Comparison of the antibacterial properties of phage endolysins SAL-1 and LysK

Antimicrob Agents Chemother. 2011 Apr;55(4):1764-7. doi: 10.1128/AAC.01097-10. Epub 2011 Jan 24.

Abstract

In spite of the high degree of amino acid sequence similarity between the newly discovered phage endolysin SAL-1 and the phage endolysin LysK, SAL-1 has an approximately 2-fold-lower MIC against several Staphylococcus aureus strains and higher bacterial cell-wall-hydrolyzing activity than LysK. The amino acid residue change contributing the most to this enhanced enzymatic activity is a change from glutamic acid to glutamine at the 114th residue.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / chemistry
  • Anti-Bacterial Agents / pharmacology*
  • Cell Wall / drug effects
  • Endopeptidases / chemistry
  • Endopeptidases / pharmacology*
  • Microbial Sensitivity Tests
  • Staphylococcus aureus / drug effects*

Substances

  • Anti-Bacterial Agents
  • Endopeptidases
  • endolysin