Skip to main content

Lactococcal Bacteriocins: Genetics and Mode of Action

  • Conference paper
Bacteriocins, Microcins and Lantibiotics

Part of the book series: NATO ASI Series ((ASIH,volume 65))

  • 292 Accesses

Abstract

Lactic acid bacteria produce a variety of antimicrobial substances which are important in food fermentation and preservation. In several instances, the inhibitory activity results from metabolic end products such as hydrogen peroxide, diacetyl, and organic acids (Lindgren & Dobrogosz, 1990). In addition, the bactericidal activity of many strains appeared to result from bacteriocin production (Klaenhammer, 1988). Although bacteriocins of lactic acid bacteria have been the subject of many studies, only little is known about their chemical structure, their mode of action, and their genetic determinants. In recent years, the increasing interest in bacteriocins produced by these organisms has resulted in the cloning and genetic characterization of several bacteriocin determinants (Joerger & Klaenhammer, 1990; Marugg, 1991; Muriana & Klaenhammer, 1991). From lactococci, the structural gene for the lantibiotic nisin has been cloned and sequenced by several groups (Buchman et al., 1988; Kaletta & Entian, 1989; Dodd et al., 1990). The genetic determinant for bacteriocin production byLactococcus lactis subsp. lactis WM4 was shown to be associated with the 131-kb plasmid pNP2 (Scherwitz et al., 1983). Cloning experiments inL. lactis identified an 18.4-kb DNA region containing the bacteriocin determinant (Scherwitz-Harmon & McKay, 1987).

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Bourdineaud JP, Boulanger P, Lazdunski C, Letellier L (1990) In vivo properties of colicin A: Channel activity is voltage dependent but translocation may be voltage independent. Proc Natl Acad Sci USA 87:1037–1041.

    Article  PubMed  CAS  Google Scholar 

  • Buchman, GW, Baneijee S, Hansen JN (1988) Structure, expression, and evolution of a gene encoding the precursor of nisin, a small protein antibiotic. J Biol Chem 263:16260–16266.

    PubMed  CAS  Google Scholar 

  • Dodd HM, Horn N, Gasson M J (1990) Analysis of the genetic determinant for the production of the peptide antibiotic nisin. J Gen Microbiol 136:555–566.

    PubMed  CAS  Google Scholar 

  • Gao FH, Abee T, Konings WN (1991) The mechanism of action of the peptide antibiotic nisin in liposomes and cytochromec oxidase proteoliposomes. Appl Environ Microbiol 57:2164–2170.

    PubMed  CAS  Google Scholar 

  • Geis A, Singh J, Teuber M (1983) Potential of lactic streptococci to produce bacteriocin. Appl Environ Microbiol 45:205–211.

    PubMed  CAS  Google Scholar 

  • Henderson JT, Chopko AL, van Wassenaar P.D (1991) Purification and primary structure of the bacteriocin PA-1 produced by Pediococcus acidilactici PAC-l.O. Manuscript submitted.

    Google Scholar 

  • Holo H, Nilssen O, Nes IF (1991) Lactococcin A, a new bacteriocin from Lactococcus lactis subsp. cremoris: isolation and characterization of the protein and its gene. J Bacteriol 173:3879–3887.

    PubMed  CAS  Google Scholar 

  • Joerger MC, Klaenhammer TR (1990) Cloning, expression, and nucleotide sequence of the Lactobacillus helveticus 481 gene encoding the bacteriocin helveticin J. J Bacteriol 172:6339–6347

    PubMed  CAS  Google Scholar 

  • Kaletta C, Entian K-D (1989) Nisin, a peptide antibiotic: cloning and sequencing of the nisA gene and posttranslational processing of its peptide product. J Bacteriol 171:1597–1601.

    PubMed  CAS  Google Scholar 

  • Klaenhammer TR (1988) Bacteriocins of lactic acid bacteria. Biochimie 70:337–349.

