed] [Google Scholar]
  59. Jack R. W., Carne A., Metzger J., Stefanović S., Sahl H. G., Jung G., Tagg J. Elucidation of the structure of SA-FF22, a lanthionine-containing antibacterial peptide produced by Streptococcus pyogenes strain FF22. Eur J Biochem. 1994 Mar 1;220(2):455–462. doi: 10.1111/j.1432-1033.1994.tb18643.x. [DOI] [PubMed] [Google Scholar]
  60. Jack R. W., Tagg J. R. Factors affecting production of the group A streptococcus bacteriocin SA-FF22. J Med Microbiol. 1992 Feb;36(2):132–138. doi: 10.1099/00222615-36-2-132. [DOI] [PubMed] [Google Scholar]
  61. Jack R., Benz R., Tagg J., Sahl H. G. The mode of action of SA-FF22, a lantibiotic isolated from Streptococcus pyogenes strain FF22. Eur J Biochem. 1994 Jan 15;219(1-2):699–705. doi: 10.1111/j.1432-1033.1994.tb19986.x. [DOI] [PubMed] [Google Scholar]
  62. Jiménez-Díaz R., Rios-Sánchez R. M., Desmazeaud M., Ruiz-Barba J. L., Piard J. C. Plantaricins S and T, Two New Bacteriocins Produced by Lactobacillus plantarum LPCO10 Isolated from a Green Olive Fermentation. Appl Environ Microbiol. 1993 May;59(5):1416–1424. doi: 10.1128/aem.59.5.1416-1424.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Joerger M. C., Klaenhammer T. R. Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Lactobacillus helveticus 481. J Bacteriol. 1986 Aug;167(2):439–446. doi: 10.1128/jb.167.2.439-446.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  64. Joerger M. C., Klaenhammer T. R. Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J. J Bacteriol. 1990 Nov;172(11):6339–6347. doi: 10.1128/jb.172.11.6339-6347.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  65. Kaletta C., Entian K. D., Kellner R., Jung G., Reis M., Sahl H. G. Pep5, a new lantibiotic: structural gene isolation and prepeptide sequence. Arch Microbiol. 1989;152(1):16–19. doi: 10.1007/BF00447005. [DOI] [PubMed] [Google Scholar]
  66. Kaletta C., Entian K. D. Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product. J Bacteriol. 1989 Mar;171(3):1597–1601. doi: 10.1128/jb.171.3.1597-1601.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Kellner R., Jung G., Hörner T., Zähner H., Schnell N., Entian K. D., Götz F. Gallidermin: a new lanthionine-containing polypeptide antibiotic. Eur J Biochem. 1988 Oct 15;177(1):53–59. doi: 10.1111/j.1432-1033.1988.tb14344.x. [DOI] [PubMed] [Google Scholar]
  68. Klaenhammer T. R. Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol Rev. 1993 Sep;12(1-3):39–85. doi: 10.1111/j.1574-6976.1993.tb00012.x. [DOI] [PubMed] [Google Scholar]
  69. Klein C., Kaletta C., Entian K. D. Biosynthesis of the lantibiotic subtilin is regulated by a histidine kinase/response regulator system. Appl Environ Microbiol. 1993 Jan;59(1):296–303. doi: 10.1128/aem.59.1.296-303.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  70. Klein C., Kaletta C., Schnell N., Entian K. D. Analysis of genes involved in biosynthesis of the lantibiotic subtilin. Appl Environ Microbiol. 1992 Jan;58(1):132–142. doi: 10.1128/aem.58.1.132-142.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  71. Kleinkauf H., von Döhren H. Nonribosomal biosynthesis of peptide antibiotics. Eur J Biochem. 1990 Aug 28;192(1):1–15. doi: 10.1111/j.1432-1033.1990.tb19188.x. [DOI] [PubMed] [Google Scholar]
  72. Kolter R., Moreno F. Genetics of ribosomally synthesized peptide antibiotics. Annu Rev Microbiol. 1992;46:141–163. doi: 10.1146/annurev.mi.46.100192.001041. [DOI] [PubMed] [Google Scholar]
