ArticleNucleic acids research2016
Structures of proline-rich peptides bound to the ribosome reveal a common mechanism of protein synthesis inhibition.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers.
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Who cites it
107 citing papers in PubMed, 178 citations in OpenAlex.
- A Small Molecule Substrate Mimic to Inhibit Bacterial Hsp70 Chaperone Function.Chembiochem : a European journal of chemical biology · 2026Article
- "Lariocidin and ribosome-targeting lasso peptides as emerging antimicrobial agents against multidrug-resistant bacteria".The Journal of antibiotics · 2026Review
- Multiscale Modeling of the Bacterial Ribosome to Identify Potential Peptide Modulators and Their Allosteric Effects.Biochemistry · 2026Article
- Prolines in linkers of multi-domain proteins: Intrinsic regulators of misfolding and aggregation.PLoS computational biology · 2026Article
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- Characterization of Proline-Rich Antimicrobial Peptides with SbmA Transporter-Dependent and Independent Antimicrobial Activity towardACS infectious diseases · 2026Article
- Integrating Metal-Organic Frameworks with Antimicrobial Peptides: Advances and Challenges in Antibacterial Therapeutics.ACS omega · 2026Review
- Antimicrobial peptide resistance in Salmonella AMR: the role of surface binding and lipopolysaccharide remodelling: one health implications.World journal of microbiology & biotechnology · 2026Review
- Mechanistic Divergence and Differential Antibacterial Potency of the Proline-Rich Antimicrobial Peptide B7-005 Across ESKAPE + E Pathogens.Probiotics and antimicrobial proteins · 2026Article
- Truncated and Disubstituted (P4K and L7R) Oncocin Peptides Target the Ribosome with Improved Antibacterial Activity.ACS omega · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- Alloferon Mitigates LPS-Induced Endometritis by Attenuating the NLRP3/CASP1/IL-1β/IL-18 Signaling Cascade.Inflammation · 2025Article
- Review
- Testing antimicrobial peptides inhibiting protein synthesis in livingFrontiers in microbiology · 2025Article
- Comparative evaluation of antimicrobial peptides: effect on formation, metabolic activity and viability ofFrontiers in microbiology · 2025Article
- Amphibian-Derived Antimicrobial Peptides: Essential Components of Innate Immunity and Potential Leads for New Antibiotic Development.Protein and peptide letters · 2025Review
- Resilience Against Resistance: Exploring Cutting-edge Therapies for Methicillin-resistantCurrent medicinal chemistry · 2025Review
- The proline-rich antimicrobial peptide B7-005: low bacterial resistance, safe for human cells and effective in zebrafish embryo bacteraemia model.Open 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
47 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
With bacterial resistance becoming a serious threat to global public health, antimicrobial peptides (AMPs) have become a promising area of focus in antibiotic research. AMPs are derived from a diverse range of species, from prokaryotes to humans, with a mechanism of action that often involves disruption of the bacterial cell membrane. Proline-rich antimicrobial peptides (PrAMPs) are instead actively transported inside the bacterial cell where they bind and inactivate specific targets. Recently, it was reported that some PrAMPs, such as Bac71 -35, oncocins and apidaecins, bind and inactivate the bacterial ribosome. Here we report the crystal structures of Bac71 -35, Pyrrhocoricin, Metalnikowin and two oncocin derivatives, bound to the Thermus thermophilus 70S ribosome. Each of the PrAMPs blocks the peptide exit tunnel of the ribosome by simultaneously occupying three well characterized antibiotic-binding sites and interferes with the initiation step of translation, thereby revealing a common mechanism of action used by these PrAMPs to inactivate protein synthesis. Our study expands the repertoire of PrAMPs and provides a framework for designing new-generation therapeutics.
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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.