1887

Microbiology Society logo

Volume 142, Issue 9

Lactococcin 972: a homodimeric lactococcal bacteriocin whose primary target is not the plasma membrane Free

Abstract

subsp. IPLA 972 was shown to produce a bacteriocin which had a bactericidal effect on sensitive lactococci. Production of lactococcin 972 reached a maximum during the late-exponential phase of growth. The bacteriocinogenic activity was heat-sensitive, active in the pH range 4·0–9·0 and showed low susceptibility to proteases. Purification of the bacteriocin rendered a single polypeptide of 7·5 kDa (monomer) as shown by SDS-PAGE. Gels overlaid with a lawn of sensitive bacteria showed inhibitory activity at a point corresponding to 15 kDa. Changes in the electrophoretic conditions allowed the detection of a band at a position corresponding to that expected for a hypothetical dimer. Sequencing of the NH-terminal end of lactococcin 972 revealed the sequence NH-EGTWQHGYGV, which is not related to any other bacteriocin sequence present in the databases. Finally, lactococcin 972 did not induce the efflux of compounds previously incorporated into the cytoplasm of sensitive cultures nor did it inhibit macromolecular synthesis, suggesting that, in contrast to other bacteriocins, its primary target is not the plasma membrane.

  • Received:
  • Accepted:
  • Published Online:
Keyword(s): bacteriocin , Lactococcus , mode of action and structure
© Society for General Microbiology 1996
Loading

Article metrics loading...

/content/journal/micro/10.1099/00221287-142-9-2393
1996-09-01
2024-04-20
Loading full text...

Full text loading...

/deliver/fulltext/micro/142/9/mic-142-9-2393.html?itemId=/content/journal/micro/10.1099/00221287-142-9-2393&mimeType=html&fmt=ahah

