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Reverse engineering synthetic antiviral amyloids

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 f...

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Autores principales: Michiels, Emiel, Roose, Kenny, Gallardo, Rodrigo, Khodaparast, Ladan, Khodaparast, Laleh, van der Kant, Rob, Siemons, Maxime, Houben, Bert, Ramakers, Meine, Wilkinson, Hannah, Guerreiro, Patricia, Louros, Nikolaos, Kaptein, Suzanne J. F., Ibañez, Lorena Itatí, Smet, Anouk, Baatsen, Pieter, Liu, Shu, Vorberg, Ina, Bormans, Guy, Neyts, Johan, Saelens, Xavier, Rousseau, Frederic, Schymkowitz, Joost
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2020
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7275043/
https://www.ncbi.nlm.nih.gov/pubmed/32504029
http://dx.doi.org/10.1038/s41467-020-16721-8
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author Michiels, Emiel
Roose, Kenny
Gallardo, Rodrigo
Khodaparast, Ladan
Khodaparast, Laleh
van der Kant, Rob
Siemons, Maxime
Houben, Bert
Ramakers, Meine
Wilkinson, Hannah
Guerreiro, Patricia
Louros, Nikolaos
Kaptein, Suzanne J. F.
Ibañez, Lorena Itatí
Smet, Anouk
Baatsen, Pieter
Liu, Shu
Vorberg, Ina
Bormans, Guy
Neyts, Johan
Saelens, Xavier
Rousseau, Frederic
Schymkowitz, Joost
author_facet Michiels, Emiel
Roose, Kenny
Gallardo, Rodrigo
Khodaparast, Ladan
Khodaparast, Laleh
van der Kant, Rob
Siemons, Maxime
Houben, Bert
Ramakers, Meine
Wilkinson, Hannah
Guerreiro, Patricia
Louros, Nikolaos
Kaptein, Suzanne J. F.
Ibañez, Lorena Itatí
Smet, Anouk
Baatsen, Pieter
Liu, Shu
Vorberg, Ina
Bormans, Guy
Neyts, Johan
Saelens, Xavier
Rousseau, Frederic
Schymkowitz, Joost
author_sort Michiels, Emiel
collection PubMed
description 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.
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spelling pubmed-72750432020-06-16 Reverse engineering synthetic antiviral amyloids Michiels, Emiel Roose, Kenny Gallardo, Rodrigo Khodaparast, Ladan Khodaparast, Laleh van der Kant, Rob Siemons, Maxime Houben, Bert Ramakers, Meine Wilkinson, Hannah Guerreiro, Patricia Louros, Nikolaos Kaptein, Suzanne J. F. Ibañez, Lorena Itatí Smet, Anouk Baatsen, Pieter Liu, Shu Vorberg, Ina Bormans, Guy Neyts, Johan Saelens, Xavier Rousseau, Frederic Schymkowitz, Joost Nat Commun Article 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. Nature Publishing Group UK 2020-06-05 /pmc/articles/PMC7275043/ /pubmed/32504029 http://dx.doi.org/10.1038/s41467-020-16721-8 Text en © The Author(s) 2020, corrected publication 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Michiels, Emiel
Roose, Kenny
Gallardo, Rodrigo
Khodaparast, Ladan
Khodaparast, Laleh
van der Kant, Rob
Siemons, Maxime
Houben, Bert
Ramakers, Meine
Wilkinson, Hannah
Guerreiro, Patricia
Louros, Nikolaos
Kaptein, Suzanne J. F.
Ibañez, Lorena Itatí
Smet, Anouk
Baatsen, Pieter
Liu, Shu
Vorberg, Ina
Bormans, Guy
Neyts, Johan
Saelens, Xavier
Rousseau, Frederic
Schymkowitz, Joost
Reverse engineering synthetic antiviral amyloids
title Reverse engineering synthetic antiviral amyloids
title_full Reverse engineering synthetic antiviral amyloids
title_fullStr Reverse engineering synthetic antiviral amyloids
title_full_unstemmed Reverse engineering synthetic antiviral amyloids
title_short Reverse engineering synthetic antiviral amyloids
title_sort reverse engineering synthetic antiviral amyloids
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7275043/
https://www.ncbi.nlm.nih.gov/pubmed/32504029
http://dx.doi.org/10.1038/s41467-020-16721-8
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