Taking aim on bacterial pathogens: from phage therapy to enzybiotics

Curr Opin Microbiol. 2007 Oct;10(5):461-72. doi: 10.1016/j.mib.2007.08.002. Epub 2007 Sep 27.


The bactericidal activity of bacteriophages has been used to treat human infections for years as an alternative or a complement to antibiotic therapy. Nowadays, endolysins (phage-encoded enzymes that break down bacterial peptidoglycan at the terminal stage of the phage reproduction cycle) have been used successfully to control antibiotic-resistant pathogenic bacteria in animal models. Their cell wall binding domains target the enzymes to their substrate, and their corresponding catalytic domains are able to cleave bonds in the peptidoglycan network. Recent research has not only revealed the surprising rich structural catalytic diversity of these murein hydrolases but has also yielded insights into their modular organization, their three-dimensional structures, and their mechanism of recognition of bacterial cell wall. These results allow endolysins to be considered as effective antimicrobials with potentially important applications in medicine and biotechnology.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology
  • Bacteria / cytology
  • Bacteria / drug effects*
  • Bacterial Infections / therapy
  • Bacteriolysis / drug effects
  • Bacteriophages / enzymology*
  • Cell Wall / drug effects
  • Endopeptidases / chemistry
  • Endopeptidases / pharmacology
  • Models, Molecular
  • N-Acetylmuramoyl-L-alanine Amidase / chemistry
  • N-Acetylmuramoyl-L-alanine Amidase / pharmacology
  • Protein Structure, Tertiary
  • Substrate Specificity
  • Viral Proteins / chemistry
  • Viral Proteins / pharmacology*
  • Virion / enzymology


  • Anti-Bacterial Agents
  • Viral Proteins
  • Endopeptidases
  • endolysin
  • N-Acetylmuramoyl-L-alanine Amidase