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Phage P68 virion-associated protein 17 displays activity against clinical isolates of Staphylococcus aureus

Marian Takác1, Udo Bläsi

  • 1Max F. Perutz Laboratories, Department of Microbiology and Immunobiology, University Departments at the Vienna Biocenter, Dr. Bohrgasse 9/4, 1030 Vienna, Austria.

Antimicrobial Agents and Chemotherapy
|June 28, 2005
PubMed

Insights

Staphylococcus aureus bacteriophage P68 has a virion-associated muralytic enzyme, Protein 17, that weakens bacterial cell walls. This enzyme shows potential as a novel antimicrobial agent against resistant strains.

Area of Science:

  • Microbiology
  • Biochemistry

Background:

  • Phage-encoded murein hydrolases play roles in phage lysis or virion structure.
  • Understanding these enzymes is crucial for phage therapy development.

Purpose of the Study:

  • To characterize the muralytic enzyme from Staphylococcus aureus bacteriophage P68.
  • To investigate its function and potential as an antimicrobial.

Main Methods:

  • Structural and functional analysis of Protein 17.
  • Assays for muralytic activity and cell lysis induction.
  • Testing activity against clinical S. aureus isolates.

Main Results:

  • Staphylococcus aureus bacteriophage P68 possesses a virion-associated muralytic enzyme, Protein 17.
  • Protein 17 has a dual function: muralytic activity (N-terminus) and cell surface binding (C-terminus).
  • Protein 17 induces premature lysis and is active against phage-resistant S. aureus strains.

Conclusions:

  • Protein 17 weakens the bacterial murein layer, facilitating phage DNA entry.
  • Virion-associated muralytic enzymes like Protein 17 represent promising antimicrobial candidates.

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