  73. Kordel M., Benz R., Sahl H. G. Mode of action of the staphylococcinlike peptide Pep 5: voltage-dependent depolarization of bacterial and artificial membranes. J Bacteriol. 1988 Jan;170(1):84–88. doi: 10.1128/jb.170.1.84-88.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Kordel M., Schüller F., Sahl H. G. Interaction of the pore forming-peptide antibiotics Pep 5, nisin and subtilin with non-energized liposomes. FEBS Lett. 1989 Feb 13;244(1):99–102. doi: 10.1016/0014-5793(89)81171-8. [DOI] [PubMed] [Google Scholar]
  75. Kozar W., Rajchert-Trzpil M., Dobrzański W. T. The effect of proflavin, ethidium bromide and an elevated temperature on the appearance of nisin-negative clones in nisin-producing strains of Streptococcus lactis. J Gen Microbiol. 1974 Aug;83(2):295–302. doi: 10.1099/00221287-83-2-295. [DOI] [PubMed] [Google Scholar]
  76. Kuipers O. P., Beerthuyzen M. M., Siezen R. J., De Vos W. M. Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. Eur J Biochem. 1993 Aug 15;216(1):281–291. doi: 10.1111/j.1432-1033.1993.tb18143.x. [DOI] [PubMed] [Google Scholar]
  77. Kupke T., Stevanović S., Sahl H. G., Götz F. Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin. J Bacteriol. 1992 Aug;174(16):5354–5361. doi: 10.1128/jb.174.16.5354-5361.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. Lewus C. B., Sun S., Montville T. J. Production of an Amylase-Sensitive Bacteriocin by an Atypical Leuconostoc paramesenteroides Strain. Appl Environ Microbiol. 1992 Jan;58(1):143–149. doi: 10.1128/aem.58.1.143-149.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  79. Linnett P. E., Strominger J. L. Additional antibiotic inhibitors of peptidoglycan synthesis. Antimicrob Agents Chemother. 1973 Sep;4(3):231–236. doi: 10.1128/aac.4.3.231. [DOI] [PMC free article] [PubMed] [Google Scholar]
  80. Liu W., Hansen J. N. Enhancement of the chemical and antimicrobial properties of subtilin by site-directed mutagenesis. J Biol Chem. 1992 Dec 15;267(35):25078–25085. [PubMed] [Google Scholar]
  81. Liu W., Hansen J. N. Some chemical and physical properties of nisin, a small-protein antibiotic produced by Lactococcus lactis. Appl Environ Microbiol. 1990 Aug;56(8):2551–2558. doi: 10.1128/aem.56.8.2551-2558.1990. [DOI] [PMC free article] [PubMed] [Google Scholar]
  82. Lämmler C. Typing of Actinomyces pyogenes by its production and susceptibility to bacteriocin-like inhibitors. Zentralbl Bakteriol. 1990 Jun;273(2):173–178. doi: 10.1016/s0934-8840(11)80245-8. [DOI] [PubMed] [Google Scholar]
  83. Maftah A., Renault D., Vignoles C., Héchard Y., Bressollier P., Ratinaud M. H., Cenatiempo Y., Julien R. Membrane permeabilization of Listeria monocytogenes and mitochondria by the bacteriocin mesentericin Y105. J Bacteriol. 1993 May;175(10):3232–3235. doi: 10.1128/jb.175.10.3232-3235.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  84. Martin J. F., Demain A. L. Control of antibiotic biosynthesis. Microbiol Rev. 1980 Jun;44(2):230–251. doi: 10.1128/mr.44.2.230-251.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Marugg J. D., Gonzalez C. F., Kunka B. S., Ledeboer A. M., Pucci M. J., Toonen M. Y., Walker S. A., Zoetmulder L. C., Vandenbergh P. A. Cloning, expression, and nucleotide sequence of genes involved in production of pediocin PA-1, and bacteriocin from Pediococcus acidilactici PAC1.0. Appl Environ Microbiol. 1992 Aug;58(8):2360–2367. doi: 10.1128/aem.58.8.2360-2367.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  86. Morris S. L., Walsh R. C., Hansen J. N. Identification and characterization of some bacterial membrane sulfhydryl groups which are targets of bacteriostatic and antibiotic action. J Biol Chem. 1984 Nov 10;259(21):13590–13594. [PubMed] [Google Scholar]
