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Related Experiment Videos

Intrinsic penicillin resistance in enterococci

R Fontana1, M Ligozzi, F Pittaluga

  • 1Istituto di Microbiologia, Università di Verona, Italy.

Microbial Drug Resistance (Larchmont, N.Y.)
|July 1, 1996
PubMed
Summary

Penicillin resistance in enterococci stems from overproducing a low-affinity penicillin-binding protein (PBP5). Genetic changes affecting PBP5 synthesis or its structure drive resistance and hypersusceptibility, impacting penicillin-binding capabilities.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Biochemistry

Background:

  • Enterococci exhibit penicillin resistance linked to penicillin-binding protein (PBP) alterations.
  • Penicillin-binding protein 5 (PBP5) is a key factor in enterococcal resistance.
  • Understanding PBP5's role is crucial for combating antibiotic resistance.

Purpose of the Study:

  • Investigate the genetic and structural basis of penicillin resistance in enterococci.
  • Elucidate the mechanisms of PBP5 overproduction and modification.
  • Explore the impact of these changes on penicillin-binding affinity.

Main Methods:

  • Genetic analysis of resistant enterococcal mutants (Enterococcus hirae ATCC 9790).
  • Identification of genetic elements controlling PBP5 synthesis.

Related Experiment Videos

  • Amino acid substitution analysis in PBP5 from resistant strains (Enterococcus faecium).
  • Antibody cross-reactivity studies to assess structural homology.

    • Main Results:

    • A deletion upstream of the pbp5 gene correlated with PBP5 overproduction and resistance in E. hirae.
    • A point mutation in pbp5 caused hypersusceptibility via premature translation termination.
    • High-level ampicillin resistance in E. faecium linked to PBP5 overproduction and modified penicillin-binding capability.
    • Amino acid substitutions, particularly polar to nonpolar changes (T to A or I) near SDN and KTG motifs, altered PBP5's penicillin-binding domain and reduced penicillin affinity.

    Conclusions:

    • Genetic alterations and structural modifications of PBP5 are central to penicillin resistance and hypersusceptibility in enterococci.
    • PBP5 overproduction and functional changes are key drivers of ampicillin resistance.
    • Specific amino acid substitutions in PBP5 significantly impact its penicillin-binding affinity, offering targets for future research.