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@ARTICLE{Michiels:153313,
      author       = {Michiels, Emiel and Roose, Kenny and Gallardo, Rodrigo and
                      Khodaparast, Ladan and Khodaparast, Laleh and van der Kant,
                      Rob and Siemons, Maxime and Houben, Bert and Ramakers, Meine
                      and Wilkinson, Hannah and Guerreiro, Patricia and Louros,
                      Nikolaos and Kaptein, Suzanne J F and Ibañez, Lorena Itatí
                      and Smet, Anouk and Baatsen, Pieter and Liu, Shu and
                      Vorberg, Ina and Bormans, Guy and Neyts, Johan and Saelens,
                      Xavier and Rousseau, Frederic and Schymkowitz, Joost},
      title        = {{R}everse engineering synthetic antiviral amyloids.},
      journal      = {Nature Communications},
      volume       = {11},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2020-01310},
      pages        = {2832},
      year         = {2020},
      abstract     = {Human amyloids have been shown to interact with viruses and
                      interfere with viral replication. Based on this observation,
                      we employed a synthetic biology approach in which we
                      engineered virus-specific amyloids against influenza A and
                      Zika proteins. Each amyloid shares a homologous
                      aggregation-prone fragment with a specific viral target
                      protein. For influenza we demonstrate that a designer
                      amyloid against PB2 accumulates in influenza A-infected
                      tissue in vivo. Moreover, this amyloid acts specifically
                      against influenza A and its common PB2 polymorphisms, but
                      not influenza B, which lacks the homologous fragment. Our
                      model amyloid demonstrates that the sequence specificity of
                      amyloid interactions has the capacity to tune amyloid-virus
                      interactions while allowing for the flexibility to maintain
                      activity on evolutionary diverging variants.},
      keywords     = {Amyloid: genetics / Amyloid: pharmacology / Amyloid:
                      therapeutic use / Animals / Antiviral Agents: pharmacology /
                      Antiviral Agents: therapeutic use / Disease Models, Animal /
                      Dogs / Female / HEK293 Cells / Host-Pathogen Interactions:
                      drug effects / Humans / Influenza A virus: drug effects /
                      Influenza A virus: genetics / Influenza A virus:
                      pathogenicity / Influenza, Human: drug therapy / Influenza,
                      Human: virology / Madin Darby Canine Kidney Cells / Mice /
                      Polymorphism, Genetic / Recombinant Proteins: genetics /
                      Recombinant Proteins: pharmacology / Recombinant Proteins:
                      therapeutic use / Reverse Genetics: methods / Synthetic
                      Biology: methods / Viral Proteins: genetics / Viral
                      Proteins: metabolism / Virus Replication: drug effects /
                      Zika Virus: drug effects / Zika Virus: genetics / Zika
                      Virus: pathogenicity / Zika Virus Infection: drug therapy /
                      Zika Virus Infection: virology / Amyloid (NLM Chemicals) /
                      Antiviral Agents (NLM Chemicals) / Recombinant Proteins (NLM
                      Chemicals) / Viral Proteins (NLM Chemicals)},
      cin          = {AG Vorberg},
      ddc          = {500},
      cid          = {I:(DE-2719)1013004},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:32504029},
      pmc          = {pmc:PMC7275043},
      doi          = {10.1038/s41467-020-16721-8},
      url          = {https://pub.dzne.de/record/153313},
}