  87. Motlagh A. M., Bhunia A. K., Szostek F., Hansen T. R., Johnson M. C., Ray B. Nucleotide and amino acid sequence of pap-gene (pediocin AcH production) in Pediococcus acidilactici H. Lett Appl Microbiol. 1992 Aug;15(2):45–48. doi: 10.1111/j.1472-765x.1992.tb00721.x. [DOI] [PubMed] [Google Scholar]
  88. Motlagh A., Bukhtiyarova M., Ray B. Complete nucleotide sequence of pSMB 74, a plasmid encoding the production of pediocin AcH in Pediococcus acidilactici. Lett Appl Microbiol. 1994 Jun;18(6):305–312. doi: 10.1111/j.1472-765x.1994.tb00876.x. [DOI] [PubMed] [Google Scholar]
  89. Mulders J. W., Boerrigter I. J., Rollema H. S., Siezen R. J., de Vos W. M. Identification and characterization of the lantibiotic nisin Z, a natural nisin variant. Eur J Biochem. 1991 Nov 1;201(3):581–584. doi: 10.1111/j.1432-1033.1991.tb16317.x. [DOI] [PubMed] [Google Scholar]
  90. Muriana P. M., Klaenhammer T. R. Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp. J Bacteriol. 1991 Mar;173(5):1779–1788. doi: 10.1128/jb.173.5.1779-1788.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Neve H., Geis A., Teuber M. Conjugal transfer and characterization of bacteriocin plasmids in group N (lactic acid) streptococci. J Bacteriol. 1984 Mar;157(3):833–838. doi: 10.1128/jb.157.3.833-838.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Nieto Lozano J. C., Meyer J. N., Sletten K., Peláz C., Nes I. F. Purification and amino acid sequence of a bacteriocin produced by Pediococcus acidilactici. J Gen Microbiol. 1992 Sep;138(9):1985–1990. doi: 10.1099/00221287-138-9-1985. [DOI] [PubMed] [Google Scholar]
  93. Nishio C., Komura S., Kurahashi K. Peptide antibiotic subtilin is synthesized via precursor proteins. Biochem Biophys Res Commun. 1983 Oct 31;116(2):751–758. doi: 10.1016/0006-291x(83)90588-0. [DOI] [PubMed] [Google Scholar]
  94. Nissen-Meyer J., Holo H., Håvarstein L. S., Sletten K., Nes I. F. A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J Bacteriol. 1992 Sep;174(17):5686–5692. doi: 10.1128/jb.174.17.5686-5692.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Nissen-Meyer J., Håvarstein L. S., Holo H., Sletten K., Nes I. F. Association of the lactococcin A immunity factor with the cell membrane: purification and characterization of the immunity factor. J Gen Microbiol. 1993 Jul;139(7):1503–1509. doi: 10.1099/00221287-139-7-1503. [DOI] [PubMed] [Google Scholar]
  96. Nissen-Meyer J., Larsen A. G., Sletten K., Daeschel M., Nes I. F. Purification and characterization of plantaricin A, a Lactobacillus plantarum bacteriocin whose activity depends on the action of two peptides. J Gen Microbiol. 1993 Sep;139(9):1973–1978. doi: 10.1099/00221287-139-9-1973. [DOI] [PubMed] [Google Scholar]
  97. Palmer D. E., Mierke D. F., Pattaroni C., Goodman M., Wakamiya T., Fukase K., Kitazawa M., Fujita H., Shiba T. Interactive NMR and computer simulation studies of lanthionine-ring structures. Biopolymers. 1989 Jan;28(1):397–408. doi: 10.1002/bip.360280137. [DOI] [PubMed] [Google Scholar]
  98. Parker M. W., Tucker A. D., Tsernoglou D., Pattus F. Insights into membrane insertion based on studies of colicins. Trends Biochem Sci. 1990 Apr;15(4):126–129. doi: 10.1016/0968-0004(90)90205-p. [DOI] [PubMed] [Google Scholar]
  99. Peschel A., Augustin J., Kupke T., Stevanovic S., Götz F. Regulation of epidermin biosynthetic genes by EpiQ. Mol Microbiol. 1993 Jul;9(1):31–39. doi: 10.1111/j.1365-2958.1993.tb01666.x. [DOI] [PubMed] [Google Scholar]
  100. Piard J. C., Kuipers O. P., Rollema H. S., Desmazeaud M. J., de Vos W. M. Structure, organization, and expression of the lct gene for lacticin 481, a novel lantibiotic produced by Lactococcus lactis. J Biol Chem. 1993 Aug 5;268(22):16361–16368. [PubMed] [Google Scholar]
