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@ARTICLE{Olari:276149,
      author       = {Olari, Lia-Raluca and Liu, Sichen and Arnold, Franziska and
                      Kühlwein, Julia and Gil Miró, Marta and Updahaya, Ajeet
                      Rijal and Stürzel, Christina and Thal, Dietmar Rudolf and
                      Walther, Paul and Sparrer, Konstantin and Danzer, Karin M
                      and Münch, Jan and Kirchhoff, Frank},
      title        = {α-{S}ynuclein fibrils enhance {HIV}-1 infection of human
                      {T} cells, macrophages and microglia.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DZNE-2025-00221},
      pages        = {813},
      year         = {2025},
      abstract     = {HIV-associated neurocognitive disorders (HAND) and viral
                      reservoirs in the brain remain a significant challenge.
                      Despite their importance, the mechanisms allowing HIV-1
                      entry and replication in the central nervous system (CNS)
                      are poorly understood. Here, we show that α-synuclein and
                      (to a lesser extent) Aβ fibrils associated with
                      neurological diseases enhance HIV-1 entry and replication in
                      human T cells, macrophages, and microglia. Additionally, an
                      HIV-1 Env-derived amyloidogenic peptide accelerated amyloid
                      formation by α-synuclein and Aβ peptides. Mechanistic
                      studies show that α-synuclein and Aβ fibrils interact with
                      HIV-1 particles and promote virion attachment and fusion
                      with target cells. Despite an overall negative surface
                      charge, these fibrils facilitate interactions between viral
                      and cellular membranes. The enhancing effects of human brain
                      extracts on HIV-1 infection correlated with their binding to
                      Thioflavin T, a dye commonly used to stain amyloids. Our
                      results suggest a detrimental interplay between HIV-1 and
                      brain amyloids that may contribute to the development of
                      neurodegenerative diseases.},
      keywords     = {Humans / alpha-Synuclein: metabolism / Microglia:
                      metabolism / Microglia: virology / HIV-1: physiology /
                      HIV-1: metabolism / Macrophages: virology / Macrophages:
                      metabolism / T-Lymphocytes: metabolism / T-Lymphocytes:
                      virology / T-Lymphocytes: immunology / Amyloid: metabolism /
                      HIV Infections: virology / HIV Infections: metabolism / HIV
                      Infections: pathology / Brain: virology / Brain: metabolism
                      / Brain: pathology / Amyloid beta-Peptides: metabolism /
                      Virus Internalization / Virus Replication / Benzothiazoles /
                      alpha-Synuclein (NLM Chemicals) / Amyloid (NLM Chemicals) /
                      Amyloid beta-Peptides (NLM Chemicals) / thioflavin T (NLM
                      Chemicals) / Benzothiazoles (NLM Chemicals)},
      cin          = {AG Danzer / AG Sparrer},
      ddc          = {500},
      cid          = {I:(DE-2719)5000072 / I:(DE-2719)1910003},
      pnm          = {352 - Disease Mechanisms (POF4-352) / 351 - Brain Function
                      (POF4-351)},
      pid          = {G:(DE-HGF)POF4-352 / G:(DE-HGF)POF4-351},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC11742913},
      pubmed       = {pmid:39827271},
      doi          = {10.1038/s41467-025-56099-z},
      url          = {https://pub.dzne.de/record/276149},
}