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Isolation of Translating Ribosomes Containing Peptidyl-tRNAs for Functional and Structural Analyses
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Macrolide resistance from the ribosome perspective

F Franceschi1, Z Kanyo, E C Sherer

  • 1Rib-X Pharmaceuticals, Inc., 300 George Street, Suite 301, New Haven, CT 06511, USA.

Current Drug Targets. Infectious Disorders
|September 24, 2004
PubMed

Insights

Macrolide antibiotics fight respiratory infections. Recent structural studies reveal how these drugs bind to bacterial ribosomes and how resistance develops at the molecular level.

Area of Science:

  • Molecular Biology
  • Microbiology
  • Pharmacology

Background:

  • Macrolides are crucial antibiotics for treating human respiratory tract infections.
  • Understanding their mechanism of action and resistance is vital, despite decades of use.

Purpose of the Study:

  • To compare the binding modes of various macrolides and ketolides to ribosomal subunits.
  • To elucidate the atomic-level details of antibiotic-ribosome interactions and resistance mechanisms.

Main Methods:

  • Structural resolution of macrolide and ketolide complexes with ribosomal 50S subunits from Haloarcula marismortui and Deinococcus radiodurans.
  • Comparative analysis of binding features at the atomic level.

Main Results:

  • Detailed comparison of binding characteristics for 14-, 15-, and 16-membered macrolides versus ketolides (telithromycin, ABT-773).
  • Insights into how modifications in 23S rRNA and ribosomal proteins L4/L22 confer resistance.

Conclusions:

  • Structural biology provides a detailed understanding of macrolide-ribosome interactions.
  • This knowledge is key to comprehending and potentially overcoming antibiotic resistance in key pathogens.

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