  101. Pore R. S. Microbial toxins, their functional role and phylogenetic validity. Biosystems. 1978 Apr;10(1-2):189–198. doi: 10.1016/0303-2647(78)90041-2. [DOI] [PubMed] [Google Scholar]
  102. Pucci M. J., Vedamuthu E. R., Kunka B. S., Vandenbergh P. A. Inhibition of Listeria monocytogenes by using bacteriocin PA-1 produced by Pediococcus acidilactici PAC 1.0. Appl Environ Microbiol. 1988 Oct;54(10):2349–2353. doi: 10.1128/aem.54.10.2349-2353.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]
  103. Pugsley A. P. The ins and outs of colicins. Part I: Production, and translocation across membranes. Microbiol Sci. 1984 Oct;1(7):168–175. [PubMed] [Google Scholar]
  104. Pugsley A. P. The ins and outs of colicins. Part II. Lethal action, immunity and ecological implications. Microbiol Sci. 1984 Nov;1(8):203–205. [PubMed] [Google Scholar]
  105. Quadri L. E., Sailer M., Roy K. L., Vederas J. C., Stiles M. E. Chemical and genetic characterization of bacteriocins produced by Carnobacterium piscicola LV17B. J Biol Chem. 1994 Apr 22;269(16):12204–12211. [PubMed] [Google Scholar]
  106. RAMSEIER H. R. [The effect of nisin on Clostridium butyricum Prazm]. Arch Mikrobiol. 1960;37:57–94. doi: 10.1007/BF00414627. [DOI] [PubMed] [Google Scholar]
  107. Raccach M., McGrath R., Daftarian H. Antibiosis of some lactic acid bacteria including Lactobacillus acidophilus toward Listeria monocytogenes. Int J Food Microbiol. 1989 Aug;9(1):25–32. doi: 10.1016/0168-1605(89)90034-2. [DOI] [PubMed] [Google Scholar]
  108. Rauch P. J., Beerthuyzen M. M., de Vos W. M. Nucleotide sequence of IS904 from Lactococcus lactis subsp. lactis strain NIZO R5. Nucleic Acids Res. 1990 Jul 25;18(14):4253–4254. doi: 10.1093/nar/18.14.4253. [DOI] [PMC free article] [PubMed] [Google Scholar]
  109. Reis M., Eschbach-Bludau M., Iglesias-Wind M. I., Kupke T., Sahl H. G. Producer immunity towards the lantibiotic Pep5: identification of the immunity gene pepI and localization and functional analysis of its gene product. Appl Environ Microbiol. 1994 Aug;60(8):2876–2883. doi: 10.1128/aem.60.8.2876-2883.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Reisinger P., Seidel H., Tschesche H., Hammes W. P. The effect of nisin on murein synthesis. Arch Microbiol. 1980 Oct;127(3):187–193. doi: 10.1007/BF00427192. [DOI] [PubMed] [Google Scholar]
  111. Rince A., Dufour A., Le Pogam S., Thuault D., Bourgeois C. M., Le Pennec J. P. Cloning, expression, and nucleotide sequence of genes involved in production of lactococcin DR, a bacteriocin from lactococcus lactis subsp. lactis. Appl Environ Microbiol. 1994 May;60(5):1652–1657. doi: 10.1128/aem.60.5.1652-1657.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Rogers L. A. THE INHIBITING EFFECT OF STREPTOCOCCUS LACTIS ON LACTOBACILLUS BULGARICUS. J Bacteriol. 1928 Nov;16(5):321–325. doi: 10.1128/jb.16.5.321-325.1928. [DOI] [PMC free article] [PubMed] [Google Scholar]
  113. Ross K. F., Ronson C. W., Tagg J. R. Isolation and characterization of the lantibiotic salivaricin A and its structural gene salA from Streptococcus salivarius 20P3. Appl Environ Microbiol. 1993 Jul;59(7):2014–2021. doi: 10.1128/aem.59.7.2014-2021.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Ruhr E., Sahl H. G. Mode of action of the peptide antibiotic nisin and influence on the membrane potential of whole cells and on cytoplasmic and artificial membrane vesicles. Antimicrob Agents Chemother. 1985 May;27(5):841–845. doi: 10.1128/aac.27.5.841. [DOI] [PMC free article] [PubMed] [Google Scholar]
