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Nuclear Localization of Avian Polyomavirus Structural Protein VP1 is a Prerequisite for the Formation of Virus-like Particles

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Journal J Virol
Date 2003 Dec 25
PMID 14694124
Citations 3
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Abstract

Virions of polyomaviruses consist of the major structural protein VP1, the minor structural proteins VP2 and VP3, and the viral genome associated with histones. An additional structural protein, VP4, is present in avian polyomavirus (APV) particles. As it had been reported that expression of APV VP1 in insect cells did not result in the formation of virus-like particles (VLP), the prerequisites for particle formation were analyzed. To this end, recombinant influenza viruses were created to (co)express the structural proteins of APV in chicken embryo cells, permissive for APV replication. VP1 expressed individually or coexpressed with VP4 did not result in VLP formation; both proteins (co)localized in the cytoplasm. Transport of VP1, or the VP1-VP4 complex, into the nucleus was facilitated by the coexpression of VP3 and resulted in the formation of VLP. Accordingly, a mutant APV VP1 carrying the N-terminal nuclear localization signal of simian virus 40 VP1 was transported to the nucleus and assembled into VLP. These results support a model of APV capsid assembly in which complexes of the structural proteins VP1, VP3 (or VP2), and VP4, formed within the cytoplasm, are transported to the nucleus using the nuclear localization signal of VP3 (or VP2); there, capsid formation is induced by the nuclear environment.

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References
1.
Salunke D, Caspar D, Garcea R . Self-assembly of purified polyomavirus capsid protein VP1. Cell. 1986; 46(6):895-904. DOI: 10.1016/0092-8674(86)90071-1. View

2.
An K, Smiley S, Gillock E, Reeves W, Consigli R . Avian polyomavirus major capsid protein VP1 interacts with the minor capsid proteins and is transported into the cell nucleus but does not assemble into capsid-like particles when expressed in the baculovirus system. Virus Res. 1999; 64(2):173-85. DOI: 10.1016/s0168-1702(99)00093-3. View

3.
Krautwald M, Muller H, Kaleta E . Polyomavirus infection in budgerigars (Melopsittacus undulatus): clinical and aetiological studies. Zentralbl Veterinarmed B. 1989; 36(6):459-67. DOI: 10.1111/j.1439-0450.1989.tb00628.x. View

4.
Montross L, Watkins S, MORELAND R, Mamon H, Caspar D, Garcea R . Nuclear assembly of polyomavirus capsids in insect cells expressing the major capsid protein VP1. J Virol. 1991; 65(9):4991-8. PMC: 248962. DOI: 10.1128/JVI.65.9.4991-4998.1991. View

5.
Rihs H, Peters R, HOBOM G . Nuclear localization of budgerigar fledgling disease virus capsid protein VP2 is conferred by residues 308-317. FEBS Lett. 1991; 291(1):6-8. DOI: 10.1016/0014-5793(91)81090-u. View