The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment - Archive ouverte HAL Access content directly
Journal Articles Virology Journal Year : 2009

The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment

Abstract

Background: The genome of measles virus consists of a non-segmented single-stranded RNA molecule of negative polarity, which is encapsidated by the viral nucleoprotein (N) within a helical nucleocapsid. The N protein possesses an intrinsically disordered C-terminal domain (aa 401-525, N TAIL) that is exposed at the surface of the viral nucleopcapsid. Thanks to its flexible nature, N TAIL interacts with several viral and cellular partners. Among these latter, the Interferon Regulator Factor 3 (IRF-3) has been reported to interact with N, with the interaction having been mapped to the regulatory domain of IRF-3 and to N TAIL. This interaction was described to lead to the phosphorylation-dependent activation of IRF-3, and to the ensuing activation of the pro-immune cytokine RANTES gene.
Fichier principal
Vignette du fichier
The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment.pdf (1.98 Mo) Télécharger le fichier
Origin : Publication funded by an institution
Loading...

Dates and versions

hal-02475099 , version 1 (06-07-2020)

Licence

Attribution

Identifiers

Cite

Matteo Colombo, Jean-Marie Bourhis, Célia Chamontin, Carine Soriano, Stéphanie Villet, et al.. The interaction between the measles virus nucleoprotein and the Interferon Regulator Factor 3 relies on a specific cellular environment. Virology Journal, 2009, 6 (1), pp.59. ⟨10.1186/1743-422X-6-59⟩. ⟨hal-02475099⟩
86 View
45 Download

Altmetric

Share

Gmail Facebook X LinkedIn More