  115. SCHINDLER C. A., SCHUHARDT V. T. PURIFICATION AND PROPERTIES OF LYSOSTAPHIN--A LYTIC AGENT FOR STAPHYLOCOCCUS AUREUS. Biochim Biophys Acta. 1965 Feb 15;97:242–250. doi: 10.1016/0304-4165(65)90088-7. [DOI] [PubMed] [Google Scholar]
  116. Sahl H. G., Brandis H. Mode of action of the staphylococcin-like peptide Pep 5 and culture conditions effecting its activity. Zentralbl Bakteriol Mikrobiol Hyg A. 1982 Jun;252(2):166–175. [PubMed] [Google Scholar]
  117. Sahl H. G., Brandis H. Production, purification and chemical properties of an antistaphylococcal agent produced by Staphylococcus epidermidis. J Gen Microbiol. 1981 Dec;127(2):377–384. doi: 10.1099/00221287-127-2-377. [DOI] [PubMed] [Google Scholar]
  118. Sahl H. G., Hahn C., Brandis H. Interaction of the staphylococcin-like peptide Pep 5 with cell walls and isolated cell wall components of Gram-positive bacteria. Zentralbl Bakteriol Mikrobiol Hyg A. 1985 Oct;260(2):197–205. doi: 10.1016/s0176-6724(85)80115-2. [DOI] [PubMed] [Google Scholar]
  119. Sahl H. G. Influence of the staphylococcinlike peptide Pep 5 on membrane potential of bacterial cells and cytoplasmic membrane vesicles. J Bacteriol. 1985 May;162(2):833–836. doi: 10.1128/jb.162.2.833-836.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  120. Sahl H. G., Kordel M., Benz R. Voltage-dependent depolarization of bacterial membranes and artificial lipid bilayers by the peptide antibiotic nisin. Arch Microbiol. 1987;149(2):120–124. doi: 10.1007/BF00425076. [DOI] [PubMed] [Google Scholar]
  121. Sahl H. G. Staphylococcin 1580 is identical to the lantibiotic epidermin: implications for the nature of bacteriocins from gram-positive bacteria. Appl Environ Microbiol. 1994 Feb;60(2):752–755. doi: 10.1128/aem.60.2.752-755.1994. [DOI] [PMC free article] [PubMed] [Google Scholar]
  122. Sano Y., Kobayashi M., Kageyama M. Functional domains of S-type pyocins deduced from chimeric molecules. J Bacteriol. 1993 Oct;175(19):6179–6185. doi: 10.1128/jb.175.19.6179-6185.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Scherwitz K. M., Baldwin K. A., McKay L. L. Plasmid linkage of a bacteriocin-like substance in Streptococcus lactis subsp. diacetylactis strain WM4: transferability to Streptococcus lactis. Appl Environ Microbiol. 1983 May;45(5):1506–1512. doi: 10.1128/aem.45.5.1506-1512.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  124. Schillinger U., Lücke F. K. Antibacterial activity of Lactobacillus sake isolated from meat. Appl Environ Microbiol. 1989 Aug;55(8):1901–1906. doi: 10.1128/aem.55.8.1901-1906.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  125. Schnell N., Engelke G., Augustin J., Rosenstein R., Ungermann V., Götz F., Entian K. D. Analysis of genes involved in the biosynthesis of lantibiotic epidermin. Eur J Biochem. 1992 Feb 15;204(1):57–68. doi: 10.1111/j.1432-1033.1992.tb16605.x. [DOI] [PubMed] [Google Scholar]
  126. Schnell N., Entian K. D., Götz F., Hörner T., Kellner R., Jung G. Structural gene isolation and prepeptide sequence of gallidermin, a new lanthionine containing antibiotic. FEMS Microbiol Lett. 1989 Apr;49(2-3):263–267. doi: 10.1016/0378-1097(89)90050-5. [DOI] [PubMed] [Google Scholar]
  127. Schnell N., Entian K. D., Schneider U., Götz F., Zähner H., Kellner R., Jung G. Prepeptide sequence of epidermin, a ribosomally synthesized antibiotic with four sulphide-rings. Nature. 1988 May 19;333(6170):276–278. doi: 10.1038/333276a0. [DOI] [PubMed] [Google Scholar]
  128. Schved F., Lalazar A., Henis Y., Juven B. J. Purification, partial characterization and plasmid-linkage of pediocin SJ-1, a bacteriocin produced by Pediococcus acidilactici. J Appl Bacteriol. 1993 Jan;74(1):67–77. doi: 10.1111/j.1365-2672.1993.tb02998.x. [DOI] [PubMed] [Google Scholar]
