Reverse engineering synthetic antiviral amyloids

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.

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Autores principales:	Emiel Michiels, 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 Itatí Ibañez, Anouk Smet, Pieter Baatsen, Shu Liu, Ina Vorberg, Guy Bormans, Johan Neyts, Xavier Saelens, Frederic Rousseau, Joost Schymkowitz
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2020
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ffcec336575043bba6212cbf4b6b3b72
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

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spelling	oai:doaj.org-article:ffcec336575043bba6212cbf4b6b3b722021-12-02T15:56:54ZReverse engineering synthetic antiviral amyloids10.1038/s41467-020-16721-82041-1723https://doaj.org/article/ffcec336575043bba6212cbf4b6b3b722020-06-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-16721-8https://doaj.org/toc/2041-1723Some 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.Emiel MichielsKenny RooseRodrigo GallardoLadan KhodaparastLaleh KhodaparastRob van der KantMaxime SiemonsBert HoubenMeine RamakersHannah WilkinsonPatricia GuerreiroNikolaos LourosSuzanne J. F. KapteinLorena Itatí IbañezAnouk SmetPieter BaatsenShu LiuIna VorbergGuy BormansJohan NeytsXavier SaelensFrederic RousseauJoost SchymkowitzNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Emiel Michiels 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 Itatí Ibañez Anouk Smet Pieter Baatsen Shu Liu Ina Vorberg Guy Bormans Johan Neyts Xavier Saelens Frederic Rousseau Joost Schymkowitz Reverse engineering synthetic antiviral amyloids
description	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.
format	article
author	Emiel Michiels 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 Itatí Ibañez Anouk Smet Pieter Baatsen Shu Liu Ina Vorberg Guy Bormans Johan Neyts Xavier Saelens Frederic Rousseau Joost Schymkowitz
author_facet	Emiel Michiels 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 Itatí Ibañez Anouk Smet Pieter Baatsen Shu Liu Ina Vorberg Guy Bormans Johan Neyts Xavier Saelens Frederic Rousseau Joost Schymkowitz
author_sort	Emiel Michiels
title	Reverse engineering synthetic antiviral amyloids
title_short	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_sort	reverse engineering synthetic antiviral amyloids
publisher	Nature Portfolio
publishDate	2020
url	https://doaj.org/article/ffcec336575043bba6212cbf4b6b3b72
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Reverse engineering synthetic antiviral amyloids

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