Abstract: 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 S. aureus, including MRSA. Lysostaphin is a bacteriocin secreted by S. simulans to kill S. aureus, and has been shown to also be a potent antimicrobial for many antibiotic resistant strains of S. aureus. 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.

Abstract: 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, live Staphylococcus aureus from 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.

Abstract: 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, live Staphylococcus aureus from 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.

Abstract: 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 S. aureus, including MRSA. Lysostaphin is a bacteriocin secreted by S. simulans to kill S. aureus, and has been shown to also be a potent antimicrobial for many antibiotic resistant strains of S. aureus. 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.

Abstract: A flexible bag is formed with a opening for placing the bag about the head of the patient and a separate connector for connection to an air supply. The open end has a closure unit permitting the collapse of the opening about the neck to enclose the head. Alternatively, the open end can be placed beneath the ears and over the nose to enclose the upper portion of the head. A separation wall within the bag separates and defines an upper air supply chamber and a lower head heating chamber. The wall has openings including flaps to distribute the air from the air supply chamber to the head enclosing chamber and thereby heating the head with the blood passing therefrom to heat the body of the patient. The head heating chamber includes air directing elements therein. The air supply chamber is L-shaped to direct air over the top of the head and to the side or back of the head.