  129. Schüller F., Benz R., Sahl H. G. The peptide antibiotic subtilin acts by formation of voltage-dependent multi-state pores in bacterial and artificial membranes. Eur J Biochem. 1989 Jun 1;182(1):181–186. doi: 10.1111/j.1432-1033.1989.tb14815.x. [DOI] [PubMed] [Google Scholar]
  130. Scott J. C., Sahl H. G., Carne A., Tagg J. R. Lantibiotic-mediated anti-lactobacillus activity of a vaginal Staphylococcus aureus isolate. FEMS Microbiol Lett. 1992 May 15;72(1):97–102. doi: 10.1016/0378-1097(92)90496-b. [DOI] [PubMed] [Google Scholar]
  131. Siezen R. J., de Vos W. M., Leunissen J. A., Dijkstra B. W. Homology modelling and protein engineering strategy of subtilases, the family of subtilisin-like serine proteinases. Protein Eng. 1991 Oct;4(7):719–737. doi: 10.1093/protein/4.7.719. [DOI] [PubMed] [Google Scholar]
  132. Simpson W. J., Tagg J. R. M-type 57 group A streptococcus bacteriocin. Can J Microbiol. 1983 Oct;29(10):1445–1451. doi: 10.1139/m83-221. [DOI] [PubMed] [Google Scholar]
  133. Song H. Y., Cramer W. A. Membrane topography of ColE1 gene products: the immunity protein. J Bacteriol. 1991 May;173(9):2935–2943. doi: 10.1128/jb.173.9.2935-2943.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  134. Steele J. L., McKay L. L. Partial characterization of the genetic basis for sucrose metabolism and nisin production in Streptococcus lactis. Appl Environ Microbiol. 1986 Jan;51(1):57–64. doi: 10.1128/aem.51.1.57-64.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  135. Steen M. T., Chung Y. J., Hansen J. N. Characterization of the nisin gene as part of a polycistronic operon in the chromosome of Lactococcus lactis ATCC 11454. Appl Environ Microbiol. 1991 Apr;57(4):1181–1188. doi: 10.1128/aem.57.4.1181-1188.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  136. Stevens K. A., Sheldon B. W., Klapes N. A., Klaenhammer T. R. Nisin treatment for inactivation of Salmonella species and other gram-negative bacteria. Appl Environ Microbiol. 1991 Dec;57(12):3613–3615. doi: 10.1128/aem.57.12.3613-3615.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Stoddard G. W., Petzel J. P., van Belkum M. J., Kok J., McKay L. L. Molecular analyses of the lactococcin A gene cluster from Lactococcus lactis subsp. lactis biovar diacetylactis WM4. Appl Environ Microbiol. 1992 Jun;58(6):1952–1961. doi: 10.1128/aem.58.6.1952-1961.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  138. Sung M. W., Johnson J. T., Van Dongen G., Whiteside T. L. Protective effects of interferon-gamma on squamous-cell carcinoma of head and neck targets in antibody-dependent cellular cytotoxicity mediated by human natural killer cells. Int J Cancer. 1996 May 3;66(3):393–399. doi: 10.1002/(SICI)1097-0215(19960503)66:3<393::AID-IJC21>3.0.CO;2-B. [DOI] [PubMed] [Google Scholar]
  139. Tagg J. R., Bannister L. V. "Fingerprinting" beta-haemolytic streptococci by their production of and sensitivity to bacteriocine-like inhibitors. J Med Microbiol. 1979 Nov;12(4):397–411. doi: 10.1099/00222615-12-4-397. [DOI] [PubMed] [Google Scholar]
  140. Tagg J. R., Dajani A. S., Wannamaker L. W. Bacteriocins of gram-positive bacteria. Bacteriol Rev. 1976 Sep;40(3):722–756. doi: 10.1128/br.40.3.722-756.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  141. Tagg J. R., McGiven A. R. Some possible autoimmune mechanisms in rheumatic carditis. Lancet. 1972 Sep 30;2(7779):686–688. doi: 10.1016/s0140-6736(72)92091-0. [DOI] [PubMed] [Google Scholar]
