Requirement of autolytic activity for bacteriocin-induced lysis

Appl Environ Microbiol. 2000 Aug;66(8):3174-9. doi: 10.1128/AEM.66.8.3174-3179.2000.

Abstract

The bacteriocin produced by Lactococcus lactis IFPL105 is bactericidal against several Lactococcus and Lactobacillus strains. Addition of the bacteriocin to exponential-growth-phase cells resulted in all cases in bacteriolysis. The bacteriolytic response of the strains was not related to differences in sensitivity to the bacteriocin and was strongly reduced in the presence of autolysin inhibitors (Co(2+) and sodium dodecyl sulfate). When L. lactis MG1363 and its derivative deficient in the production of the major autolysin AcmA (MG1363acmADelta1) were incubated with the bacteriocin, the latter did not lyse and no intracellular proteins were released into the medium. Incubation of cell wall fragments of L. lactis MG1363, or of L. lactis MG1363acmADelta1 to which extracellular AcmA was added, in the presence or absence of the bacteriocin had no effect on the speed of cell wall degradation. This result indicates that the bacteriocin does not degrade cell walls, nor does it directly activate the autolysin AcmA. The autolysin was also responsible for the observed lysis of L. lactis MG1363 cells during incubation with nisin or the mixture of lactococcins A, B, and M. The results presented here show that lysis of L. lactis after addition of the bacteriocins is caused by the resulting cell damage, which promotes uncontrolled degradation of the cell walls by AcmA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacteriocins / metabolism*
  • Bacteriocins / pharmacology*
  • Bacteriolysis*
  • Cell Wall / metabolism
  • Enzyme Activation
  • Lactobacillus / drug effects
  • Lactobacillus / growth & development
  • Lactococcus / drug effects
  • Lactococcus / growth & development
  • Lactococcus lactis / genetics
  • Lactococcus lactis / growth & development
  • Lactococcus lactis / metabolism*
  • Muramidase / metabolism
  • N-Acetylmuramoyl-L-alanine Amidase / metabolism*

Substances

  • Bacteriocins
  • AcmA protein, Lactococcus lactis
  • Muramidase
  • N-Acetylmuramoyl-L-alanine Amidase