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Published on: September 28, 2022
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.
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.
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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