Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway

Abstract Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-...

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Autores principales:	Florian Sonthonnax, Benoit Besson, Emilie Bonnaud, Grégory Jouvion, David Merino, Florence Larrous, Hervé Bourhy
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/f8f3f8130e7649328ef8b6b504e512a9
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spelling	oai:doaj.org-article:f8f3f8130e7649328ef8b6b504e512a92021-12-02T16:08:28ZLyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway10.1038/s41598-019-48507-42045-2322https://doaj.org/article/f8f3f8130e7649328ef8b6b504e512a92019-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-019-48507-4https://doaj.org/toc/2045-2322Abstract Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2-TPL2 complex, to efficiently inhibit the nuclear factor-κB (NF-κB) pathway. Using transfections, protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein in the control of Jak-Stat signaling pathway, in synergy with the P protein. In unstimulated cells, both M and P proteins were found to interact with JAK1. Upon type-I IFN stimulation, the M switches toward pSTAT1 interaction, which results in an enhanced capacity of P protein to interact with pSTAT1 and restrain it in the cytoplasm. Furthermore, the role for M-protein positions 77, 100, 104 and 110 was also demonstrated in interaction with both JAK1 and pY-STAT1, and confirmed in vivo. Together, these data indicate that M protein cooperates with P protein to restrain in parallel, and sequentially, NF-κB and Jak-Stat pathways.Florian SonthonnaxBenoit BessonEmilie BonnaudGrégory JouvionDavid MerinoFlorence LarrousHervé BourhyNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 9, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Florian Sonthonnax Benoit Besson Emilie Bonnaud Grégory Jouvion David Merino Florence Larrous Hervé Bourhy Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
description	Abstract Phosphoprotein (P) and matrix protein (M) cooperate to undermine the immune response to rabies virus (RABV) infections. While P is involved in the modulation of the Jak-Stat pathway through the cytoplasmic retention of interferon (IFN)-activated STAT1 (pSTAT1), M interacts with the RelAp43-p105-ABIN2-TPL2 complex, to efficiently inhibit the nuclear factor-κB (NF-κB) pathway. Using transfections, protein-complementation assays, reverse genetics and DNA ChIP, we identified a role of M protein in the control of Jak-Stat signaling pathway, in synergy with the P protein. In unstimulated cells, both M and P proteins were found to interact with JAK1. Upon type-I IFN stimulation, the M switches toward pSTAT1 interaction, which results in an enhanced capacity of P protein to interact with pSTAT1 and restrain it in the cytoplasm. Furthermore, the role for M-protein positions 77, 100, 104 and 110 was also demonstrated in interaction with both JAK1 and pY-STAT1, and confirmed in vivo. Together, these data indicate that M protein cooperates with P protein to restrain in parallel, and sequentially, NF-κB and Jak-Stat pathways.
format	article
author	Florian Sonthonnax Benoit Besson Emilie Bonnaud Grégory Jouvion David Merino Florence Larrous Hervé Bourhy
author_facet	Florian Sonthonnax Benoit Besson Emilie Bonnaud Grégory Jouvion David Merino Florence Larrous Hervé Bourhy
author_sort	Florian Sonthonnax
title	Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
title_short	Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
title_full	Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
title_fullStr	Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
title_full_unstemmed	Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway
title_sort	lyssavirus matrix protein cooperates with phosphoprotein to modulate the jak-stat pathway
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/f8f3f8130e7649328ef8b6b504e512a9
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Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway

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