Reference : ORF9p phosphorylation by ORF47p is crucial for the formation and egress of the Varice...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/137585
ORF9p phosphorylation by ORF47p is crucial for the formation and egress of the Varicella-zoster virus (VZV) viral particles.
English
Riva, Laura mailto [Université de Liège - ULiège > > GIGA-R : Virologie - Immunologie >]
Thiry, Marc mailto [Université de Liège - ULiège > Département des sciences de la vie > Biologie cellulaire >]
BONTEMS, Sébastien mailto [Centre Hospitalier Universitaire de Liège - CHU > >]
Joris, Aline [> >]
Piette, Jacques mailto [Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Virologie - Immunologie >]
Lebrun, Marielle* [Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Virologie et immunologie >]
Sadzot-Delvaux, Catherine* mailto [Université de Liège - ULiège > Département des sciences de la vie > GIGA-R : Virologie et immunologie >]
* These authors have contributed equally to this work.
2013
Journal of Virology
87
5
2868-2881
Yes (verified by ORBi)
International
0022-538X
1098-5514
[en] Varicella Zoster virus ; ORF9p ; phosphorylation
[en] The role of the tegument during the herpesvirus lytic cycle is still not clearly established, particularly at the late phase of infection, when the newly produced viral particles need to be fully assembled before being released from the infected cell. The Varicella-zoster virus (VZV) protein coded by ORF9 (ORF9p) is an essential tegument protein and, even though its mRNA is the most expressed during the productive infection, little is known about its functions. Using a GalK positive/negative selection technique, we modified a BAC containing the complete VZV genome creating viruses expressing mutant versions of ORF9p.We showed that ORF9p is hyper-phosphorylated during the infection, especially through its interaction with the viral Ser/Thr kinase ORF47p; we identified a consensus site within ORF9p recognized by ORF47p and demonstrated its importance for ORF9p phosphorylation. Strikingly, an ultra-structural analysis revealed that the mutation of this consensus site (Glutamate 85 to Arginine) strongly affects viral assembly and release, reproducing ORF47 kinase dead VZV phenotype. It also slightly diminishes the infectivity towards immature dendritic cells. Taken together, our results identify ORF9p as a new viral substrate of ORF47p and suggest a determinant role of this phosphorylation for viral infectivity, especially during the process of viral particle formation and egress.
Researchers
http://hdl.handle.net/2268/137585
10.1128/JVI.02757-12

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