ArticleMolecular cell2018
Odilorhabdins, Antibacterial Agents that Cause Miscoding by Binding at a New Ribosomal Site.
Article in Molecular cell, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers, 1 of them a synthesis that pooled it.
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Who cites it
81 citing papers in PubMed, 1 synthesis or guideline pooled it, 136 citations in OpenAlex.
- Bactericidal activity of silver nanoparticles in drug-resistant bacteria.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023Pooled it
- N-terminal lysine as a critical determinant of odilorhabdin susceptibility to inactivation by the self-resistance acetyltransferase OatA.Antimicrobial agents and chemotherapy · 2026Article
- Total Synthesis and Structural Revision of Rhabdobranin Reveals a Cryptic Gram-Negative Antibiotic.Journal of the American Chemical Society · 2026Article
- Epidemiology of Infections Caused by Gram-Positive Cocci-Microorganisms · 2026Review
- "Lariocidin and ribosome-targeting lasso peptides as emerging antimicrobial agents against multidrug-resistant bacteria".The Journal of antibiotics · 2026Review
- MexXY-OprM efflux pump mediates resistance to odilorhabdins inMicrobiology spectrum · 2026Article
- The magnitude of the pharmacodynamic index for NOSO-502: pathogen clearance, emergence of resistance and human dose predictions.The Journal of antimicrobial chemotherapy · 2026Article
- CpxR and LrhA coordinate the regulation of Xenocoumacin 1 biosynthesis, flagellar assembly, and chemotaxis inFrontiers in microbiology · 2026Article
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- Saskemycin, a potent and selective antimycobacterial agent targeting a unique site on the ribosome.Research square · 2025Article
- Pleiotropic role of PAX cyclolipopeptides in theApplied and environmental microbiology · 2025Article
- Whole-Genome Sequencing and Biosynthetic Gene Cluster Analysis of Novel Entomopathogenic BacteriaBiology · 2025Article
- OmpR Indirectly Regulates Biosynthesis of Xenocoumacin 1 inMicroorganisms · 2025Article
- Current Approaches and Implications in Discovery of Novel Bioactive Products from Microbial Sources.Current microbiology · 2025Review
- Identification of Two Distinct Stereoselective Lysine 5-Hydroxylases by Genome Mining Based on Alazopeptin Biosynthetic Enzymes.Chemistry (Weinheim an der Bergstrasse, Germany) · 2025Article
- Article
- Fighting Antimicrobial Resistance: Innovative Drugs in Antibacterial Research.Angewandte Chemie (International ed. in English) · 2025Review
- Quorum sensing regulators and non-ribosomal peptide synthetases govern antibacterial secretions inFrontiers in microbiology · 2025Article
- Intracellularly driven chemical modifications of antimicrobial secondary metabolites: Potent mechanisms of self-resistance.Pharmaceutical science advances · 2024Review
- Harnessing Gram-negative bacteria for novel anti-Gram-negative antibiotics.Microbial biotechnology · 2024Review
21 more citing papers are in PubMed but not listed here.
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Authors and funding
24 authors at 10 institutions in 4 countries.
Funding
Abstract
Growing resistance of pathogenic bacteria and shortage of antibiotic discovery platforms challenge the use of antibiotics in the clinic. This threat calls for exploration of unconventional sources of antibiotics and identification of inhibitors able to eradicate resistant bacteria. Here we describe a different class of antibiotics, odilorhabdins (ODLs), produced by the enzymes of the non-ribosomal peptide synthetase gene cluster of the nematode-symbiotic bacterium Xenorhabdus nematophila. ODLs show activity against Gram-positive and Gram-negative pathogens, including carbapenem-resistant Enterobacteriaceae, and can eradicate infections in animal models. We demonstrate that the bactericidal ODLs interfere with protein synthesis. Genetic and structural analyses reveal that ODLs bind to the small ribosomal subunit at a site not exploited by current antibiotics. ODLs induce miscoding and promote hungry codon readthrough, amino acid misincorporation, and premature stop codon bypass. We propose that ODLs' miscoding activity reflects their ability to increase the affinity of non-cognate aminoacyl-tRNAs to the ribosome.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.