ArticleNature communications2024
Bactericidal effect of tetracycline in E. coli strain ED1a may be associated with ribosome dysfunction.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Cryo-EM reveals multiple mechanisms of ribosome inhibition by doxycycline.Nature communications · 2026Article
- Conformational analysis of different tautomers of some antibiotics.Journal of molecular modeling · 2026Article
- Capturing ribosomal structures in cellular extracts with cryoPRISM: A purification-free cryoEM approach reveals novel structural states.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- TANGO: Analysis and curation of particles in cryo-electron tomography.Nature communications · 2026Article
- Resolving structural heterogeneity in situ through cryogenic electron tomography.Current opinion in structural biology · 2026Review
- Sodium butyrate augments the antibacterial activity of tetracycline against clinical isolates of multidrug-resistant Vibrio cholerae.Gut pathogens · 2026Article
- Uncovering nitroxoline activity spectrum, mode of action and resistance across Gram-negative bacteria.Nature communications · 2025Article
- Rapid structural analysis of bacterial ribosomes in situ.Communications biology · 2025Article
- The evolution of heteroresistance via small colony variants in Escherichia coli following long term exposure to bacteriostatic antibiotics.Nature communications · 2024Article
- The Evolution of Heteroresistance via Small Colony Variants inbioRxiv : the preprint server for biology · 2024Article
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Authors and funding
9 authors.
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Abstract
Ribosomes translate the genetic code into proteins. Recent technical advances have facilitated in situ structural analyses of ribosome functional states inside eukaryotic cells and the minimal bacterium Mycoplasma. However, such analyses of Gram-negative bacteria are lacking, despite their ribosomes being major antimicrobial drug targets. Here we compare two E. coli strains, a lab E. coli K-12 and human gut isolate E. coli ED1a, for which tetracycline exhibits bacteriostatic and bactericidal action, respectively. Using our approach for close-to-native E. coli sample preparation, we assess the two strains by cryo-ET and visualize their ribosomes at high resolution in situ. Upon tetracycline treatment, these exhibit virtually identical drug binding sites, yet the conformation distribution of ribosomal complexes differs. While K-12 retains ribosomes in a translation-competent state, tRNAs are lost in the vast majority of ED1a ribosomes. These structural findings together with the proteome-wide abundance and thermal stability assessments indicate that antibiotic responses are complex in cells and can differ between different strains of a single species, thus arguing that all relevant bacterial strains should be analyzed in situ when addressing antibiotic mode of action.
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