Lytic enzymes of staphylococcal phages: Correlation between secondary structure and stability

Abstract

Lytic enzymes of bacteriophages K, phi11, and phi80α can lyse (destroy) cells of antibiotic-resistant strains of Staphylococcus aureus, which makes these enzymes promising antimicrobial agents. The stability of recombinant lysins of phages K, phi11, and phi80α was investigated under the conditions of storage and functioning, and the correlation between the stability and the secondary structure of the enzymes was found. It has been shown that the lower the content of disordered structures in the enzyme molecules, the greater the stability (half-inactivation time) of the lysins. At the storage temperature, the beta-structural lysin of phage phi11 shows the highest stability, while the phage K lysin with an alpha-helical structure and the phi80α lysin with a disordered secondary structure are less stable.