    Article  PubMed  CAS  Google Scholar 

  • Konisky J (1982) Colicins and other bacteriocins with established modes of action. Ann Rev Microbiol 36:125–144

    Article  CAS  Google Scholar 

  • Kordel M, Benz R, Sahl H-G (1988) Mode of action of the staphylococcinlike peptide Pep5: voltagedependent depolarization of bacterial and artificial membranes. J Bacteriol 170:84–88

    PubMed  CAS  Google Scholar 

  • Lindgren SE, Dobrogosz WJ (1990) Antagonistic activities of lactic acid bacteria in food and feed fermentations. FEMS Microbiol Reviews 87:149–164

    Article  CAS  Google Scholar 

  • Marugg J (1991) Personal communication

    Google Scholar 

  • Muriana PM, Klaenhammer TR (1991) Cloning, phenotypic expression, and DNA sequence of the gene for lactacin F, an antimicrobial peptide produced by Lactobacillus spp. J Bacteriol 173:1779–1788

    PubMed  CAS  Google Scholar 

  • Neve H, Geis A, Teuber M (1984) Conjugal transfer and characterization of bacteriocin plasmids in group N (lactic acid) streptococci. J Bacteriol 157:833–838

    PubMed  CAS  Google Scholar 

  • Poolman B, Smid EJ, Konings WN (1987) Kinetic properties of a phosphate-bond-driven glutamate-glutamine transport system inStreptococcus lactis and Streptococcus cremoris. J Bacteriol 169:1460–1468

    PubMed  CAS  Google Scholar 

  • Pressler U, Braun V, Wittman-Liebold B, Benz R (1986) Structural and functional properties of colicin B. J Biol. Chem 261:2654–2659

    PubMed  CAS  Google Scholar 

  • Ruhr E, Sahl H-G (1985) 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 27:841–845

    PubMed  CAS  Google Scholar 

  • Schein SD, Kagan B, Finkelstein A (1978) Colicin K acts by forming voltage dependent channels in phospholipid bilayer membranes. Nature (London) 276:159–163

    Article  CAS  Google Scholar 

  • Scherwitz KM, Baldwin KA, McKay LL (1983) Plasmid linkage of a bacteriocin-like substance in Streptococcus lactis subsp. diacetylactis strain WM4: transferability to Streptococcus lactis. Appl Environ Microbiol 45:1506–1512

    PubMed  CAS  Google Scholar 

  • Scherwitz-Harmon KM, McKay LL (1987) Restriction enzyme analysis of lactose and bacteriocin plasmids from Streptococcus lactis subsp. diacety lactis WM4 and cloning of Bell fragments coding for bacteriocin production. Appl Environ Microbiol 53:1171–1174

    Google Scholar 

  • Schüller F, Benz R, Sahl H-G (1989) The peptide antibiotic subtilin acts by formation of voltagedependent multi-state pores in bacterial and artificial membranes. Eur J Biochem 182:181–186.

    Article  PubMed  Google Scholar 

  • van Belkum MJ, Hayema BJ, Geis A, Kok J, Venema G (1989) Cloning of two bacteriocin genes from a lactococcal bacteriocin plasmid. Appl Environ Microbiol 55:1187–1191

    PubMed  Google Scholar 

  • van Belkum MJ, Hayema BJ, Jeeninga RE, Kok J, Venema G (1991) Organization and nucleotide sequences of two lactococcal bacteriocin operons. Appl Environ Microbiol 57:492–498

    PubMed  Google Scholar 

  • van Belkum MJ, Kok J, Venema G, Holo H, Nes IF, Konings WN, Abee T (1991) The bacteriocin lactococcin A specifically increases permeability of lactococcal cytoplasmic membranes in a voltage-independent, protein-mediated manner. J Bacteriol 173:7934–7941.

    PubMed  Google Scholar 

  • van Belkum MJ, Kok J, Venema G (1992) Cloning, sequencing, and expression in Escherichia coli of IcnB, a third bacteriocin determinant from the lactococcal bacteriocin plasmid p9B4–6. In press.

    Google Scholar 

  • Wilmsen HU, Pugsley AP, Pattus F (1990) Colicin N forms voltage-and pH-dependent channels in planar lipid bilayer membranes. Eur Biophys J 18:149–158.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1992 Springer-Verlag Berlin Heidelberg

About this paper

Cite this paper

van Belkum, M.J. et al. (1992). Lactococcal Bacteriocins: Genetics and Mode of Action. In: James, R., Lazdunski, C., Pattus, F. (eds) Bacteriocins, Microcins and Lantibiotics. NATO ASI Series, vol 65. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-76974-0_7

Download citation

  • DOI: https://doi.org/10.1007/978-3-642-76974-0_7

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-642-76976-4

  • Online ISBN: 978-3-642-76974-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics