Host-Endolysins interactions

(Bacterio)phages are viruses that specifically infect bacteria. They are tremendously diverse and the most abundant living entities on Earth with an estimated total population size of 1031 phage particles. During infection they inject their DNA in the host bacteria and drive the cell machinery to produce new progeny phages. At the end of the infection cycle, phages (with the exception of a few known filamentous phages) produce enzymes called (endo)lysins that degrade the peptidoglycan (PG) leading to bacterial lysis and death in order to release the progeny virions. PG is a heteropolymer that protects the bacterial cell against osmotic pressure. The ability of endolysins to degrade PG causing the death of the bacterial cell makes these enzymes a very interesting biocontrol agent against problematic antibiotic resistant pathogenic bacteria. Considering that the muralytic activity of endolysins is directed to different bonds of the PG, which differs from species to species, it is conceivable that there is a relation between the endolysins and the bacteria that they target. This work is based on the oligonucleotide-stickiness method1, where the stickiness () – the binding analysis (or hybridization) stability of an oligo