The Novel Phage-Derived Antimicrobial Agent HY-133 Is Active against Livestock-Associated Methicillin-Resistant Staphylococcus aureus

Antimicrob Agents Chemother. 2018 Jun 26;62(7):e00385-18. doi: 10.1128/AAC.00385-18. Print 2018 Jul.

Abstract

Livestock-associated methicillin-resistant Staphylococcus aureus (LA-MRSA) isolates are increasingly migrating from livestock into human and animal health care settings. Alternative substances are needed to overcome the drawbacks of currently available drugs used for MRSA eradication. The recombinant bacteriophage endolysin HY-133 has proved to be an active agent against S. aureus Here, the in vitro activity of HY-133 was studied against a large collection of genetically diverse LA-MRSA isolates revealing its high activity against mecA-, mecB-, and mecC-positive LA-MRSA.

Keywords: LA-MRSA; Staphylococcus aureus; antimicrobial agents; bacteriophage therapy; endolysin; livestock; susceptibility testing.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Animals
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / genetics
  • Bacteriophages / metabolism*
  • Endopeptidases / pharmacology*
  • Humans
  • Livestock
  • Methicillin-Resistant Staphylococcus aureus / drug effects*
  • Methicillin-Resistant Staphylococcus aureus / isolation & purification
  • Microbial Sensitivity Tests
  • Penicillin-Binding Proteins / genetics
  • Recombinant Proteins / pharmacology*
  • Staphylococcal Infections / drug therapy
  • Staphylococcal Infections / veterinary

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Penicillin-Binding Proteins
  • Recombinant Proteins
  • mecA protein, Staphylococcus aureus
  • Endopeptidases
  • HY-133
  • endolysin
  • Adenosine Triphosphatases