{
  "id": 163704,
  "title": "Real-time analysis of pore formation by bi-component staphylococcal leukotoxins using the two-electrode voltage-clamp technique",
  "url": "https://urgent.news/2026/08/04/real-time-analysis-of-pore-formation-by-bi-component-staphylococcal",
  "topic": "science",
  "section": "Science",
  "published": "2026-08-04T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.08.03.742423v1?rss=1"
  },
  "original_language": "en",
  "account": "Pore forming toxins, or PFTs, are cytotoxins produced by certain bacteria in a water-soluble form. These toxins can create pores in the membranes of host cells, causing cell death through lytic activity. Staphylococcus aureus is known to produce bi-component PFTs, specifically the leukocidins, which target and lyse specific types of leukocytes, erythrocytes, and endothelial cells by interacting with membrane receptors. Most of these receptors are G protein-coupled receptors (GPCRs), such as complement or chemokine receptors.\n\nGamma-hemolysins, also known as Hlgs, are the primary leukocidins secreted by S. aureus. These toxins form receptor-dependent hetero-octameric pores, though the exact mechanisms are not yet fully understood. Due to the necessity of specific receptors within a lipid bilayer environment, studying these molecular mechanisms is technically challenging. To address this issue, researchers developed a novel, sensitive method for cell surface expression of a wide variety of target receptors and real-time recording of currents generated by newly formed pores.\n\nThis method involves the heterologous expression of receptors in Xenopus oocytes, coupled with the two-electrode voltage-clamp technique and the use of electrophysiological robots. By employing this approach, researchers were able to characterize the concentration-dependent kinetics of pore formation, determine receptor density as a limiting factor, observe specific responses to non-cognate pairing of PFTs, and detect cell surface binding of F subunits preceding pore formation. Additionally, the team proposed a hybrid model of subunit oligomerization to explain these findings.\n\nThe newly developed method can easily be implemented for in vitro characterization of various PFTs on a wide range of membrane receptors. This technique can be used to decipher early mechanisms of pore formation and screen therapeutic agents capable of blocking the cytotoxicity of receptor-dependent PFTs.",
  "summary": "Pore forming toxins (PFTs) are cytotoxins secreted in water-soluble form by pathogenic bacteria. They have the ability to form pores in the membrane of host cells, ultimately leading to cell death by lytic activity. Staphylococcus aureus produces a variety of bi-component PFTs, the leukocidins, which target and lyse particular leukocytes, erythrocytes and endothelial cells through specific…",
  "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."
}