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Journal of Virology, April 2009, p. 3150-3161, Vol. 83, No. 7
0022-538X/09/$08.00+0     doi:10.1128/JVI.01456-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Mengovirus-Induced Rearrangement of the Nuclear Pore Complex: Hijacking Cellular Phosphorylation Machinery{triangledown}

Maryana V. Bardina,1,2,{dagger} Peter V. Lidsky,1,{dagger} Eugene V. Sheval,2 Ksenia V. Fominykh,1,2 Frank J. M. van Kuppeveld,3 Vladimir Y. Polyakov,2 and Vadim I. Agol1,2*

M. P. Chumakov Institute of Poliomyelitis and Viral Encephalitides, Russian Academy of Medical Sciences, Moscow Region 142782, Russia,1 M. V. Lomonosov Moscow State University, Moscow 119899; Russia,2 Department of Medical Microbiology, Radboud University Nijmegen Medical Centre, Nijmegen Centre for Molecular Life Sciences, Nijmegen 6500 HB, The Netherlands3

Received 11 July 2008/ Accepted 5 January 2009

Representatives of several picornavirus genera have been shown previously to significantly enhance noncontrollable bidirectional exchange of proteins between nuclei and cytoplasm. In enteroviruses and rhinoviruses, enhanced permeabilization of the nuclear pores appears to be primarily due to proteolytic degradation of some nucleoporins (protein components of the pore), whereas this effect in cardiovirus-infected cells is triggered by the leader (L) protein, devoid of any enzymatic activities. Here, we present evidence that expression of L alone was sufficient to cause permeabilization of the nuclear envelope in HeLa cells. In contrast to poliovirus, mengovirus infection of these cells did not elicit loss of nucleoporins Nup62 and Nup153 from the nuclear pore complex. Instead, nuclear envelope permeabilization was accompanied by hyperphosphorylation of Nup62 in cells infected with wild-type mengovirus, whereas both of these alterations were suppressed in L-deficient virus mutants. Since phosphorylation of Nup62 (although less prominent) did accompany permeabilization of the nuclear envelope prior to its mitotic disassembly in uninfected cells, we hypothesize that cardiovirus L alters the nucleocytoplasmic traffic by hijacking some components of the normal cell division machinery. The variability and biological significance of picornaviral interactions with the nucleocytoplasmic transport in the infected cells are discussed.

* Corresponding author. Mailing address: Institute of Poliomyelitis, Moscow Region 142782, Russia. Phone: 7 (495) 439 9026. Fax: 7 (495) 439 9321. E-mail: agol{at}belozersky.msu.ru

{triangledown} Published ahead of print on 14 January 2009.

{dagger} M.V.B. and P.V.L. contributed equally to this study.

Journal of Virology, April 2009, p. 3150-3161, Vol. 83, No. 7
0022-538X/09/$08.00+0     doi:10.1128/JVI.01456-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



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