Lahmidi, Soumia; Strunk, Ulrike; Smiley, James R.; Pearson, Angela et Duplay, Pascale (2017). Herpes simplex virus 1 infection of T cells causes VP11/12-dependent phosphorylation and degradation of the cellular protein Dok-2 Virology , vol. 511 . pp. 66-73. DOI: 10.1016/j.virol.2017.08.018.
Ce document n'est pas hébergé sur EspaceINRS.Résumé
Previous studies have shown that HSV-1 infection of lymphocytes induces the tyrosine phosphorylation of several proteins that might correspond to viral or host proteins. VP11/12, a viral tegument protein, is the major HSV-induced tyrosine phosphorylated protein identified thus far. In this report, we demonstrated that the cellular adaptor proteins Dok-2 and Dok-1 are tyrosine phosphorylated upon HSV-1 infection. In addition, HSV-1 induced the selective degradation of Dok-2. Finally, we provide evidence that Dok-2 interacts with VP11/12, and that HSV-induced tyrosine phosphorylation and degradation of Dok-2 require VP11/12. Inactivation of either the Src Family Kinases binding motifs or the SHC binding motif of VP11/12 eliminated the interaction of Dok-2 with VP11/12. Elimination of the binding of Dok-2 to VP11/12 prevented Dok-2 phosphorylation and degradation. We propose that HSV-induced Dok phosphorylation and Dok-2 degradation is an immune evasion mechanism to inactivate T cells that might play an important role in HSV pathogenesis.
| Type de document: | Article |
|---|---|
| Mots-clés libres: | Dok, Herpes simplex virus, VP11/12, Tegument, T cell, Immune evasion |
| Centre: | Centre INRS-Institut Armand Frappier |
| Date de dépôt: | 10 mars 2019 19:27 |
| Dernière modification: | 10 mars 2019 19:27 |
| URI: | https://espace.inrs.ca/id/eprint/7527 |
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