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

Marianne Horgan1, Gary O'Flynn, Jennifer Garry

  • 1Teagasc, Moorepark Food Research Centre, Fermoy, County Cork, Ireland.

Insights

A truncated phage lysin, LysK’s CHAP domain, shows potent lytic activity against Staphylococcus aureus, including MRSA. This truncated enzyme offers a promising new strategy for combating staphylococcal infections.

Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Bacteriophage endolysins are enzymes that degrade bacterial cell walls.
  • LysK is a phage endolysin with known antibacterial properties.
  • Staphylococcus aureus, particularly methicillin-resistant Staphylococcus aureus (MRSA), poses a significant public health threat.

Purpose of the Study:

  • To investigate the lytic activity of a truncated LysK endolysin derivative.
  • To determine if the CHAP domain alone retains antibacterial function.
  • To assess the efficacy against clinical isolates of Staphylococcus aureus.

Main Methods:

  • Purification of the truncated LysK endolysin containing the CHAP domain.
  • Testing the lytic activity of the purified enzyme against various Staphylococcus aureus strains.
  • Evaluating activity against live clinical isolates, including MRSA.

Main Results:

  • The truncated LysK derivative, comprising solely the CHAP domain, demonstrated significant lytic activity.
  • The enzyme was effective against multiple live clinical isolates of Staphylococcus aureus.
  • High lytic activity was observed against methicillin-resistant Staphylococcus aureus (MRSA).

Conclusions:

  • A truncated phage endolysin (LysK's CHAP domain) retains potent lytic activity against Staphylococcus aureus.
  • This truncated enzyme represents a novel and potentially effective therapeutic agent.
  • This finding opens new avenues for developing antimicrobial strategies against resistant staphylococci.

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