  142. Tagg J. R., Skjold S., Wannamaker L. W. Transduction of bacteriocin determinants in group A streptococci. J Exp Med. 1976 Jun 1;143(6):1540–1544. doi: 10.1084/jem.143.6.1540. [DOI] [PMC free article] [PubMed] [Google Scholar]
  143. Tagg J. R., Wannamaker L. W. Genetic basis of streptococcin A-FF22 production. Antimicrob Agents Chemother. 1976 Aug;10(2):299–306. doi: 10.1128/aac.10.2.299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  144. Tagg J. R., Wannamaker L. W. Streptococcin A-FF22: nisin-like antibiotic substance produced by a group A streptococcus. Antimicrob Agents Chemother. 1978 Jul;14(1):31–39. doi: 10.1128/aac.14.1.31. [DOI] [PMC free article] [PubMed] [Google Scholar]
  145. Tahara T., Kanatani K., Yoshida K., Miura H., Sakamoto M., Oshimura M. Purification and some properties of acidocin 8912, a novel bacteriocin produced by Lactobacillus acidophilus TK8912. Biosci Biotechnol Biochem. 1992 Aug;56(8):1212–1215. doi: 10.1271/bbb.56.1212. [DOI] [PubMed] [Google Scholar]
  146. Tichaczek P. S., Vogel R. F., Hammes W. P. Cloning and sequencing of curA encoding curvacin A, the bacteriocin produced by Lactobacillus curvatus LTH1174. Arch Microbiol. 1993;160(4):279–283. doi: 10.1007/BF00292077. [DOI] [PubMed] [Google Scholar]
  147. Tichaczek P. S., Vogel R. F., Hammes W. P. Cloning and sequencing of sakP encoding sakacin P, the bacteriocin produced by Lactobacillus sake LTH 673. Microbiology. 1994 Feb;140(Pt 2):361–367. doi: 10.1099/13500872-140-2-361. [DOI] [PubMed] [Google Scholar]
  148. Tsai H. J., Sandine W. E. Conjugal transfer of nisin plasmid genes from Streptococcus lactis 7962 to Leuconostoc dextranicum 181. Appl Environ Microbiol. 1987 Feb;53(2):352–357. doi: 10.1128/aem.53.2.352-357.1987. [DOI] [PMC free article] [PubMed] [Google Scholar]
  149. Upreti G. C., Hinsdill R. D. Isolation and characterization of a bacteriocin from a homofermentative Lactobacillus. Antimicrob Agents Chemother. 1973 Oct;4(4):487–494. doi: 10.1128/aac.4.4.487. [DOI] [PMC free article] [PubMed] [Google Scholar]
  150. Upreti G. C., Hinsdill R. D. Production and mode of action of lactocin 27: bacteriocin from a homofermentative Lactobacillus. Antimicrob Agents Chemother. 1975 Feb;7(2):139–145. doi: 10.1128/aac.7.2.139. [DOI] [PMC free article] [PubMed] [Google Scholar]
  151. Van de Ven F. J., Van den Hooven H. W., Konings R. N., Hilbers C. W. NMR studies of lantibiotics. The structure of nisin in aqueous solution. Eur J Biochem. 1991 Dec 18;202(3):1181–1188. doi: 10.1111/j.1432-1033.1991.tb16488.x. [DOI] [PubMed] [Google Scholar]
  152. Vaughan E. E., Daly C., Fitzgerald G. F. Identification and characterization of helveticin V-1829, a bacteriocin produced by Lactobacillus helveticus 1829. J Appl Bacteriol. 1992 Oct;73(4):299–308. doi: 10.1111/j.1365-2672.1992.tb04981.x. [DOI] [PubMed] [Google Scholar]
  153. Venema K., Abee T., Haandrikman A. J., Leenhouts K. J., Kok J., Konings W. N., Venema G. Mode of Action of Lactococcin B, a Thiol-Activated Bacteriocin from Lactococcus lactis. Appl Environ Microbiol. 1993 Apr;59(4):1041–1048. doi: 10.1128/aem.59.4.1041-1048.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  154. Vogel H., Nilsson L., Rigler R., Meder S., Boheim G., Beck W., Kurth H. H., Jung G. Structural fluctuations between two conformational states of a transmembrane helical peptide are related to its channel-forming properties in planar lipid membranes. Eur J Biochem. 1993 Mar 1;212(2):305–313. doi: 10.1111/j.1432-1033.1993.tb17663.x. [DOI] [PubMed] [Google Scholar]
