Phage lysin LysK can be truncated to its CHAP domain and retain lytic activity against live antibiotic-resistant staphylococci.
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.
Horgan
Marianne
M
Teagasc, Moorepark Food Research Centre, Fermoy, County Cork, Ireland.
O'Flynn
Gary
G
Garry
Jennifer
J
Cooney
Jakki
J
Coffey
Aidan
A
Fitzgerald
Gerald F
GF
Ross
R Paul
RP
McAuliffe
Olivia
O
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D001433:Bacteriolysis; D001435:Bacteriophages / Q000201:enzymology*; D024881:Drug Resistance, Bacterial; D009088:Mucoproteins / Q000235:genetics* / Q000378:metabolism*; D017384:Sequence Deletion; D013203:Staphylococcal Infections / Q000382:microbiology; D013210:Staphylococcus / Q000187:drug effects* / Q000302:isolation & purification
D000900:Anti-Bacterial Agents; D009088:Mucoproteins; C010393:lysin, gastropoda