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Journal of Virology, March 2005, p. 3557-3564, Vol. 79, No. 6
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.6.3557-3564.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Importin- Promotes Passage through the Nuclear Pore Complex of Human Immunodeficiency Virus Type 1 Vpr

Masakazu Kamata,¹ Yuko Nitahara-Kasahara,¹ Yoichi Miyamoto,² Yoshihiro Yoneda,² and Yoko Aida^1*

Retrovirus Research Unit, RIKEN, Wako, Saitama,¹ Department of Frontier Biosciences, Graduate School of Frontier Biosciences, Osaka University, Suita, Osaka, Japan²

Received 16 June 2004/ Accepted 3 November 2004

Viral protein R (Vpr) of human immunodeficiency virus type 1 has potent karyophilic properties, but details of the mechanism by which it enters the nucleus remain to be clarified. We reported previously that two regions, located between residues 17 and 34 (H1) and between residues 46 and 74 (H2), are indispensable for the nuclear localization of Vpr. Here, we reveal that a chimeric protein composed of the nuclear localization signal of Vpr, glutathione S-transferase, and green fluorescent protein was localized at the nuclear envelope and then entered the nucleus upon addition of importin-. An in vitro transport assay using a series of derivatives of importin- demonstrated that the carboxyl terminus was required for this nuclear import process. We also showed that Vpr interacts with importin- through H1 and H2; only the interaction via H1 is indispensable for the nuclear entry of Vpr. These observations indicate that importin- functions as a mediator for the nuclear entry of Vpr.

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* Corresponding author. Mailing address: Retrovirus Research Unit, RIKEN, 2-1 Hirosawa, Wako, Saitama 351-0198, Japan. Phone: 81 48 462 4408. Fax: 81 48 462 4399. E-mail: aida{at}riken.jp.

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Journal of Virology, March 2005, p. 3557-3564, Vol. 79, No. 6
0022-538X/05/$08.00+0     doi:10.1128/JVI.79.6.3557-3564.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

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