Modified lactic acid bacteria detect and inhibit multiresistant enterococci

ACS Synth Biol. 2015 Mar 20;4(3):299-306. doi: 10.1021/sb500090b. Epub 2014 Jun 16.

Abstract

We designed Lactococcus lactis to detect Enterococcus faecalis. Upon detection, L. lactis produce and secrete antienterococcal peptides. The peptides inhibit enterococcal growth and reduce viability of enterococci in the vicinity of L. lactis. The enterococcal sex pheromone cCF10 serves as the signal for detection. Expression vectors derived from pCF10, a cCF10-responsive E. faecalis sex-pheromone conjugative plasmid, were engineered in L. lactis for the detection system. Recombinant host strains were engineered to express genes for three bacteriocins, enterocin A, hiracin JM79 and enterocin P, each with potent antimicrobial activity against E. faecalis. Sensitive detection and specific inhibition occur both in agar and liquid media. The engineered L. lactis also inhibited growth of multidrug-resistant E. faecium strains, when induced by cCF10. The presented vectors and strains can be components of a toolbox for the development of alternative antibiotic technologies targeting enterococci at the site of infection.

Keywords: Enterococcus faecalis; Lactococcus lactis; drug delivery vector; lactic acid bacteria; recombinant plasmids.

Publication types

  • Research Support, American Recovery and Reinvestment Act
  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Bacteriocin Plasmids / genetics*
  • Bacteriocins / genetics
  • Bacteriocins / metabolism
  • Bacteriocins / pharmacology*
  • Biosensing Techniques / methods*
  • Enterococcus faecalis / drug effects*
  • Enterococcus faecalis / isolation & purification*
  • Lactococcus lactis / genetics*
  • Lactococcus lactis / metabolism
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Recombinant Proteins / pharmacology

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • Recombinant Proteins