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Related Experiment Videos

Labile 50S ribosome from partial macrolide-resistant Staphylococcus aureus

K Endou1, S Endoh, M Matsuoka

  • 1Division of Microbiology, Hokkaido Institute of Pharmaceutical Sciences, Japan.

Biological & Pharmaceutical Bulletin
|March 1, 1993
PubMed
Summary

Staphylococcus aureus exhibits macrolide-lincosamide-streptogramin B resistance due to a labile 50S ribosomal subunit. This subunit cleaves into smaller particles, preventing rokitamycin binding and conferring resistance.

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Area of Science:

  • Microbiology
  • Molecular Biology
  • Antibiotic Resistance

Background:

  • Staphylococcus aureus strains S704 and 8325MMT7 display inherent resistance to macrolide antibiotics.
  • This resistance, termed PM-resistance, extends to lincosamide and streptogramin B antibiotics but not all macrolides.

Purpose of the Study:

  • To investigate the ribosomal basis of PM-resistance in Staphylococcus aureus.
  • To determine the role of ribosomal subunits in antibiotic resistance.

Main Methods:

  • Dissociation of 70S ribosomes into 30S and 50S subunits using sucrose gradient centrifugation.
  • Analysis of subunit stability and antibiotic binding.
  • Identification of ribosomal protein components.

Main Results:

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  • The 50S ribosomal subunit from resistant strains was unstable and cleaved into smaller particles (approx. 40S).
  • Rokitamycin (RKM) failed to bind to these smaller particles.
  • A specific 33.0kDa protein component was absent in the cleaved 50S subunit particles.

Conclusions:

  • The lability and subsequent cleavage of the 50S ribosomal subunit is a key factor in Staphylococcus aureus's PM-resistance.
  • This structural alteration of the ribosome prevents effective antibiotic binding, leading to resistance.