Endogenous protein phosphorylation was studied in extracts of hamster fibroblasts infected with pseudorabies virus. The major phosphorylation was detected quite late in infection and involved an acidic protein of Mr 62000. It was catalysed by an enzyme activity with the properties of cellular casein kinase II. Two-dimensional gel analysis was used to demonstrate that this same protein was also phosphorylated in vivo. The phosphoprotein was detected in mature virions and is most likely viral in origin.
KatanM.,
StevelyW. S.,
LeaderD. P.1985; Partial purification and characterization of a new protein kinase from cells infected with pseudorabies virus. European Journal of Biochemistry 152:57–65
KatanM.,
McgarveyM. J.,
StevelyW. S.,
LeaderD. P.1986; The phosphorylation of ribosomal protein S6 by protein kinases from cells infected with pseudorabies virus. Biochemical Journal 239:205–211
KennedyI. M.,
StevelyW. S.,
LeaderD. P.1981; Phosphorylation of ribosomal proteins in hamster fibroblasts infected with pseudorabies virus or herpes simplex virus. Journal of Virology 39:359–366
McGeochD. J.,
DavisonA. J.1986; Alphaherpesviruses possess a gene homologous to the protein kinase gene family of eukaryotes and retroviruses. Nucleic Acids Research 14:1765–1777
PurvesF. C.,
KatanM.,
StevelyW. S.,
LeaderD. P.1986; Characteristics of the induction of a new protein kinase in cells infected with herpesviruses. Journal of General Virology 67:1049–1057
StevelyW. S.,
KatanM.,
StirlingV.,
SmithG.,
LeaderD. p.1985; Protein kinase activities associated with the virions of pseudorabies and herpes simplex virus. Journal of General Virology 66:661–673