{
  "abstract": "Host cells contest invasion by intracellular bacterial pathogens with multiple strategies that recognise and/or damage the bacterial surface. To identify host defence factors targeted to intracellular bacteria, we developed a proximity biotinylation approach coupled to quantitative mass spectrometry that maps the host-bacterial interface during infection. Using this method, we discovered that intracellular Shigella and Salmonella become targeted by UFM1-protein ligase 1 (UFL1), an E3 ligase that catalyses the covalent attachment of Ubiquitin-fold modifier 1 (UFM1) to target substrates in a process called UFMylation. Shigella antagonises UFMylation in a dual manner: first, using its lipopolysaccharide to shield from UFL1 recruitment; second, preventing UFM1 decoration by the bacterial effector IpaH9.8. Absence of UFMylation leads to an increase of bacterial burden in human cells and zebrafish larvae. Contrary to ubiquitylation, the protective role of UFMylation is independent of autophagy. Altogether, our proximity mapping of the host-bacterial interface identifies UFMylation as an ancient antibacterial pathway and holds great promise to reveal other cell-autonomous immunity mechanisms.",
  "abstract_shown": true,
  "affiliations": [
    "Department of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK. ana.lopez@unige.ch.",
    "Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland. ana.lopez@unige.ch.",
    "VIB-UGent Center for Medical Biotechnology, VIB, Ghent, Belgium.",
    "Department of Biomolecular Medicine, Ghent University, Ghent, Belgium.",
    "Department of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK.",
    "Department of Molecular Microbiology and Immunology, Oregon Health & Science University, Portland, Oregon, USA.",
    "Department of Microbiology and Immunology, Dalhousie University, Halifax, Nova Scotia, Canada.",
    "Department of Cell and Chemical Biology, Leiden University Medical Centre, Leiden, The Netherlands.",
    "Department of Microbiology and Molecular Medicine, University of Geneva, Geneva, Switzerland.",
    "Department of Infection Biology, London School of Hygiene and Tropical Medicine, London, UK. serge.mostowy@lshtm.ac.uk."
  ],
  "article_type": "research support, non u.s. gov't",
  "arxiv": null,
  "author_total": 17,
  "authors": [
    {
      "affs": [
        0,
        1
      ],
      "name": "Ana T López-Jiménez",
      "orcid": "0000-0002-0289-738X"
    },
    {
      "affs": [
        2,
        3
      ],
      "name": "Fabien Théry",
      "orcid": "0000-0001-5007-0371"
    },
    {
      "affs": [
        4
      ],
      "name": "Kathryn Wright",
      "orcid": "0000-0001-6508-3386"
    },
    {
      "affs": [
        4
      ],
      "name": "Hannah Painter"
    },
    {
      "affs": [
        5
      ],
      "name": "Shelby T Hoffmeister"
    },
    {
      "affs": [
        6
      ],
      "name": "Lucas Jarche"
    },
    {
      "affs": [
        6
      ],
      "name": "Jeremy Benjamin"
    },
    {
      "affs": [
        7
      ],
      "name": "Gerbrand J van der Heden van Noort",
      "orcid": "0000-0001-5955-6431"
    },
    {
      "affs": [
        4
      ],
      "name": "Dominik Brokatzky"
    },
    {
      "affs": [
        4
      ],
      "name": "Margarida C Gomes",
      "orcid": "0000-0001-9656-6145"
    },
    {
      "affs": [
        4
      ],
      "name": "Sydney L Miles"
    },
    {
      "affs": [
        4
      ],
      "name": "Damián Lobato-Márquez",
      "orcid": "0000-0002-0044-7588"
    },
    {
      "affs": [
        8
      ],
      "name": "Eva-Maria Frickel",
      "orcid": "0000-0002-9515-3442"
    },
    {
      "affs": [
        6
      ],
      "name": "John Rohde",
      "orcid": "0000-0002-8569-3760"
    },
    {
      "affs": [
        5
      ],
      "name": "Jonathan N Pruneda",
      "orcid": "0000-0002-0304-4418"
    },
    {
      "affs": [
        2,
        3
      ],
      "name": "Francis Impens",
      "orcid": "0000-0003-2886-9616"
    },
    {
      "affs": [
        9
      ],
      "name": "Serge Mostowy",
      "orcid": "0000-0002-7286-6503"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/9dmyjmq3yxqg0.bib",
  "cited_by": 1,
  "doi": "10.1038/s41467-026-77860-y",
  "fulltext_url": "https://europepmc.org/articles/PMC13680623",
  "id": "9dmyjmq3yxqg0",
  "issns": [
    "2041-1723"
  ],
  "landing_url": "https://europepmc.org/article/MED/42897205",
  "language": "eng",
  "licence": "CC-BY",
  "licence_label": "CC BY",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "openalex",
      "1312|Ubiquitin and proteasome pathways"
    ]
  ],
  "openalex": "W7213445003",
  "pdf_url": "https://europepmc.org/articles/PMC13680623?pdf=render",
  "pmcid": "PMC13680623",
  "pmid": "42897205",
  "published": "2026-09-17",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/9dmyjmq3yxqg0.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:19:41Z",
      "native_id": "MED:42897205",
      "source": "europepmc",
      "url": "https://europepmc.org/article/MED/42897205"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Ubiquitin and proteasome pathways",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Proximity biotinylation at the host-Shigella interface reveals UFMylation as an antibacterial pathway.",
  "title_text": "Proximity biotinylation at the host-Shigella interface reveals UFMylation as an antibacterial pathway.",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:19:41Z",
  "url": "https://research.draconitic.com/paper/9dmyjmq3yxqg0",
  "venue": "Nature communications",
  "versions": []
}