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J Virol, March 1998, p. 1731-1736, Vol. 72, No. 3
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Eukaryotic Elongation Factor 1delta Is Hyperphosphorylated by the Protein Kinase Encoded by the UL13 Gene of Herpes Simplex Virus 1

Yasushi Kawaguchi,dagger Charles Van Sant, and Bernard Roizman*

The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, Chicago, Illinois 60637

Received 16 September 1997/Accepted 24 November 1997

The translation elongation factor 1delta (EF-1delta ) consists of two forms, a hypophosphorylated form (apparent Mr, 38,000) and a hyperphosphorylated form (apparent Mr, 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-1delta accumulates in cells infected with herpes simplex virus 1. We now report that the accumulation of the hyperphosphorylated EF-1delta is due to phosphorylation by UL13 protein kinase based on the following observations. (i) The relative amounts of hypo- and hyperphosphorylated EF-1delta in Vero cells infected with mutant virus lacking the UL13 gene could not be differentiated from those of mock-infected cells. In contrast, the hyperphosphorylated EF-1delta was the predominant form in Vero cells infected with wild-type viruses, a recombinant virus in which the deleted UL13 sequences were restored, or with a virus lacking the US3 gene, which also encodes a protein kinase. (ii) The absence of the hyperphosphorylated EF-1delta in cells infected with the UL13 deletion mutant was not due to failure of posttranslational modification of infected-cell protein 22 (ICP22)/US1.5 or of interaction with ICP0, inasmuch as preferential accumulation of hyperphosphorylated EF-1delta was observed in cells infected with viruses from which the genes encoding ICP22/US1.5 or ICP0 had been deleted. (iii) Both forms of EF-1delta were labeled by 32Pi in vivo, but the prevalence of the hyperphosphorylated EF-1delta was dependent on the presence of the UL13 protein. (iv) EF-1delta immunoprecipitated from uninfected Vero cells was phosphorylated by UL13 precipitated by the anti-UL13 antibody from lysates of wild-type virus-infected cells, but not by complexes formed by the interaction of the UL13 antibody with lysates of cells infected with a mutant lacking the UL13 gene. This is the first evidence that a viral protein kinase targets a cellular protein. Together with evidence that ICP0 also interacts with EF-1delta 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.

* Corresponding author. Mailing address: The Marjorie B. Kovler Viral Oncology Laboratories, The University of Chicago, 910 E. 58th St., Chicago, IL 60637. Phone: (773) 702-1898. Fax: (773) 702-1631. E-mail: bernard{at}kovler.uchicago.edu.

dagger Present address: Department of Cell Regulation, Division of Virology and Immunology, Medical Research Institute, Tokyo Medical and Dental University, Yushima, Bunkyo-ku, Tokyo 113, Japan.




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