{
  "abstract": "The adenylate cyclase toxin (CyaA) from Bordetella pertussis intoxicates host cells by directly translocating its N‐terminal catalytic domain across the plasma membrane; however, the forces driving this unique process remain poorly defined. Here, we dissect the membrane translocation mechanisms of two peptide segments derived from CyaA: P233 and P454 from the catalytic domain and the translocation region, respectively. Both P454 and P233 are calmodulin‐binding segments that are sequentially involved in the translocation and activation of the catalytic domain. Using a newly developed Droplet Interface Bilayer (DIB) approach, called DIB‐Pipette, which enables direct visualization of peptide transport under controlled membrane potentials, we show that P454 translocates across membranes independently of membrane potential, whereas P233 translocation requires a negative electric membrane potential. Strikingly, covalent coupling of P233 and P454 enables efficient translocation of the resulting peptide even in the absence of a membrane potential. Together, these results suggest that two distinct membrane‐active segments within CyaA act cooperatively to promote translocation at the peptide level, revealing an intrinsic mechanism that may contribute to membrane potential‐dependent translocation. These findings provide new mechanistic insights into the CyaA cell intoxication process and reveal a multifunctional strategy for protein delivery across membranes.",
  "abstract_shown": true,
  "affiliations": [],
  "article_type": null,
  "arxiv": null,
  "author_total": 10,
  "authors": [
    {
      "name": "Gaia Scilironi"
    },
    {
      "name": "Nicolas Carvalho"
    },
    {
      "name": "Jacinthe Frangieh"
    },
    {
      "name": "Corentin Léger"
    },
    {
      "name": "Dorothée Raoux-Barbot"
    },
    {
      "name": "J. Iñaki Guijarro"
    },
    {
      "name": "Daniel Ladant"
    },
    {
      "name": "Sophie Cribier"
    },
    {
      "name": "Nicolas Rodriguez"
    },
    {
      "name": "Alexandre Chenal"
    }
  ],
  "bibtex": "https://research.draconitic.com/paper/a6my6r27xb6s5.bib",
  "cited_by": 0,
  "doi": "10.1002/advs.77133",
  "fulltext_url": null,
  "id": "a6my6r27xb6s5",
  "issns": [
    "2198-3844"
  ],
  "landing_url": "https://hal.science/hal-05783983v2",
  "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": [
    [
      "hal",
      "0.sdv"
    ],
    [
      "openalex",
      "1312|Lipid Membrane Structure and Behavior"
    ]
  ],
  "openalex": "W7155515220",
  "pdf_url": "https://hal.science/hal-05783983/document",
  "pmcid": null,
  "pmid": "42627250",
  "published": "2026-08-21",
  "publisher": "Wiley Open Access",
  "ris": "https://research.draconitic.com/paper/a6my6r27xb6s5.ris",
  "sources": [
    {
      "first_seen": "2026-10-30T12:17:50Z",
      "native_id": "hal-05783983",
      "source": "hal",
      "url": "https://hal.science/hal-05783983v2"
    }
  ],
  "subjects": [
    {
      "field": "biochemistry",
      "origin": "openalex:1312|Lipid Membrane Structure and Behavior",
      "subfield": "molecular-biology"
    }
  ],
  "title": "Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation",
  "title_text": "Covalently Linked Peptides and Membrane Potential Enable CyaA Segment Translocation",
  "type": "peer-reviewed",
  "updated_at": "2026-10-30T12:17:50Z",
  "url": "https://research.draconitic.com/paper/a6my6r27xb6s5",
  "venue": "Advanced Science",
  "versions": []
}