{
  "id": 11486827,
  "title": "ALS/FTD-linked TDP-43 alterations prevent HSV-1 infection by disrupting cell-adhesion pathways",
  "url": "https://urgent.news/2026/10/02/als-ftd-linked-tdp-43-alterations-prevent-hsv-1-infection-by",
  "topic": "science",
  "section": "Science",
  "published": "2026-10-02T00:00:00.000Z",
  "source": {
    "name": "bioRxiv",
    "slug": "biorxiv",
    "url": "https://www.biorxiv.org/content/10.64898/2026.09.28.755069v1?rss=1"
  },
  "original_language": "en",
  "account": "The article discusses how alterations in TDP-43, a protein associated with neurodegenerative disorders such as ALS and FTD, can prevent herpes simplex virus type-1 (HSV-1) infection. TDP-43 alterations are a key feature of these conditions, and research has now linked them to viral infections as well. The study found that ALS/FTD-linked forms of human TDP-43 hinder HSV-1 infection, and this effect was consistent across different mutations, sporadic ALS, and C9ORF72-ALS. This protective mechanism was observed in both neural and non-neural cell types, using patient-derived cells and animal models.\n\nIn addition to hindering infection, TDP-43 mutations also prevented inflammatory and cell stress-related responses to HSV-1 exposure. The protective effect was attributed to a loss-of-function mechanism, as TDP-43 knockdown but not overexpression was sufficient to protect cells from HSV-1 infection. Moreover, neurons with TDP-43 mutation exhibited disruptions in adhesion-related pathways, leading to reduced early-stage viral binding and entry. These disruptions were linked to alternative RNA splicing and impairment of focal adhesion kinase (FAK/PTK2), a critical mediator of cell-adhesion pathways.\n\nInhibition of FAK was found to decrease HSV-1 infection, while genetic enhancement of functional FAK promoted infectivity in cells with TDP-43 mutation. In conclusion, this study highlights the role of TDP-43 in affecting virus-host interactions by influencing adhesion pathways required for viral infection.",
  "summary": "TAR DNA-binding protein-43 (TDP-43) alterations are a key hallmark of amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), and other neurodegenerative disorders. Increasing evidence links these conditions to viral infections, but it is not known if and how viral pathogens may be affected by disease-associated TDP-43. We found that ALS/FTD-linked forms of human TDP-43 prevent…",
  "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."
}