ArticleNucleic acids research2012
Investigating the entire course of telithromycin binding to Escherichia coli ribosomes.
Article in Nucleic acids research, 2012. 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, 19 citations in OpenAlex.
- Evaluation of the MYCOPLASMA IST3 urogenital mycoplasma assay in an international multicentre trial.The Journal of antimicrobial chemotherapy · 2021Article
- Correlating Drug-Target Residence Time and Post-antibiotic Effect: Insight into Target Vulnerability.ACS infectious diseases · 2020Article
- A long-distance rRNA base pair impacts the ability of macrolide antibiotics to kill bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Kinetics of drug-ribosome interactions defines the cidality of macrolide antibiotics.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Parametrization of macrolide antibiotics using the force field toolkit.Journal of computational chemistry · 2015Article
- Synthesis and evaluation of chloramphenicol homodimers: molecular target, antimicrobial activity, and toxicity against human cells.PloS one · 2015Article
- Conjugation with polyamines enhances the antibacterial and anticancer activity of chloramphenicol.Nucleic acids research · 2014Article
- In vitro activity of the new fluoroketolide solithromycin (CEM-101) against macrolide-resistant and -susceptible Mycoplasma genitalium strains.Antimicrobial agents and chemotherapy · 2014Article
- Insights into the mode of action of novel fluoroketolides, potent inhibitors of bacterial protein synthesis.Antimicrobial agents and chemotherapy · 2014Article
- Impact of ribosomal modification on the binding of the antibiotic telithromycin using a combined grand canonical monte carlo/molecular dynamics simulation approach.PLoS computational biology · 2013Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Applying kinetics and footprinting analysis, we show that telithromycin, a ketolide antibiotic, binds to Escherichia coli ribosomes in a two-step process. During the first, rapidly equilibrated step, telithromycin binds to a low-affinity site (K(T) = 500 nM), in which the lactone ring is positioned at the upper portion of the peptide exit tunnel, while the alkyl-aryl side chain of the drug inserts a groove formed by nucleotides A789 and U790 of 23S rRNA. During the second step, telithromycin shifts slowly to a high-affinity site (K(T)* = 8.33 nM), in which the lactone ring remains essentially at the same position, while the side chain interacts with the base pair U2609:A752 and the extended loop of protein L22. Consistently, mutations perturbing either the base pair U2609:A752 or the L22-loop hinder shifting of telithromycin to the final position, without affecting the initial step of binding. In contrast, mutation Lys63Glu in protein L4 placed on the opposite side of the tunnel, exerts only a minor effect on telithromycin binding. Polyamines disfavor both sequential steps of binding. Our data correlate well with recent crystallographic data and rationalize the changes in the accessibility of ribosomes to telithromycin in response to ribosomal mutations and ionic changes.
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