Abstract <p>Antibiotic resistance is a major global threat, especially in the case of such gram-negative pathogens as <i>Escherichia coli</i> and <i>Pseudomonas aeruginosa</i>. Bacteriophages encode many uncharacterized proteins, making them a potential source of new antimicrobial agents. We examined early proteins of the vB_EcoP_G7C (G7C) phage for antibacterial activity. Thirteen short (&lt;1000 bp) ORFs without known homologs were cloned into an inducible system and tested in <i>E. coli</i> and <i>P. aeruginosa</i>. Four proteins—strGp16.1, strGp17.1, strGp17.2, and strGp17.3—significantly inhibited bacterial growth, and strGp16.1 completely suppressed <i>P. aeruginosa</i> under experimental conditions. These findings indicate that early phage proteins can influence bacterial physiology and may provide a basis for novel antibacterial strategies.</p>

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Screening of the G7C Bacteriophage Early Proteins for Antibacterial Activity

  • S. Y. Rassadina,
  • V. A. Kasyanov,
  • M. Dmitrieva,
  • I. V. Kurdyumova,
  • D. A. Antonova,
  • O. S. Sokolova,
  • M. V. Yakunina

摘要

Abstract

Antibiotic resistance is a major global threat, especially in the case of such gram-negative pathogens as Escherichia coli and Pseudomonas aeruginosa. Bacteriophages encode many uncharacterized proteins, making them a potential source of new antimicrobial agents. We examined early proteins of the vB_EcoP_G7C (G7C) phage for antibacterial activity. Thirteen short (<1000 bp) ORFs without known homologs were cloned into an inducible system and tested in E. coli and P. aeruginosa. Four proteins—strGp16.1, strGp17.1, strGp17.2, and strGp17.3—significantly inhibited bacterial growth, and strGp16.1 completely suppressed P. aeruginosa under experimental conditions. These findings indicate that early phage proteins can influence bacterial physiology and may provide a basis for novel antibacterial strategies.