Details

Autor(en) / Beteiligte

• Colombo, Matteo
• Bourhis, Jean-Marie
• Chamontin, Celia
• Soriano, Carine
• Villet, Stéphanie
• Costanzo, Stéphanie
• Couturier, Marie
• Belle, Valérie
• Fournel, André
• Darbon, Hervé
• Gerlier, Denis
• Longhi, Sonia

Titel

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

Ist Teil von

• Virology journal, 2009-05, Vol.6 (1), p.59-59, Article 59

Ort / Verlag

England: BioMed Central Ltd

Erscheinungsjahr

2009

Link zum Volltext

Quelle

SpringerLink (Online service)

Beschreibungen/Notizen

• 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. After confirming the reciprocal ability of IRF-3 and N to be co-immunoprecipitated in 293T cells, we thoroughly investigated the N(TAIL)-IRF-3 interaction using a recombinant, monomeric form of the regulatory domain of IRF-3. Using a large panel of spectroscopic approaches, including circular dichroism, fluorescence spectroscopy, nuclear magnetic resonance and electron paramagnetic resonance spectroscopy, we failed to detect any direct interaction between IRF-3 and either full-length N or NTAIL under conditions where these latter interact with the C-terminal X domain of the viral phosphoprotein. Furthermore, such interaction was neither detected in E. coli nor in a yeast two hybrid assay. Altogether, these data support the requirement for a specific cellular environment, such as that provided by 293T human cells, for the N(TAIL)-IRF-3 interaction to occur. This dependence from a specific cellular context likely reflects the requirement for a human or mammalian cellular co-factor.