ArticleAntimicrobial agents and chemotherapy2014
Synergy of streptogramin antibiotics occurs independently of their effects on translation.
Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 67 citations in OpenAlex.
- Structure-based design and synthesis of group A streptogramins that bind to the nascent peptide exit tunnel of the ribosome.European journal of medicinal chemistry · 2026Article
- The post antibiotic effect of streptogramins on gram-positive bacteria primarily arises from the type a component.Microbial pathogenesis · 2026Article
- Multiscale Modeling of the Bacterial Ribosome to Identify Potential Peptide Modulators and Their Allosteric Effects.Biochemistry · 2026Article
- Transcription co-inhibition alters drug resistance evolution and enhances Mycobacterium tuberculosis clearance from granulomas.Nature microbiology · 2026Article
- Initial leads to combat streptogramin resistance generated from X-ray fragment screening against VatD.Structure (London, England : 1993) · 2025Article
- Analysis of Co-localized Biosynthetic Gene Clusters Identifies a Membrane-Permeabilizing Natural Product.Journal of natural products · 2024Article
- Navigating Antibacterial Frontiers: A Panoramic Exploration of Antibacterial Landscapes, Resistance Mechanisms, and Emerging Therapeutic Strategies.ACS infectious diseases · 2024Review
- The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.Structure (London, England : 1993) · 2024Article
- Hibernating ribosomes as drug targets?Frontiers in microbiology · 2024Review
- Treatment of MRSA Infection: Where are We?Current medicinal chemistry · 2024Review
- Biotransformation-coupled mutasynthesis for the generation of novel pristinamycin derivatives by engineering the phenylglycine residue.RSC chemical biology · 2023Article
- Structural insights into the mechanism of overcoming Erm-mediated resistance by macrolides acting together with hygromycin-A.Nature communications · 2023Article
- The Myxobacterial Antibiotic Myxovalargin: Biosynthesis, Structural Revision, Total Synthesis, and Molecular Characterization of Ribosomal Inhibition.Journal of the American Chemical Society · 2023Article
- Sample-efficient identification of high-dimensional antibiotic synergy with a normalized diagonal sampling design.PLoS computational biology · 2022Article
- Three critical regions of the erythromycin resistance methyltransferase, ErmE, are required for function supporting a model for the interaction of Erm family enzymes with substrate rRNA.RNA (New York, N.Y.) · 2022Article
- RNA-Binding Macrocyclic Peptides.Frontiers in molecular biosciences · 2022Review
- Structural basis of ABCF-mediated resistance to pleuromutilin, lincosamide, and streptogramin A antibiotics in Gram-positive pathogens.Nature communications · 2021Article
- Inhibition of mitochondrial translation suppresses glioblastoma stem cell growth.Cell reports · 2021Article
- Binding and Action of Triphenylphosphonium Analog of Chloramphenicol upon the Bacterial Ribosome.Antibiotics (Basel, Switzerland) · 2021Article
- Structure of Erm-modified 70S ribosome reveals the mechanism of macrolide resistance.Nature chemical biology · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Streptogramin antibiotics are divided into types A and B, which in combination can act synergistically. We compared the molecular interactions of the streptogramin combinations Synercid (type A, dalfopristin; type B, quinupristin) and NXL 103 (type A, flopristin; type B, linopristin) with the Escherichia coli 70S ribosome by X-ray crystallography. We further analyzed the activity of the streptogramin components individually and in combination. The streptogramin A and B components in Synercid and NXL 103 exhibit synergistic antimicrobial activity against certain pathogenic bacteria. However, in transcription-coupled translation assays, only combinations that include dalfopristin, the streptogramin A component of Synercid, show synergy. Notably, the diethylaminoethylsulfonyl group in dalfopristin reduces its activity but is the basis for synergy in transcription-coupled translation assays before its rapid hydrolysis from the depsipeptide core. Replacement of the diethylaminoethylsulfonyl group in dalfopristin by a nonhydrolyzable group may therefore be beneficial for synergy. The absence of general streptogramin synergy in transcription-coupled translation assays suggests that the synergistic antimicrobial activity of streptogramins can occur independently of the effects of streptogramin on translation.
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