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Bacterial infections are responsible for significant morbidity and mortality in clinical settings.1 Many infections that would have been cured easily by antibiotics in the past now are resistant, resulting in sicker patients and longer hospitalizations. The endolysins of the bacteriophages are highly evolved molecules that have been specifically developed by phages to quickly and efficiently allow their progeny to be released from the host bacterium. These enzymes damage the bacterial cell wall’s integrity by hydrolyzing the four major bonds in its peptidoglycan component.2 The endolysins that have been characterized are amidases; usually do not have signal sequences to translocate them through the cytoplasmic membrane and cleave their substrate in the peptidoglycan. Instead, the endolysins’ translocation is controlled by a second phage gene products called holins.3 The bacteriophages during development in the infected bacterium, endolysin accumulates in the cytoplasm in until bacteriophage maturation. During a specific time controlled genetically, holin molecules inserted in the cytoplasmic membrane are activated, resulting in the formation of pores so the preformed endolysin in the cytoplasm can access the peptidoglycan, thereby causing cell lysis and the release of the new bacteriophages.3 Bacteriophages are able to lyse their targeted bacterial hosts, and this has been known for almost a century, and since the late 1910s bacteriophages have been used to prevent and treat human and animal diseases of bacterial origin. But bacteriophage-encoded enzymes have only recently begun to be used for various applications; e.g.: reducing bacterial contamination in dairy products and the preparation of bacterial vaccines.4,5 Materials and Methods

Extraction, Purification and Therapeutic Use of Bacteriophage Endolysin against Multi-Drug Resistant Staphylococcus aureus: in-vivo and in-vitro study