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Antibacterial Activity of Bacteriophage Lytic Enzyme Ply900

Yuan Li1, Luxiang Xu1, Yuhan Zhang1

  • 1College of Veterinary Medicine (Preventive Veterinary Medicine), Northeast Agricultural University, No. 600, Changjiang Road, Xiangfang District, Harbin 150030, China.

Veterinary Sciences
|January 28, 2026
PubMed

Insights

The bacteriophage lytic enzyme Ply900 effectively combats Streptococcus suis infections in mice, showing broad antibacterial activity and stability. This lysin offers a promising new strategy against multi-drug resistant bacterial pathogens.

Area of Science:

  • Microbiology
  • Bacteriophage Therapy
  • Antimicrobial Resistance

Background:

  • Streptococcus suis (S. suis) is a significant zoonotic pathogen causing severe diseases in both animals and humans.
  • The rise of multi-drug resistance (MDR) in bacteria necessitates the development of alternative antibacterial treatments.
  • Bacteriophage-derived lysins represent a promising class of antimicrobials.

Purpose of the Study:

  • To evaluate the antibacterial potential and therapeutic efficacy of the bacteriophage lytic enzyme Ply900 against S. suis.
  • To analyze the functional domains of Ply900 and elucidate its mechanism of action.
  • To assess the in vivo therapeutic dynamics and resistance development potential of Ply900.

Main Methods:

  • In vitro lytic activity assays against various bacterial strains.
  • Biochemical stability tests under different environmental conditions.
  • In vivo efficacy study using a mouse model of S. suis infection, including survival rate analysis.
  • Mechanistic analysis of Ply900's domain functions and key amino acid residues involved in cleavage.

Main Results:

  • Ply900 demonstrated potent lytic activity against S. suis, S. agalactiae, and S. aureus.
  • The enzyme exhibited broad biochemical stability, tolerating diverse conditions.
  • In vivo studies showed effective S. suis eradication and improved survival rates in infected mice.
  • No induced resistance to Ply900 was observed in the treated bacterial populations.
  • The SH3B and CHAP domains were identified as crucial for synergistic peptidoglycan binding and cleavage.

Conclusions:

  • Lysin Ply900 is a potent antibacterial agent with broad-spectrum activity and stability.
  • Ply900 demonstrates significant therapeutic potential for treating S. suis infections in vivo.
  • The enzyme's mechanism involves synergistic domain interactions, and no resistance was induced, highlighting its promise for clinical and agricultural applications.
Keywords:
Streptococcus suisantibiotic replacementbacteriophage lytic enzymemulti-drug resistance

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