ArticleNature structural & molecular biology2015
The proline-rich antimicrobial peptide Onc112 inhibits translation by blocking and destabilizing the initiation complex.
Article in Nature structural & molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 103 papers.
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Who cites it
103 citing papers in PubMed, 186 citations in OpenAlex.
- Reframing Antimicrobial Peptides beyond Direct Antimicrobial Activity toward Host-Directed Functions and Disease-Specific Therapeutic Applications.Journal of microbiology and biotechnology · 2026Review
- Marine Antimicrobial Peptides: From Ocean Biodiversity to Genome Mining, Multi-Omics Discovery, and Biotechnological Innovation in the Battle Against Antimicrobial Resistance.Probiotics and antimicrobial proteins · 2026Review
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- Harnessing toxin-mediated ribosome stalling as a complementary tool to annotate bacterial ORFs.Nucleic acids research · 2026Article
- Phospholipid composition strongly affects the assembly of β barrel proteins into purified bacterial outer membranes.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
- Antimicrobial Peptides: Current Status, Mechanisms of Action, and Strategies to Overcome Therapeutic Limitations.Microorganisms · 2025Review
- Truncated and Disubstituted (P4K and L7R) Oncocin Peptides Target the Ribosome with Improved Antibacterial Activity.ACS omega · 2025Article
- An intracellular release peptide display technology unveils an antimicrobial peptide with low probability for resistance development.iScience · 2025Article
- Antimicrobial Peptide-Peptoid Macrocycles from the Polymyxin B2 Chemical Space.Angewandte Chemie (International ed. in English) · 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
- Comparative evaluation of antimicrobial peptides: effect on formation, metabolic activity and viability ofFrontiers in microbiology · 2025Article
- Antimicrobial Peptides: Mechanisms, Applications, and Therapeutic Potential.Infection and drug resistance · 2025Review
- Testing antimicrobial peptides inhibiting protein synthesis in livingFrontiers in microbiology · 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
- Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.EMBO reports · 2024Article
- Sequence diversity of apidaecin-like peptides arresting the terminating ribosome.Nucleic acids research · 2024Article
43 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The increasing prevalence of multidrug-resistant pathogenic bacteria is making current antibiotics obsolete. Proline-rich antimicrobial peptides (PrAMPs) display potent activity against Gram-negative bacteria and thus represent an avenue for antibiotic development. PrAMPs from the oncocin family interact with the ribosome to inhibit translation, but their mode of action has remained unclear. Here we have determined a structure of the Onc112 peptide in complex with the Thermus thermophilus 70S ribosome at a resolution of 3.1 Å by X-ray crystallography. The Onc112 peptide binds within the ribosomal exit tunnel and extends toward the peptidyl transferase center, where it overlaps with the binding site for an aminoacyl-tRNA. We show biochemically that the binding of Onc112 blocks and destabilizes the initiation complex, thus preventing entry into the elongation phase. Our findings provide a basis for the future development of this class of potent antimicrobial agents.
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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.