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Updated: Jun 14, 2025
08:03
A Tandem Liquid Chromatography–Mass Spectrometry-based Approach for Metabolite Analysis of Staphylococcus aureus
Published on: March 28, 2017
10.1K
Structural studies on ribosomes of differentially macrolide-resistant Staphylococcus aureus strains
André Rivalta1, Aliza Fedorenko1, Alexandre Le Scornet2
1Department of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Life Science Alliance
|June 9, 2025
Summary
Antimicrobial resistance in Staphylococcus aureus is a growing threat. This study reveals how solithromycin binds to resistant bacterial ribosomes, offering insights for developing new antibiotics against drug-resistant infections.
Area of Science:
- Microbiology
- Structural Biology
- Drug Discovery
Background:
- Antimicrobial resistance (AMR) is a significant global health concern.
- Macrolide antibiotics are losing efficacy against pathogens like Staphylococcus aureus.
- Erm-family methyltransferases cause macrolide resistance by modifying 23S ribosomal RNA.
Purpose of the Study:
- To investigate the structural basis of macrolide-ribosome interactions in Staphylococcus aureus.
- To understand how ErmB-mediated methylation affects drug binding.
- To explore strategies for overcoming macrolide resistance in S. aureus.
Main Methods:
- Cryo-electron microscopy (cryo-EM) to determine high-resolution ribosome structures.
- Analysis of S. aureus strains with varying ermB expression.
- Microbiological and biochemical assays to validate drug binding and resistance.
Main Results:
- High-resolution structures of solithromycin-bound ribosomes, including those with A2058 dimethylation, were determined.
- Specific interactions enabling solithromycin binding despite resistance mechanisms were identified.
- Structural findings were corroborated by microbiological and biochemical data.
Conclusions:
- Solithromycin can bind to resistant S. aureus ribosomes, even with A2058 dimethylation.
- Understanding these interactions can guide the development of novel ketolides.
- Further optimization of ketolide-ribosome interactions may enhance efficacy against resistant S. aureus.
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