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The translation elongation factor 1δ (EF-1δ) consists of two forms, a hypophosphorylated form (apparentM r , 38,000) and a hyperphosphorylated form (apparentM r , 40,000). Earlier Y. Kawaguchi, R. Bruni, and B. Roizman (J. Virol. 71:1019–1024, 1997) reported that whereas mock-infected cells accumulate the hypophosphorylated form, the hyperphosphorylated form of EF-1δ accumulates in cells infected with herpes simplex virus 1. We now report that the accumulation of the hyperphosphorylated EF-1δ is due to phosphorylation by UL 13 protein kinase based on the following observations. (i) The relative amounts of hypo- and hyperphosphorylated EF-1δ in Vero cells infected with mutant virus lacking the UL 13 gene could not be differentiated from those of mock-infected cells. In contrast, the hyperphosphorylated EF-1δ was the predominant form in Vero cells infected with wild-type viruses, a recombinant virus in which the deleted UL 13 sequences were restored, or with a virus lacking the US 3 gene, which also encodes a protein kinase. (ii) The absence of the hyperphosphorylated EF-1δ in cells infected with the UL 13 deletion mutant was not due to failure of posttranslational modification of infected-cell protein 22 (ICP22)/US 1.5 or of interaction with ICP0, inasmuch as preferential accumulation of hyperphosphorylated EF-1δ was observed in cells infected with viruses from which the genes encoding ICP22/US 1.5 or ICP0 had been deleted. (iii) Both forms of EF-1δ were labeled by32 Pi in vivo, but the prevalence of the hyperphosphorylated EF-1δ was dependent on the presence of the UL 13 protein. (iv) EF-1δ immunoprecipitated from uninfected Vero cells was phosphorylated by UL 13 precipitated by the anti-UL 13 antibody from lysates of wild-type virus-infected cells, but not by complexes formed by the interaction of the UL 13 antibody with lysates of cells infected with a mutant lacking the UL 13 gene. This is the first evidence that a viral protein kinase targets a cellular protein. Together with evidence that ICP0 also interacts with EF-1δ reported in the paper cited above, these data indicate that herpes simplex virus 1 has evolved a complex strategy for optimization of infected-cell protein synthesis.

Eukaryotic Elongation Factor 1δ Is Hyperphosphorylated by the Protein Kinase Encoded by the U L 13 Gene of Herpes Simplex Virus 1

Eukaryotic Elongation Factor 1δ Is Hyperphosphorylated by the Protein Kinase Encoded by the U _L 13 Gene of Herpes Simplex Virus 1