Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition

NS1 of influenza A virus inhibits TRIM25 activity, which is an E3 ligase important for induction of the interferon response. Here, Koliopoulos et al. present structures of TRIM25 and NS1 and show how NS1 binding interferes with substrate recognition of TRIM25.

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Autores principales:	Marios G. Koliopoulos, Mathilde Lethier, Annemarthe G. van der Veen, Kevin Haubrich, Janosch Hennig, Eva Kowalinski, Rebecca V. Stevens, Stephen R. Martin, Caetano Reis e Sousa, Stephen Cusack, Katrin Rittinger
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/37466ebb4272497c9f39f54fcc779957
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spelling	oai:doaj.org-article:37466ebb4272497c9f39f54fcc7799572021-12-02T16:50:11ZMolecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition10.1038/s41467-018-04214-82041-1723https://doaj.org/article/37466ebb4272497c9f39f54fcc7799572018-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-04214-8https://doaj.org/toc/2041-1723NS1 of influenza A virus inhibits TRIM25 activity, which is an E3 ligase important for induction of the interferon response. Here, Koliopoulos et al. present structures of TRIM25 and NS1 and show how NS1 binding interferes with substrate recognition of TRIM25.Marios G. KoliopoulosMathilde LethierAnnemarthe G. van der VeenKevin HaubrichJanosch HennigEva KowalinskiRebecca V. StevensStephen R. MartinCaetano Reis e SousaStephen CusackKatrin RittingerNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Marios G. Koliopoulos Mathilde Lethier Annemarthe G. van der Veen Kevin Haubrich Janosch Hennig Eva Kowalinski Rebecca V. Stevens Stephen R. Martin Caetano Reis e Sousa Stephen Cusack Katrin Rittinger Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
description	NS1 of influenza A virus inhibits TRIM25 activity, which is an E3 ligase important for induction of the interferon response. Here, Koliopoulos et al. present structures of TRIM25 and NS1 and show how NS1 binding interferes with substrate recognition of TRIM25.
format	article
author	Marios G. Koliopoulos Mathilde Lethier Annemarthe G. van der Veen Kevin Haubrich Janosch Hennig Eva Kowalinski Rebecca V. Stevens Stephen R. Martin Caetano Reis e Sousa Stephen Cusack Katrin Rittinger
author_facet	Marios G. Koliopoulos Mathilde Lethier Annemarthe G. van der Veen Kevin Haubrich Janosch Hennig Eva Kowalinski Rebecca V. Stevens Stephen R. Martin Caetano Reis e Sousa Stephen Cusack Katrin Rittinger
author_sort	Marios G. Koliopoulos
title	Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
title_short	Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
title_full	Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
title_fullStr	Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
title_full_unstemmed	Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition
title_sort	molecular mechanism of influenza a ns1-mediated trim25 recognition and inhibition
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/37466ebb4272497c9f39f54fcc779957
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Molecular mechanism of influenza A NS1-mediated TRIM25 recognition and inhibition

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