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Journal of Virology, September 2002, p. 9368-9377, Vol. 76, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.18.9368-9377.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Interaction of the Vp3 Nuclear Localization Signal with the Importin {alpha}2/ß Heterodimer Directs Nuclear Entry of Infecting Simian Virus 40

Akira Nakanishi,1 Dorothy Shum,1 Hiroshi Morioka,2 Eiko Otsuka,2,{dagger} and Harumi Kasamatsu1*

Department of Molecular, Cell, and Developmental Biology and Molecular Biology Institute, University of California at Los Angeles, Los Angeles, California 90095,1 Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan2

Received 13 March 2002/ Accepted 12 June 2002

For nuclear entry of large nucleoprotein complexes, it is thought that one key nuclear localization signal (NLS) of a protein component becomes exposed to mediate importin recognition. We show that the nuclear entry of simian virus 40 involves a dynamic interplay between two distinct interiorly situated capsid NLSs, the Vp1 NLS and the Vp3 NLS, and the selective exposure and importin recognition of the Vp3 NLS. The Vp3 NLS-null mutants assembled normally into virion-like particles (VLP) in mutant DNA-transfected cells. When used to infect a new host, the null VLP entered the cell normally but was impaired in viral DNA nuclear entry due to a lack of recognition by the importin {alpha}2/ß heterodimer, leading to reduced viability. Both Vp3 and Vp1 NLSs directed importin interaction in vitro, but the Vp1 NLS, which overlaps the Vp1 DNA binding domain, did not bind importins in the presence of DNA. The results suggest that certain canonical NLSs within a nucleoprotein complex, such as the Vp1 NLS, can be masked from functioning by binding to the nucleic acid component and that the availability of an NLS that is not masked and can become exposed for importin binding, such as the Vp3 NLS, is a general feature of the nuclear entry of the nucleoprotein complexes, including those of other animal viruses.

* Corresponding author. Mailing address: Molecular Biology Institute, 456 Boyer Hall, University of California, Los Angeles, 611 E. Charles E. Young Dr., Box 951570, Los Angeles, CA 90095-1570. Phone: (310) 825-3048. Fax: (310) 206-7286. E-mail: harumi_K{at}mbi.ucla.edu.

{dagger} Present address: National Institute of Advanced Science and Technology (AIST), 2-17 Tsukisamu-higashi, Toyohira-ku, Sapporo 062-8517, Japan.

Journal of Virology, September 2002, p. 9368-9377, Vol. 76, No. 18
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.18.9368-9377.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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