Extensive natural variation in bacterial ribosomal drug-binding sites

Ribosomes from certain bacteria possess divergent drug-binding sites compared to those of Escherichia coli, leading to natural evasion or hypersensitivity to antibiotics. However, in the absence of systematic studies, it is unknown whether this divergence is rare or common among bacterial species. Here, we address this by reconstructing the evolutionary history of drug-binding residues in bacterial ribosomes. We find that many rRNA residues that are currently viewed as bacterial-specific features of ribosomal drug-binding sites are in fact conserved only in a subset of bacteria. Conversely, species with divergent drug-binding sites are widespread in nature, arising from ancient rRNA polymorphisms at the direct ribosome-drug interface. Using a few bacterial species harboring divergent drug-binding sites, we identify their intrinsic resistance to corresponding ribosome-targeting antibiotics. Overall, we reveal the extensive lineage-specific diversity of ribosomal drug-binding sites, offering a resource for developing more targeted antibiotics and enabling personalized drug selection for specific pathogens.

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Publication Details

Journal
Cell Reports
Published
2025-06-17
DOI
https://doi.org/10.1016/j.celrep.2025.115878
Primary Topic
RNA and protein synthesis mechanisms
Type
article
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article

Extensive natural variation in bacterial ribosomal drug-binding sites

Sergey Melnikov, Karla Helena-Bueno, Chinenye L. Ekemezie, Charlotte R. Brown et al.
Cell Reports
RNA and protein synthesis mechanisms
article

Extensive natural variation in bacterial ribosomal drug-binding sites

Sergey Melnikov, Karla Helena-Bueno, Chinenye L. Ekemezie, Charlotte R. Brown, Tom A. Williams, Lewis I. Chan
article en

Abstract

Ribosomes from certain bacteria possess divergent drug-binding sites compared to those of Escherichia coli, leading to natural evasion or hypersensitivity to antibiotics. However, in the absence of systematic studies, it is unknown whether this divergence is rare or common among bacterial species. Here, we address this by reconstructing the evolutionary history of drug-binding residues in bacterial ribosomes. We find that many rRNA residues that are currently viewed as bacterial-specific features of ribosomal drug-binding sites are in fact conserved only in a subset of bacteria. Conversely, species with divergent drug-binding sites are widespread in nature, arising from ancient rRNA polymorphisms at the direct ribosome-drug interface. Using a few bacterial species harboring divergent drug-binding sites, we identify their intrinsic resistance to corresponding ribosome-targeting antibiotics. Overall, we reveal the extensive lineage-specific diversity of ribosomal drug-binding sites, offering a resource for developing more targeted antibiotics and enabling personalized drug selection for specific pathogens.

Cell ReportsVol. 44(7)
University of Bristol (GB), Newcastle University (GB)
Zero hunger
Openalex Percentile: Top 87%
RNA and protein synthesis mechanisms
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Extensive natural variation in bacterial ribosomal drug-binding sites — Sergey Melnikov, Karla Helena-Bueno, et al. · Cell Reports (2025) | TGRS Research Map | TGRS