Enhanced staphylolytic activity of the Staphylococcus aureus bacteriophage vB—SauS-philPLA88 virion-associated peptidoglycan hydrolase HydH5: fusions, deletions and synergy with LysH5

Abstract

Virion-associated peptidoglycan hydrolases have a potential as antimicrobial agents due to their ability to lyse Gram positive bacteria on contact. Full-length HydH5, a virion-associated peptidoglycan hydrolase from the Staphylococcus aureus bacteriophage vB_SauS-phi-IPLA88, and two truncated derivatives, containing only the CHAP domain, exhibited high lytic activity against live S. aureus cells. Three different fusion proteins were created and showed higher staphylolytic activity than the parental enzyme or its deletion construct. Parental and fusion proteins lysed S. aureus cells in zymograms, plate lysis and turbidity reduction assays. In plate lysis assays, HydH5 and its derivative fusions lysed bovine and human S. aureus, S. aureus MRSA N315 strain, and human Staphylococcus epidermidis strains. HydH5 and its derivative fusions proteins displayed antimicrobial synergy with the endolysin LysH5 in vitro suggesting that the two enzymes have distinct cut sites and thus may be more efficient in combination for the elimination of staphylococcal infections.

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