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Journal of Virology, July 2009, p. 7349-7352, Vol. 83, No. 14
0022-538X/09/$08.00+0     doi:10.1128/JVI.01748-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Rhinovirus 3C Protease Can Localize in the Nucleus and Alter Active and Passive Nucleocytoplasmic Transport{triangledown}

Reena Ghildyal,1 Benjamin Jordan,1 Dongsheng Li,2 Hayat Dagher,2 Phillip G. Bardin,2 James E. Gern,3 and David A. Jans1*

Department of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria, Australia,1 Department of Respiratory and Sleep Medicine, Monash Medical Centre, Clayton, Victoria, Australia,2 Department of Pediatrics, University of Wisconsin Medical School, Madison, Wisconsin3

Received 18 August 2008/ Accepted 11 March 2009

The degradation of nuclear pore components and disruption of nucleocytoplasmic trafficking during rhinovirus infection have been attributed to viral 2A protease. Here we show for the first time that rhinovirus 3C protease may also have a role. Specifically, we show that 3C and its precursor, 3CD, can target green fluorescent protein to the nucleus of living cells, leading to degradation of nuclear pore components, and that incubation with recombinant 3C disrupts active and passive nucleocytoplasmic transport in a semi-intact cell nuclear transport system dependent on 3C protease activity. 3C may thus contribute to host cell shutoff in infected cells by localizing in the nucleus and facilitating nuclear pore breakdown.

* Corresponding author. Mailing address: Nuclear Signalling Laboratory, Department of Biochemistry and Molecular Biology, Monash University, Wellington Road, Clayton, Victoria, Australia. Phone: 613 9905 3778. Fax: 613 9905 3726. E-mail: David.Jans{at}med.monash.edu.au

{triangledown} Published ahead of print on 29 April 2009.

Journal of Virology, July 2009, p. 7349-7352, Vol. 83, No. 14
0022-538X/09/$08.00+0     doi:10.1128/JVI.01748-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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