Phosphorylation of Structural Components Promotes Dissociation of the Herpes Simplex Virus Type 1 Tegument

摘要: The role of phosphorylation in the dissociation structural components herpes simplex virus type 1 (HSV-1) tegument was investigated, using an vitro assay. Addition physiological concentrations ATP and magnesium to wild-type virions presence detergent promoted release VP13/14 VP22. VP1/2 UL13 protein kinase were not significantly solubilized. However, a with inactivated protein, we found that VP22 severely impaired. casein II (CKII) mutant release. Heat inactivation or addition phosphatase inhibited both proteins. Incorporation radiolabeled into assay demonstrated VP1/2, VP13/14, VP16, Incubation detergent-purified, heat-inactivated capsid-tegument recombinant kinases showed by CKII, A (PKA), PKC, VP16 PKA, CKII PKC. Proteolytic mapping phosphoamino acid analysis phosphorylated correlated previously published work. virion-associated cells infected cycloheximide. Use equine herpesvirus resulted enhanced VP10, homolog HSV-1 VP13/14. These results suggest major proteins from alphaherpesvirus may be initiated events mediated cellular kinases.