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The C-terminal cytoplasmic tail of herpes simplex virus type 1 gE protein is phosphorylated in vivo and in vitro by cellular enzymes in the absence of other viral proteins

Molecular Virology Laboratory, Hellenic Pasteur Institute, 127 Vas. Sofias Avenue, Athens, Greece¹
Department of Experimental and Diagnostic Medicine (Section of Microbiology), University of Ferrara, Via Luigi Borsari 46, I-44100 Ferrara, Italy²
Interdepartmental Center for Biotechnology, University of Ferrara, Via Fossato di Mortara 64-B, I-44100 Ferrara, Italy³

Author for correspondence: Penelope Mavromara. Fax +30 1 6423498. e-mail penelopm{at}hol.gr

Herpes simplex virus 1 glycoprotein E (gE-1) is highly phosphorylated in culture cells during infection. In this report, it is shown that phosphorylation is mediated by host enzymes in human cells stably transfected with gE, in the absence of other herpesvirus products. In contrast, a tailless gE product (C terminus deletion mutant) is not phosphorylated. By using an in vitro kinase assay combined with linker-insertion mutagenesis, it is shown that casein kinase II catalyses the phosphorylation of the C-terminal domain of the protein. Also, it is demonstrated that the serine residues at positions 476 and/or 477 in the cytoplasmic portion of the protein are the major acceptors for the phosphate groups.

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