{
  "abstract": "Atypical chemokine receptor 1 (ACKR1) is one of the most promiscuous receptors in the human chemokine system, engaging structurally diverse chemokines through a conformationally flexible N-terminal tail. This same interface is exploited by pathogens, including Plasmodium vivax and Staphylococcus aureus (SA), via a compact sulfotyrosine code. Among pathogenic proteins recognizing ACKR1, the SA leukocidin pair HlgAB is a notable exception. HlgAB-mediated pore formation is only weakly competed by chemokines, the Duffy binding protein, or antibodies targeting the receptor's N-terminus, leaving open how HlgAB engage ACKR1. Combining structural biology approaches with cell-based assays, we show that HlgA and HlgB engage ACKR1 sulfated N-terminus with distinct affinities and site hierarchies, with a single higher-affinity site for sulfated tyrosine 41 present in HlgA but absent in HlgB. Unexpectedly, this N-terminal engagement is dispensable for pore formation; productive lysis instead requires a separate interaction between the toxins and ACKR1 extracellular vestibule. These results define a two-step recognition mechanism, toxin capture by the sulfotyrosine N-terminus followed by vestibule-dependent pore formation, and extend the view that ACKR1 promiscuity arises from distributed, ligand-specific use of multiple receptor surfaces rather than a single adaptable interface.",
  "abstract_shown": true,
  "affiliations": [
    "IGF, Univ Montpellier, CNRS, INSERM, 141 rue de la Cardonille, Montpellier, 34094, France."
  ],
  "article_type": "New results",
  "arxiv": null,
  "author_total": 13,
  "authors": [
    {
      "name": "A. Fouillen"
    },
    {
      "name": "E. Logerot"
    },
    {
      "name": "Z. Ammar"
    },
    {
      "name": "T. Girbau"
    },
    {
      "name": "I. Brabet"
    },
    {
      "name": "O. Otun"
    },
    {
      "name": "R. Ben Boubaker"
    },
    {
      "name": "C. Le Drezen"
    },
    {
      "name": "M. Bacia-Verloop"
    },
    {
      "name": "A. Desfosses"
    },
    {
      "name": "C. Leyrat"
    },
    {
      "name": "S. Granier"
    },
    {
      "affs": [
        0
      ],
      "name": "C. Bechara"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/8j8n53a7e0hb9.bib",
  "cited_by": 0,
  "doi": "10.64898/2026.09.07.749789",
  "fulltext_url": "https://www.biorxiv.org/content/10.64898/2026.09.07.749789v1.full",
  "id": "8j8n53a7e0hb9",
  "issns": [],
  "landing_url": "https://www.biorxiv.org/content/10.64898/2026.09.07.749789v1",
  "language": null,
  "licence": "CC-BY-NC-ND",
  "licence_label": "CC BY-NC-ND",
  "licence_source": "article",
  "licence_url": "https://creativecommons.org/licenses/by-nc-nd/4.0/",
  "metadata_licence": null,
  "native_subjects": [
    [
      "biorxiv",
      "biochemistry"
    ],
    [
      "openalex",
      "2730|Chemokine receptors and signaling"
    ]
  ],
  "openalex": "W7212262405",
  "pdf_url": "https://www.biorxiv.org/content/10.64898/2026.09.07.749789v1.full.pdf",
  "pmcid": null,
  "pmid": null,
  "published": "2026-09-07",
  "publisher": null,
  "ris": "https://research.draconitic.com/paper/8j8n53a7e0hb9.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:21:09Z",
      "native_id": "10.64898/2026.09.07.749789",
      "source": "biorxiv",
      "url": "https://www.biorxiv.org/content/10.64898/2026.09.07.749789v1"
    }
  ],
  "subjects": [
    {
      "field": "medicine",
      "origin": "openalex:2730|Chemokine receptors and signaling",
      "subfield": "oncology"
    }
  ],
  "title": "Distinct atypical chemokine receptor 1 determinants underlie bacterial toxins recognition and pore formation",
  "title_text": "Distinct atypical chemokine receptor 1 determinants underlie bacterial toxins recognition and pore formation",
  "type": "preprint",
  "updated_at": "2026-10-30T12:21:09Z",
  "url": "https://research.draconitic.com/paper/8j8n53a7e0hb9",
  "venue": "bioRxiv",
  "versions": []
}