ArticleEMBO reports2024
Activity, structure, and diversity of Type II proline-rich antimicrobial peptides from insects.
Article in EMBO reports, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed.
- Molecular and Functional Characterization of Black Soldier Fly Derived Peptide Against Food-Relevant Bacteria.Foods (Basel, Switzerland) · 2026Article
- Time-resolved phenotyping at subcellular resolution reveals shared principles and key trade-offs across antimicrobial peptide activities.bioRxiv : the preprint server for biology · 2026Article
- Flipping antimicrobial peptides in the exit tunnel of the bacterial ribosome.Nature communications · 2026Article
- Review
- Insect I-Type Lysozymes Function as Antiviral Proteases by Forming Biomolecular Condensates.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- Interactions ofInternational journal of molecular sciences · 2025Article
- Substitution of Proline Residues by 4-Fluoro-l-Proline Affects the Mechanism of the Proline-Rich Antimicrobial Peptide Api137.Antibiotics (Basel, Switzerland) · 2025Article
- The structure of the Vibrio natriegens 70S ribosome in complex with the proline-rich antimicrobial peptide Bac5(1-17).Nucleic acids research · 2025Article
- Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Apidaecin 1b (Api), the first characterized Type II Proline-rich antimicrobial peptide (PrAMP), is encoded in the honey bee genome. It inhibits bacterial growth by binding in the nascent peptide exit tunnel of the ribosome after the release of the completed protein and trapping the release factors. By genome mining, we have identified 71 PrAMPs encoded in insect genomes as pre-pro-polyproteins. Having chemically synthesized and tested the activity of 26 peptides, we demonstrate that despite significant sequence variation in the N-terminal sequence, the majority of the PrAMPs that retain the conserved C-terminal sequence of Api are able to trap the ribosome at the stop codons and induce stop codon readthrough-all hallmarks of Type II PrAMP mode of action. Some of the characterized PrAMPs exhibit superior antibacterial activity in comparison with Api. The newly solved crystallographic structures of the ribosome complexed with Api and with the more active peptide Fva1 from the stingless bee demonstrate the universal placement of the PrAMPs' C-terminal pharmacophore in the post-release ribosome despite variations in their N-terminal sequence.
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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.