Service interruption on Monday 11 July from 12:30 to 13:00: all the sites of the CCSD (HAL, Epiciences, SciencesConf, AureHAL) will be inaccessible (network hardware connection).
Skip to Main content Skip to Navigation
Journal articles

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-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.
Document type :
Journal articles
Complete list of metadata

Cited literature [41 references]  Display  Hide  Download
Contributor : Florence LARROUS Connect in order to contact the contributor
Submitted on : Monday, June 15, 2020 - 4:23:00 PM
Last modification on : Thursday, April 7, 2022 - 1:58:17 PM


Distributed under a Creative Commons Attribution 4.0 International License




Florian Sonthonnax, Benoit Besson, Emilie Bonnaud, Grégory Jouvion, David Merino, et al.. Lyssavirus matrix protein cooperates with phosphoprotein to modulate the Jak-Stat pathway. Scientific Reports, Nature Publishing Group, 2019, 9 (1), pp.12171. ⟨10.1038/s41598-019-48507-4⟩. ⟨pasteur-02868844⟩



Record views


Files downloads