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Reverse engineering synthetic antiviral amyloids

Emiel Michiels, Kenny Roose (UGent) , Rodrigo Gallardo, Ladan Khodaparast, Laleh Khodaparast, Rob van der Kant, Maxime Siemons, Bert Houben, Meine Ramakers, Hannah Wilkinson, et al.
(2020) NATURE COMMUNICATIONS. 11(1).
Author
Organization
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. Some human amyloid proteins have been shown to interact with viral proteins, suggesting that they may have potential as therapeutic agents. Here the authors design synthetic amyloids specific for influenza A and Zika virus proteins, respectively, and show that they can inhibit viral replication.
Keywords
CELL-CULTURE, PROTEIN, AGGREGATION, SPECIFICITY, BRAIN

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MLA
Michiels, Emiel, et al. “Reverse Engineering Synthetic Antiviral Amyloids.” NATURE COMMUNICATIONS, vol. 11, no. 1, 2020, doi:10.1038/s41467-020-16721-8.
APA
Michiels, E., Roose, K., Gallardo, R., Khodaparast, L., Khodaparast, L., van der Kant, R., … Schymkowitz, J. (2020). Reverse engineering synthetic antiviral amyloids. NATURE COMMUNICATIONS, 11(1). https://doi.org/10.1038/s41467-020-16721-8
Chicago author-date
Michiels, Emiel, Kenny Roose, Rodrigo Gallardo, Ladan Khodaparast, Laleh Khodaparast, Rob van der Kant, Maxime Siemons, et al. 2020. “Reverse Engineering Synthetic Antiviral Amyloids.” NATURE COMMUNICATIONS 11 (1). https://doi.org/10.1038/s41467-020-16721-8.
Chicago author-date (all authors)
Michiels, Emiel, Kenny Roose, Rodrigo Gallardo, Ladan Khodaparast, Laleh Khodaparast, Rob van der Kant, Maxime Siemons, Bert Houben, Meine Ramakers, Hannah Wilkinson, Patricia Guerreiro, Nikolaos Louros, Suzanne J. F. Kaptein, Lorena Ibanez, Anouk Smet, Pieter Baatsen, Shu Liu, Ina Vorberg, Guy Bormans, Johan Neyts, Xavier Saelens, Frederic Rousseau, and Joost Schymkowitz. 2020. “Reverse Engineering Synthetic Antiviral Amyloids.” NATURE COMMUNICATIONS 11 (1). doi:10.1038/s41467-020-16721-8.
Vancouver
1.
Michiels E, Roose K, Gallardo R, Khodaparast L, Khodaparast L, van der Kant R, et al. Reverse engineering synthetic antiviral amyloids. NATURE COMMUNICATIONS. 2020;11(1).
IEEE
[1]
E. Michiels et al., “Reverse engineering synthetic antiviral amyloids,” NATURE COMMUNICATIONS, vol. 11, no. 1, 2020.
@article{8669427,
  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. Some human amyloid proteins have been shown to interact with viral proteins, suggesting that they may have potential as therapeutic agents. Here the authors design synthetic amyloids specific for influenza A and Zika virus proteins, respectively, and show that they can inhibit viral replication.}},
  articleno    = {{2832}},
  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 Ibanez, Lorena 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}},
  issn         = {{2041-1723}},
  journal      = {{NATURE COMMUNICATIONS}},
  keywords     = {{CELL-CULTURE,PROTEIN,AGGREGATION,SPECIFICITY,BRAIN}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{13}},
  title        = {{Reverse engineering synthetic antiviral amyloids}},
  url          = {{http://doi.org/10.1038/s41467-020-16721-8}},
  volume       = {{11}},
  year         = {{2020}},
}
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