{
  "id": 6651592,
  "title": "Distinct atypical chemokine receptor 1 determinants underlie bacterial toxins recognition and pore formation",
  "url": "https://urgent.news/2026/09/10/distinct-atypical-chemokine-receptor-1-determinants-underlie",
  "topic": "science",
  "section": "Science",
  "published": "2026-09-10T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.07.749789v1?rss=1"
  },
  "original_language": "en",
  "account": "Distinct atypical chemokine receptor 1 (ACKR1) determinants underlie bacterial toxins recognition and pore formation. Atypical chemokine receptor 1 (ACKR1) is a promiscuous receptor that interacts with various chemokines through a flexible N-terminal tail. Pathogens such as Plasmodium vivax and Staphylococcus aureus (SA) exploit this interface using a sulfotyrosine code. Among SA's toxic proteins, HlgAB-mediated pore formation is only weakly competed by chemokines, the Duffy binding protein, or antibodies targeting ACKR1's N-terminus. Using structural biology and cell-based assays, researchers demonstrated that HlgA and HlgB bind to ACKR1's sulfated N-terminus with varying affinities and site hierarchies. HlgA has a single higher-affinity site for sulfated tyrosine 41, absent in HlgB. Surprisingly, this N-terminal engagement is not essential for pore formation; instead, productive lysis relies on an independent interaction between the toxins and ACKR1's extracellular vestibule. These findings reveal a two-step recognition mechanism, where the toxins first bind to the sulfotyrosine N-terminus and then are guided to the vestibule for pore formation, highlighting ACKR1's promiscuity from distributed, ligand-specific receptor surfaces.",
  "summary": "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…",
  "key_points": [],
  "editors_take": null,
  "illustration": null,
  "coverage": {
    "outlets": 1,
    "also_reported_by": []
  },
  "ai_generated": true,
  "disclaimer": "Summaries, key points and the editor’s take are written by software from other outlets’ reporting and may contain errors — always check the linked original."
}