Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci

Appl Environ Microbiol. 2009 Feb;75(3):872-4. doi: 10.1128/AEM.01831-08. Epub 2008 Dec 1.

Abstract

A truncated derivative of the phage endolysin LysK containing only the CHAP (cysteine- and histidine-dependent amidohydrolase/peptidase) domain exhibited lytic activity against live clinical staphylococcal isolates, including methicillin-resistant Staphylococcus aureus. This is the first known report of a truncated phage lysin which retains high lytic activity against live staphylococcal cells.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Bacteriolysis*
  • Bacteriophages / enzymology*
  • Drug Resistance, Bacterial
  • Mucoproteins / genetics*
  • Mucoproteins / metabolism*
  • Sequence Deletion*
  • Staphylococcal Infections / microbiology
  • Staphylococcus / drug effects*
  • Staphylococcus / isolation & purification

Substances

  • Anti-Bacterial Agents
  • Mucoproteins
  • lysin, gastropoda