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Journal of Virology, February 2006, p. 1798-1806, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1798-1806.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Importin-ß Family Members Mediate Alpharetrovirus Gag Nuclear Entry via Interactions with Matrix and Nucleocapsid

Kristin L. Butterfield-Gerson,1,{dagger} Lisa Z. Scheifele,2,{dagger},{ddagger} Eileen P. Ryan,2 Anita K. Hopper,1 and Leslie J. Parent2,3*

Departments of Biochemistry and Molecular Biology,1 Medicine,2 Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, Pennsylvania 170333

Received 21 September 2005/ Accepted 23 November 2005

The retroviral Gag polyprotein orchestrates the assembly and release of virus particles from infected cells. We previously reported that nuclear transport of the Rous sarcoma virus (RSV) Gag protein is intrinsic to the virus assembly pathway. To identify cis- and trans-acting factors governing nucleocytoplasmic trafficking, we developed novel vectors to express regions of Gag in Saccharomyces cerevisiae. The localization of Gag proteins was examined in the wild type and in mutant strains deficient in members of the importin-ß family. We confirmed the Crm1p dependence of the previously identified Gag p10 nuclear export signal. The known nuclear localization signal (NLS) in MA (matrix) was also functional in S. cerevisiae, and additionally we discovered a novel NLS within the NC (nucleocapsid) domain of Gag. MA utilizes Kap120p and Mtr10p import receptors while nuclear entry of NC involves the classical importin-{alpha}/ß (Kap60p/95p) pathway. NC also possesses nuclear targeting activity in avian cells and contains the primary signal for the import of the Gag polyprotein. Thus, the nucleocytoplasmic dynamics of RSV Gag depend upon the counterbalance of Crm1p-mediated export with two independent NLSs, each interacting with distinct nuclear import factors.

* Corresponding author. Mailing address: Division of Infectious Diseases HO36, Penn State College of Medicine, 500 University Drive, Hershey, PA 17033. Phone: (717) 531-3997. Fax: (717) 531-4633. E-mail: lparent{at}psu.edu.

{dagger} These authors contributed equally to this work.

{ddagger} Present address: Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, 733 North Broadway, Baltimore, MD 21205.

Journal of Virology, February 2006, p. 1798-1806, Vol. 80, No. 4
0022-538X/06/$08.00+0     doi:10.1128/JVI.80.4.1798-1806.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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