  155. Von Tersch M. A., Carlton B. C. Bacteriocin from Bacillus megaterium ATCC 19213: comparative studies with megacin A-216. J Bacteriol. 1983 Aug;155(2):866–871. doi: 10.1128/jb.155.2.866-871.1983. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Weil H. P., Beck-Sickinger A. G., Metzger J., Stevanovic S., Jung G., Josten M., Sahl H. G. Biosynthesis of the lantibiotic Pep5. Isolation and characterization of a prepeptide containing dehydroamino acids. Eur J Biochem. 1990 Nov 26;194(1):217–223. doi: 10.1111/j.1432-1033.1990.tb19446.x. [DOI] [PubMed] [Google Scholar]
  157. Worobo R. W., Henkel T., Sailer M., Roy K. L., Vederas J. C., Stiles M. E. Characteristics and genetic determinant of a hydrophobic peptide bacteriocin, carnobacteriocin A, produced by Carnobacterium piscicola LV17A. Microbiology. 1994 Mar;140(Pt 3):517–526. doi: 10.1099/00221287-140-3-517. [DOI] [PubMed] [Google Scholar]
  158. Yang R., Johnson M. C., Ray B. Novel method to extract large amounts of bacteriocins from lactic acid bacteria. Appl Environ Microbiol. 1992 Oct;58(10):3355–3359. doi: 10.1128/aem.58.10.3355-3359.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  159. Zajdel J. K., Ceglowski P., Dobrazański W. T. Mechanism of action of lactostrepcin 5, a bacteriocin produced by Streptococcus cremoris 202. Appl Environ Microbiol. 1985 Apr;49(4):969–974. doi: 10.1128/aem.49.4.969-974.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  160. de Vos W. M., Mulders J. W., Siezen R. J., Hugenholtz J., Kuipers O. P. Properties of nisin Z and distribution of its gene, nisZ, in Lactococcus lactis. Appl Environ Microbiol. 1993 Jan;59(1):213–218. doi: 10.1128/aem.59.1.213-218.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  161. van Belkum M. J., Hayema B. J., Geis A., Kok J., Venema G. Cloning of two bacteriocin genes from a lactococcal bacteriocin plasmid. Appl Environ Microbiol. 1989 May;55(5):1187–1191. doi: 10.1128/aem.55.5.1187-1191.1989. [DOI] [PMC free article] [PubMed] [Google Scholar]
  162. van Belkum M. J., Hayema B. J., Jeeninga R. E., Kok J., Venema G. Organization and nucleotide sequences of two lactococcal bacteriocin operons. Appl Environ Microbiol. 1991 Feb;57(2):492–498. doi: 10.1128/aem.57.2.492-498.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  163. van Belkum M. J., Kok J., Venema G. Cloning, sequencing, and expression in Escherichia coli of lcnB, a third bacteriocin determinant from the lactococcal bacteriocin plasmid p9B4-6. Appl Environ Microbiol. 1992 Feb;58(2):572–577. doi: 10.1128/aem.58.2.572-577.1992. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. van Belkum M. J., Kok J., Venema G., Holo H., Nes I. F., Konings W. N., Abee T. The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner. J Bacteriol. 1991 Dec;173(24):7934–7941. doi: 10.1128/jb.173.24.7934-7941.1991. [DOI] [PMC free article] [PubMed] [Google Scholar]
  165. van der Meer J. R., Polman J., Beerthuyzen M. M., Siezen R. J., Kuipers O. P., De Vos W. M. Characterization of the Lactococcus lactis nisin A operon genes nisP, encoding a subtilisin-like serine protease involved in precursor processing, and nisR, encoding a regulatory protein involved in nisin biosynthesis. J Bacteriol. 1993 May;175(9):2578–2588. doi: 10.1128/jb.175.9.2578-2588.1993. [DOI] [PMC free article] [PubMed] [Google Scholar]
  166. van der Meer J. R., Rollema H. S., Siezen R. J., Beerthuyzen M. M., Kuipers O. P., de Vos W. M. Influence of amino acid substitutions in the nisin leader peptide on biosynthesis and secretion of nisin by Lactococcus lactis. J Biol Chem. 1994 Feb 4;269(5):3555–3562. [PubMed] [Google Scholar]

Articles from Microbiological Reviews are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES