Functions of a protein kinase activity associated with purified capsids of the granulosis virus infecting Plodia interpunctella.

Activation of a protein kinase associated with purified capsids of the granulosis virus of Plodia interpunctella resulted in release of the DNA from the nucleocapsid as determined by electron microscopy. Heat treatment of the virions (65 degrees for 10 min) inactivated the kinase and prevented this uncoating event. The basic viral core protein, VP12, is the predominant phosphate acceptor for the protein kinase and was the only DNA-binding protein present in nucleocapsids. VP12 binding to 32P-nick-translated granulosis virus DNA was determined by the hybridization of the nick-translated DNA to nucleocapsid proteins transferred electrophoretically to nitrocellolose after separation by sodium dodecyl sulfate polyacrylamide gel electrophoresis. Profiles obtained when nick-translated DNA was added to sucrose gradients in the absence and presence of VP12 substantiated the DNA-binding capability of VP12. Comparison of the DNA-binding capability of phosphorylated and nonphosphorylated VP12 using sucrose gradient sedimentation provided evidence that phosphorylation of the basic protein reduced its capability to bind DNA. We propose the endogenous protein kinase activity of the granulosis virus may function in two ways: release of the DNA from the nucleocapsid (uncoating), and decondensation of the DNA due to phosphorylation of the basic core protein, VP12.