Plasmid-specified FemABX-like immunity factor in Staphylococcus sciuri DD 4747

Lucie S Heath1, Shaw R Gargis, S Rochelle Smithberg

  • 1Department of Biological Sciences, The University of Alabama, Tuscaloosa, AL 35487-0334, USA.

Insights

A novel Staphylococcus sciuri plasmid gene confers resistance to lysostaphin endopeptidase by altering cell wall peptidoglycan composition. This immunity gene is the first identified not linked to its corresponding bacteriolytic enzyme.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Bacterial Genetics

Background:

  • Plasmids in Staphylococcus species carry genes conferring various traits.
  • Lysostaphin endopeptidase is a key enzyme used against Staphylococcus aureus infections.
  • Understanding resistance mechanisms is crucial for developing effective antimicrobial strategies.

Purpose of the Study:

  • To characterize a novel gene from Staphylococcus sciuri DD 4747 with potential antimicrobial resistance functions.
  • To investigate the role of an epr-like gene in lysostaphin endopeptidase resistance in Staphylococcus aureus.

Main Methods:

  • Plasmid isolation and sequencing from Staphylococcus sciuri DD 4747.
  • Genetic manipulation of Staphylococcus aureus RN4220 by introducing the epr-like gene.
  • Assessment of lysostaphin endopeptidase resistance in recombinant strains.
  • Analysis of cell wall peptidoglycan composition using biochemical methods.

Main Results:

  • A plasmid from S. sciuri DD 4747 contained replication, amidase-like, and epr-like genes.
  • Introduction of the epr-like gene into S. aureus RN4220 increased resistance to lysostaphin endopeptidase.
  • Recombinant strains exhibited altered peptidoglycan composition with increased serine and decreased glycine content.
  • The epr-like gene was identified as a member of the femABX-like immunity gene family.

Conclusions:

  • The identified epr-like gene confers resistance to lysostaphin endopeptidase in Staphylococcus species.
  • This gene functions by modifying cell wall peptidoglycan structure.
  • This represents the first instance of a femABX-like immunity gene not physically linked to the gene for the bacteriolytic enzyme it protects against.

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