ArticleNature chemical biology2023
Structural basis for translation inhibition by the glycosylated drosocin peptide.
Article in Nature chemical biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 29 citations in OpenAlex.
- Structural basis of nucleotide-dependent conformational switching of a CBS-family protein on the archaeal 50S ribosome.Science China. Life sciences · 2026Article
- Molecular and Functional Characterization of Black Soldier Fly Derived Peptide Against Food-Relevant Bacteria.Foods (Basel, Switzerland) · 2026Article
- Enhancement of Anti-Melanogenic Activity ofMarine drugs · 2026Article
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- The neuroimmune system and cognition.Nature immunology · 2026Review
- Antimicrobial Peptides and ESKAPEE Pathogens: A New Frontier in the Fight Against Antimicrobial Resistance.Probiotics and antimicrobial proteins · 2026Review
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- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- Mechanistic Divergence and Differential Antibacterial Potency of the Proline-Rich Antimicrobial Peptide B7-005 Across ESKAPE + E Pathogens.Probiotics and antimicrobial proteins · 2026Article
- Saskemycin, a potent and selective antimycobacterial agent targeting a unique site on the ribosome.Research square · 2025Article
- N-acetyl-glucosamine primes Pseudomonas aeruginosa for virulence through a type IV pili/cAMP-mediated morphology transition.Nature communications · 2025Article
- Truncated and Disubstituted (P4K and L7R) Oncocin Peptides Target the Ribosome with Improved Antibacterial Activity.ACS omega · 2025Article
- Review
- A large-scale curated and filterable dataset for cryo-EM foundation model pre-training.Scientific data · 2025Article
- Designing New Chimeric Proline-Rich Antimicrobial Peptides to Enhance Efficacy Toward the ESKAPE+E: Beyond Sequence Extension.Biomolecules · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- The proline-rich antimicrobial peptide Api137 disrupts large ribosomal subunit assembly and induces misfolding.Nature communications · 2025Article
- Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024Review
- Paenilamicins are context-specific translocation inhibitors of protein synthesis.Nature chemical biology · 2024Article
- Stereorandomized Oncocins with Preserved Ribosome Binding and Antibacterial Activity.Journal of medicinal chemistry · 2024Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The proline-rich antimicrobial peptide (PrAMP) drosocin is produced by Drosophila species to combat bacterial infection. Unlike many PrAMPs, drosocin is O-glycosylated at threonine 11, a post-translation modification that enhances its antimicrobial activity. Here we demonstrate that the O-glycosylation not only influences cellular uptake of the peptide but also interacts with its intracellular target, the ribosome. Cryogenic electron microscopy structures of glycosylated drosocin on the ribosome at 2.0-2.8-Å resolution reveal that the peptide interferes with translation termination by binding within the polypeptide exit tunnel and trapping RF1 on the ribosome, reminiscent of that reported for the PrAMP apidaecin. The glycosylation of drosocin enables multiple interactions with U2609 of the 23S rRNA, leading to conformational changes that break the canonical base pair with A752. Collectively, our study reveals novel molecular insights into the interaction of O-glycosylated drosocin with the ribosome, which provide a structural basis for future development of this class of antimicrobials.
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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.