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February, 2014, vol. 3, special issue 2 (Biotechnology)
pages: 164-170
Article type: Biotechnology of Biotechnology
Abstract: Bacteriophage endolysins are peptidoglycan hydrolases, produced in the lytic system of bacteriophage in order to lyse host peptidoglycan from within and release virions into the environment. Phages infecting Gram-positive bacteria express endolysin genes with the characteristic modular structure, consisting of at least two functional domains: N-terminal enzymatically active domain (EAD) and C-terminal cell wall binding domain (CBD). CBDs specifically recognize ligands and bind to the bacterial cell wall, whereas EAD catalyze lysis of the peptidoglycan bonds. The reveal of endolysin modular structure leads to new opportunities for domain swapping, construction of chimeras and production of specifically engineered recombinant endolysins and their functional domains with the diverse biotechnological applications from without, such as in detection, elimination and biocontrol of pathogens, or as anti-bacterials in experimental therapy.
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