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J. Biol. Chem., Vol. 277, Issue 26, 23958-23964, June 28, 2002

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Nuclear Import Strategies of High Risk HPV16 L1 Major Capsid Protein^*

Lisa M. Nelson, Robert C. Rose^§, and Junona Moroianu^¶

From the  Biology Department, Boston College, Chestnut Hill, Massachusetts 02467 and the ^§ Department of Medicine and Microbiology and Immunology, University of Rochester School of Medicine and Dentistry, Infectious Diseases Unit, Rochester, New York 14642

During the late phase of human papillomavirus (HPV) infection, the L1 major capsid proteins enter the nuclei of host epithelial cells and, together with the L2 minor capsid proteins, assemble the replicated viral DNA into virions. We investigated the nuclear import of the L1 major capsid protein of high risk HPV16. When digitonin-permeabilized HeLa cells were incubated with HPV16 L1 capsomeres, the L1 protein was imported into the nucleus in a receptor-mediated manner. HPV16 L1 capsomeres formed complexes with Kap 21 heterodimers via interaction with Kap 2. Accordingly, nuclear import of HPV16 L1 capsomeres was mediated by Kap 21 heterodimers, required RanGDP and free GTP, and was independent of GTP hydrolysis. Remarkably, HPV16 L1 capsomeres also interacted with Kap 2 and binding of RanGTP to Kap 2 did not dissociate the HPV16 L1·Kap 2 complex. Significantly, HPV16 L1 capsomeres inhibited the nuclear import of Kap 2 and of a Kap 2-specific M9-containing cargo. These data suggest that, during the productive stage of infection, while the HPV16 L1 major capsid protein enters the nucleus via the Kap 21-mediated pathway to assemble the virions, it also inhibits the Kap 2-mediated nuclear import of host hnRNP A1 protein and, in this way, favors virion formation.

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