United States of America, As Represented by the Secretary of Agriculture

Stephen C Becker

David M Donovan

Multi-drug resistant superbugs are a persistent problem in modern health care. LysK is a staphylococcal bacteriophage endolysin from the phage K. It is a peptidoglycan hydrolase enzyme that can lyse many staphylococcal strains and thus is a potent antimicrobial against, including MRSA. Lysostaphin is a bacteriocin secreted byto kill, and has been shown to also be a potent antimicrobial for many antibiotic resistant strains of. This study describes optimal reaction conditions for the recombinant His-tagged LysK protein, compares its MIC and antimicrobial activity to lysostaphin and demonstrates synergy when the two are used in combination against the MRSA USA300.

Lys K endolysin is synergistic with lysostaphin against MRSA

Multi-drug resistant superbugs are a persistent problem in modern health care. This invention provides an antimicrobial endolysin-Lysostaphin triple fusion protein, comprising (1) an endolysin CHAP endopeptidase domain, (2) an endolysin amidase domain, and (3) a Lysostaphin glycyl-glycine endopeptidase domain. The domains are derived from two proteins that show antimicrobial synergy when used in combination. The protein has specificity and exolytic activity for the peptidoglycan cell wall of untreated, livefrom many growth phases i.e. stationary, logarithmic and biofilm growth. The recombinant triple fusion protein comprising the three functional antimicrobial domains is designed to be refractory to resistance development.

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Baltimore, MD, United States of America

Stephen C Becker