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Journal of Virology, December 2004, p. 13447-13454, Vol. 78, No. 24
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.24.13447-13454.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Positively Charged Termini of L2 Minor Capsid Protein Required for Bovine Papillomavirus Infection Function Separately in Nuclear Import and DNA Binding

Alyson Fay,¹ William H. Yutzy IV,² Richard B. S. Roden,^2,3,4 and Junona Moroianu^1*

Biology Department, Boston College, Chestnut Hill, Massachusetts,¹ Departments of Pathology,² Oncology,³ Gynecology & Obstretics, The Johns Hopkins University, Baltimore, Maryland⁴

Received 2 June 2004/ Accepted 29 July 2004

During the papillomavirus (PV) life cycle, the L2 minor capsid protein enters the nucleus twice: in the initial phase after entry of virions into cells and in the productive phase to mediate encapsidation of the newly replicated viral genome. Therefore, we investigated the interactions of the L2 protein of bovine PV type 1 (BPV1) with the nuclear import machinery and the viral DNA. We found that BPV1 L2 bound to the karyopherin 2 (Kap 2) adapter and formed a complex with Kap 2ß1 heterodimers. Previous data have shown that the positively charged termini of BPV1 L2 are required for BPV1 infection after the binding of the virions to the cell surface. We determined that these BPV1 L2 termini function as nuclear localization signals (NLSs). Both the N-terminal NLS (nNLS) and the C-terminal NLS (cNLS) interacted with Kap 2, formed a complex with Kap 2ß1 heterodimers, and mediated nuclear import via a Kap 2ß1 pathway. Interestingly, the cNLS was also the major DNA binding site of BPV1 L2. Consistent with the promiscuous DNA encapsidation by BPV1 pseudovirions, this DNA binding occurred without nucleotide sequence specificity. Moreover, an L2 mutant encoding a scrambled version of the cNLS, which supports production of virions, rescued the DNA binding but not the Kap 2 interaction. These data support a model in which BPV1 L2 functions as an adapter between the viral DNA via the cNLS and the Kaps via the nNLS and facilitates nuclear import of the DNA during infection.

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* Corresponding author. Mailing address: Biology Department, Boston College, Chestnut Hill, MA 02467. Phone: (617) 552-1713. Fax: (617) 552-2011. E-mail: moroianu{at}bc.edu.

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Journal of Virology, December 2004, p. 13447-13454, Vol. 78, No. 24
0022-538X/04/$08.00+0     DOI: 10.1128/JVI.78.24.13447-13454.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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