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Journal of Virology, February 1999, p. 1468-1478, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Polo-Like Kinase 1 as a Target for Human Cytomegalovirus pp65 Lower Matrix Protein

A. Gallina,1 L. Simoncini,1 S. Garbelli,1 E. Percivalle,2 G. Pedrali-Noy,1 K. S. Lee,3 R. L. Erikson,3 B. Plachter,4 G. Gerna,2 and G. Milanesi1,*

Istituto di Genetica Biochimica ed Evoluzionistica, Consiglio Nazionale delle Ricerche,1 and Servizio di Virologia, IRCCS Policlinico San Matteo,2 Pavia, Italy; Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 021383; and Institut für Virologie, Universität Mainz, Mainz, Germany4

Received 7 August 1998/Accepted 13 November 1998

Human cytomegalovirus (HCMV) pp65 protein is the major constituent of viral dense bodies but is dispensable for viral growth in vitro. pp65 copurifies with a S/T kinase activity and has been implicated in phosphorylation of HCMV IE1 immediate-early protein and its escape from major histocompatibility complex 1 presentation. Furthermore, the presence of pp65 correlates with a virion-associated kinase activity. To clarify the role of pp65, yeast two-hybrid system (THS) screening was performed to identify pp65 cellular partners. A total of 18 out of 48 yeast clones harboring cDNAs for putative pp65 binding proteins encoded the Polo-like kinase 1 (Plk1) C-terminal domain. Plk1 behaved as a bona fide pp65 partner in THS control crosses, and the interaction was confirmed by in vitro binding experiments. Endogenous Plk1 was coimmunoprecipitated with pp65 from transiently transfected COS7 cells. In infected fibroblasts, Plk1 was coimmunoprecipitated with pp65 at late infection stages. Furthermore, Plk1 was detected within wild-type HCMV particles but not within the particles of a pp65-negative mutant (RVAd65). The hydrophilic region of pp65 was phosphorylated in vitro by Plk1. These results suggest that one function of pp65 may be to capture a cell kinase, perhaps in order to alter its activity, nucleotide preference, substrate specificity, or subcellular localization to the advantage of HCMV.

* Corresponding author. Mailing address: Istituto di Genetica Biochimica ed Evoluzionistica, CNR, via Abbiategrasso 207, I-27100 Pavia, Italy. Phone: 39-382-546345. Fax: 39-382-422286. E-mail: milanesi{at}igbe.pv.cnr.it.

Journal of Virology, February 1999, p. 1468-1478, Vol. 73, No. 2
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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