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Journal of Virology, September 2002, p. 9434-9445, Vol. 76, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.18.9434-9445.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Signals That Dictate Nuclear, Nucleolar, and Cytoplasmic Shuttling of the {gamma}134.5 Protein of Herpes Simplex Virus Type 1

Guofeng Cheng, Marie-Elena Brett, and Bin He*

Department of Microbiology and Immunology, College of Medicine, The University of Illinois at Chicago, Chicago, Illinois 60612

Received 20 March 2002/ Accepted 12 June 2002

The {gamma}134.5 protein of herpes simplex virus type 1 (HSV-1) is required for viral neurovirulence in vivo. In infected cells, this viral protein prevents the shutoff of protein synthesis mediated by double-stranded-RNA-dependent protein kinase PKR. This is accomplished by recruiting protein phosphatase 1 to dephosphorylate the {alpha} subunit of translation initiation factor eIF-2 (eIF-2{alpha}). Moreover, the {gamma}134.5 protein is implicated in viral egress and interacts with proliferating cell nuclear antigen. In this report, we show that the {gamma}134.5 protein encoded by HSV-1(F) is distributed in the nucleus, nucleolus, and cytoplasm in transfected or superinfected cells. Deletion analysis revealed that the Arg-rich cluster from amino acids 1 to 16 in the {gamma}134.5 protein functions as a nucleolar localization signal. The region from amino acids 208 to 236, containing a bipartite basic amino acid cluster, is able to mediate nuclear localization. R215A and R216A substitutions in the bipartite motif disrupt this activity. Intriguingly, leptomycin B, an inhibitor of nuclear export, blocks the cytoplasmic accumulation of the {gamma}134.5 protein. L134A and L136A substitutions in the leucine-rich motif completely excluded the {gamma}134.5 protein from the cytoplasm. These results suggest that the {gamma}134.5 protein continuously shuttles between the nucleus, nucleolus, and cytoplasm, which may be a requirement for the different activities of the {gamma}134.5 protein in virus-infected cells.

* Corresponding author. Mailing address: Department of Microbiology and Immunology (M/C 790), College of Medicine, The University of Illinois at Chicago, 835 S. Wolcott Ave., Chicago, IL 60612. Phone: (312) 996-2391. Fax: (312) 996-6415. E-mail: tshuo{at}uic.edu.

Journal of Virology, September 2002, p. 9434-9445, Vol. 76, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.18.9434-9445.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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