References

  1. Abee T., Klaenhammer T. R., Letellier L. 1994; Kinetics studies of the action of lacticin F, a bacteriocin produced by Lactobacillus johnsonii that forms poration complexes in the cytoplasmic membrane. Appl Environ Microbiol 60:1006–1013
     [Google Scholar]
  2. Allison G. E., Fremaux C., Klaenhammer T. R. 1994; Expansion ot bacteriocin activity and host range upon complementation of two peptides encoded within the lactacin F operon. J Bacterial 176:2235–2241
     [Google Scholar]
  3. van Belkum M. J., Kok J., Venema G., Holo H., Nes I. F., Konings W. N., Abee T. 1991; The bacteriocin lactococcin A specifically increases the permeability of lactococcal cytoplasmic membranes in a vmltage-independent, protein-mediated manner. J Bacterial 173:7934–7941
     [Google Scholar]
  4. Bunhia A. K., Johnson M. C., Ray B. 1987; Direct detection of an antimicrobial peptide of Pediococcus addilactici in sodium dodecyl sulfate polyacrylamide gel electrophoresis. J Ind Microbiol 2:319–322
     [Google Scholar]
  5. Edman P., Begg G. 1967; A protein sequenator. Eur J Biocbem 1:80–81
     [Google Scholar]
  6. Food and Drug Administration 1988; Nisin preparation; affirmation of GRAS status as a direct human food ingredient. Food and Drug Administration Federal Regulation 5311247
     [Google Scholar]
  7. Gasson M. J. 1983; Plasmid complements of Streptococcus lactis NCDO 712 and other lactic streptococci after protoplast-induced curing. J Bacterial 154:1–9
     [Google Scholar]
  8. Geis A., Singh J., Teuber M. 1983; Potential of lactic streptococci to produce bacteriocin. Appl Emviron Microbiol 45:205–211
     [Google Scholar]
  9. González B., Arca P., Mayo B., Suárez J. E. 1994; Detection, purification, and partial characterization of plantaricin C, a bacteriocin produced by Lactobacillus piantarntn strain of dairy origin. Appl Environ Microbiol 60:2158–2163
     [Google Scholar]
  10. Jack R. W., Tagg J. R., Ray B. 1995; Bacteriocins of Grampositive bacteria. Microbiol Rev 59:171–200
     [Google Scholar]
  11. Jiménez-Díaz R., Ruíz-Barba J. L., Cathcart D. P., Holo H., Nes I. F., Sletten K. H., Warner P. J. 1995; Purification and partial amino acid sequence of plantaricin S, a bacteriocin produced by Lactobacillus planiarum LPCQ10, the activity of which depends on the complementary action of two peptides. Appl Environ Microbiol 61:4459–4463
     [Google Scholar]
  12. Joerger M. C., Klaenhammer T. R. 1986; Characterization and purification of helveticin J and evidence for a chromosomally determined bacteriocin produced by Eactobacilhis helveticus 481. J Bacterial 167:439–446
     [Google Scholar]
  13. Klaenhammer T. R. 1993; Genetics of bacteriocins produced by lactic acid bacteria. FEMS Microbiol Rev 12:39–86
     [Google Scholar]
  14. Martínez B., Suárez J. E., Rodríguez A. 1995; Antagonistic activities of wild lactococcal strains isolated from homemade cheeses. J Food Prot 58:1118–1123
     [Google Scholar]
  15. Morgan S., Ross R. P., Hill C. 1995; Bacteriolytic activity caused by the presence of a novel lactococcal plasmid encoding lactococcins A, B, and M. Appl Environ Microbiol 61:2995–3001
     [Google Scholar]
  16. Nettles C. G., Barefoot S. F. 1993; Biochemical and generic characteristics of bacteriocins of food associated lactic acid bacteria. J Food Prot 56:338–356
     [Google Scholar]
  17. Nissen-Meyer J., Holo H., Håvarstein L. S., Sletten K., Nes Y. F. 1992; A novel lactococcal bacteriocin whose activity depends on the complementary action of two peptides. J Bacterial 174:5686–5692
     [Google Scholar]
  18. Piard J. C., Desmazeaud M. 1991; Inhibiting factors produced by lactic acid bacteria. 1. Oxygen metabolites and catabolism end- products. Lait 71:525–541
     [Google Scholar]
  19. Piard J. C., Desmazeaud M. 1992; Inhibiting factors produced by lactic acid bacteria. 2. Bacteriocins and other antibacterial substances. Lait 72:113–142
     [Google Scholar]
  20. Reddish G. F. 1929; Methods for testing antiseptics. J Lab Clin Med 14:649–658
     [Google Scholar]
  21. Rodríguez A., Caso J.L, Suárez J. E. 1986; Characteristics of the developmental cycle of actinophage 𝜙C31. J Gen Microbiol 132:1695–1701
     [Google Scholar]
  22. Schägger H., von Jagow G. 1987; Tricine-sodium dodecyl sulphate-polyacrylamide gel electrophoresis For the separation of proteins in the range from 1 to 100 kDa. And Biochem 166:368–379
     [Google Scholar]
  23. Toba T., Yoshioka E., Itoh T. 1991a; Acidophilucin A, a new heat labile bacteriocin produced by Lactobacillus acidophilus LAPT 1060. Lett Appl Microbiol 12:106–108
     [Google Scholar]
  24. Toba T., Yoshioka E., Itoh T. 1991b; Lacticin, a bacteriocin produced by Lactobacillus delbrueckii subsp. lactis. . Lett Appl Microbiol 12:43–45
     [Google Scholar]
http://instance.metastore.ingenta.com/content/journal/micro/10.1099/00221287-142-9-2393
Loading
Lactococcin 972: a homodimeric lactococcal bacteriocin whose primary target is not the plasma membrane
Microbiology 142, 2393 (1996); https://doi.org/10.1099/00221287-142-9-2393
/content/journal/micro/10.1099/00221287-142-9-2393
/content/journal/micro/10.1099/00221287-142-9-2393
Loading

Data & Media loading...

Most cited Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error