{
  "abstract": "Ribosome hibernation is a conserved bacterial stress-response mechanism that promotes translational shutdown and enhances survival under adverse conditions, contributing to persistence and tolerance to ribosome-targeting antibiotics. Here, we report high-resolution cryo-electron microscopy (cryo-EM) structures (2.5–2.8 Å) of hibernating 70S ribosomes from four clinically important ESKAPE pathogens: Pseudomonas aeruginosa , Enterobacter hormaechei , Klebsiella quasipneumoniae , and Acinetobacter baumannii . Structural analyses identified the bound hibernation factors as HPF in P. aeruginosa and E. hormaechei , and YfiA in K. quasipneumoniae and A. baumannii . Despite sequence divergence, HPF and YfiA adopt a conserved fold and occupy the same ribosomal binding site, interacting primarily with 16S rRNA and ribosomal proteins uS7 and uS9 and occupying the A- and P-sites while extending toward the E-site. Comparative analyses revealed a conserved core interaction network, including contacts with functionally important modified 16S rRNA nucleotides, alongside species-specific adaptations that preserve overall ribosome-binding architecture. Analysis of hibernating ribosome populations uncovered substantial heterogeneity in E-site tRNA occupancy, bS21 association, and mRNA binding among species, suggesting that these features are species-dependent rather than determined solely by the identity of the hibernation factor. Together, these structures provide a comprehensive comparative view of HPF- and YfiA-mediated ribosome hibernation across major Gram-negative pathogens, revealing conserved molecular principles and species-specific adaptations that expand our understanding of bacterial translational dormancy and establish a structural framework for future antibacterial strategies targeting ribosome hibernation.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 8,
  "authors": [
    {
      "name": "Vasanthakrishnan Radhakrishnan Balasubramaniam"
    },
    {
      "name": "Olivier Delalande"
    },
    {
      "name": "Yann Lefrançois Copy"
    },
    {
      "name": "Sophie Chat"
    },
    {
      "name": "Sylvie Georgeault-Daguenet"
    },
    {
      "name": "Mohamed Sassi"
    },
    {
      "name": "Emmanuel Giudice"
    },
    {
      "name": "Reynald Gillet"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/3z77arwnp7b03.bib",
  "cited_by": 0,
  "doi": "10.1038/s42003-026-11002-4",
  "fulltext_url": null,
  "id": "3z77arwnp7b03",
  "issns": [
    "2399-3642"
  ],
  "landing_url": "https://hal.science/hal-05778509v1",
  "language": "en",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "journal",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1312|RNA and protein synthesis mechanisms"
    ]
  ],
  "openalex": "W7214231086",
  "pdf_url": "https://www.nature.com/articles/s42003-026-11002-4_reference.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-10-05",
  "publisher": "Nature Publishing Group",
  "ris": "https://research.draconitic.com/paper/3z77arwnp7b03.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:47Z",
      "native_id": "hal-05778509",
      "source": "hal",
      "url": "https://hal.science/hal-05778509v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|RNA and protein synthesis mechanisms",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Structural characterization of hibernating ribosomes in four Gram-negative pathogenic bacteria",
  "title_text": "Structural characterization of hibernating ribosomes in four Gram-negative pathogenic bacteria",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:47Z",
  "url": "https://research.draconitic.com/paper/3z77arwnp7b03",
  "venue": "Communications Biology",
  "versions": []
}