Identification of TSPphg as a Bacteriophage Endolysin with Peptidoglycan-Degrading and Bacteriolytic Activity
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Feng Wang, Xinyu Ji and Lianbing Lin
With the serious emergence and dissemination of bacterial drug resistance worldwide, there is a critical need to find alternatives to common antibiotics for the treatment of bacterial infections. Previously, by decoding the complete genome of Thermus phage TSP4 belonging to the family of Siphoviridae, we have identified a bacteriophage lytic protein named TSPphg, which is heat-stable below the temperature of 70 °C and has considerable bacteriolytic activity. Here, we further performed the molecular modelling of TSPphg and found that His24 in motif HXXXD and His109 in motif HXH are functional residues that are critical for its antimicrobial activity. LC-MS analysis further confirmed that TSPphg has specific peptidoglycan-degrading activity, causing lysis of bacterial cell walls and thus bacteria destruction. These results suggest the potential application of TSPphg in combating antibiotic-resistant pathogenic bacteria and provide insights into the bacteriophage-based strategies to tackle the menacing bacterial infections.
Bacteriophage; lysins; drug resistance; bacterial infections