{
  "abstract": "D-alanylation of teichoic acids is a conserved modification of Gram-positive bacterial cell envelopes that modulates resistance to environmental stresses and host interactions. While the cytosolic steps of this pathway are well characterized, the extracellular reactions responsible for transferring D-alanine onto teichoic acids remain poorly understood. Here we investigate the organization of the Dlt machinery in the symbiotic bacterium Lactiplantibacillus plantarum. We determined the 2.3 Å crystal structure of the extracellular catalytic domain of DltD, which adopts an SGNH-hydrolase fold with a conserved Ser-His-Asp catalytic triad. Docking analyses with lipoteichoic acids (LTA) fragments suggest that the glycerol-phosphate backbone of LTA is accommodated along a surface groove leading to the catalytic serine, with conserved residues contributing to substrate positioning. Biochemical measurements further reveal direct interactions between DltD, the acyl-carrier protein DltX, and the LTA esterase DltE. The conserved C-terminal motif of DltX binds DltD and is required for efficient D-alanylation and for L. plantarum-mediated promotion of Drosophila juvenile growth. Together, our findings support a revised model in which DltD, DltE, and DltX form a coordinated extracellular interaction network that dynamically regulates LTA D-alanylation. This work provides new mechanistic insights into the organization of the Dlt machinery and reveals how species-specific adaptations of this conserved pathway contribute to bacterial interactions with the host.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 11,
  "authors": [
    {
      "name": "Renata C Matos"
    },
    {
      "name": "Nikos Nikolopoulos"
    },
    {
      "name": "Quentin Perrier"
    },
    {
      "name": "Xavier Robert"
    },
    {
      "name": "Virginie Gueguen-Chaignon"
    },
    {
      "name": "Hiroto Hirayama"
    },
    {
      "name": "Jean-Pierre Simorre"
    },
    {
      "name": "François Leulier"
    },
    {
      "name": "Christophe Grangeasse"
    },
    {
      "name": "Yann Guerardel"
    },
    {
      "name": "Stéphanie Ravaud"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/197g9gz2r7eks.bib",
  "cited_by": 0,
  "doi": "10.1016/j.jbc.2026.113522",
  "fulltext_url": null,
  "id": "197g9gz2r7eks",
  "issns": [
    "0021-9258",
    "1083-351X"
  ],
  "landing_url": "https://hal.science/hal-05749201v1",
  "language": "en",
  "licence": "CC-BY-4.0",
  "licence_label": "CC BY 4.0",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
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      "0.sdv"
    ],
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      "hal",
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    [
      "openalex",
      "1311|Bacterial Genetics and Biotechnology"
    ]
  ],
  "openalex": "W7211958361",
  "pdf_url": "https://hal.science/hal-05749201/document",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-14",
  "publisher": "American Society for Biochemistry and Molecular Biology",
  "ris": "https://research.draconitic.com/paper/197g9gz2r7eks.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:34Z",
      "native_id": "hal-05749201",
      "source": "hal",
      "url": "https://hal.science/hal-05749201v1"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "hal:2.sdv.bbm.bs",
      "subfield": "structural-biology"
    },
    {
      "field": "biology",
      "origin": "hal:1.sdv.ee",
      "subfield": "ecology"
    },
    {
      "field": "biology",
      "origin": "hal:1.sdv.mp",
      "subfield": "microbiology"
    },
    {
      "field": "biology",
      "origin": "hal:1.sdv.ba",
      "subfield": "zoology-behaviour"
    }
  ],
  "title": "A DltE–DltD–DltX interaction network regulates lipoteichoic acid D-alanylation and Lactiplantibacillus plantarum-mediated growth promotion in Drosophila",
  "title_text": "A DltE–DltD–DltX interaction network regulates lipoteichoic acid D-alanylation and Lactiplantibacillus plantarum-mediated growth promotion in Drosophila",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:34Z",
  "url": "https://research.draconitic.com/paper/197g9gz2r7eks",
  "venue": "Journal of Biological Chemistry",
  "versions": []
}