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Journal of Virology, February 2000, p. 1658-1662, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Mechanism of Assembly of Recombinant Murine Polyomavirus-Like Particles

Uli Schmidt,* Rainer Rudolph, and Gerald Böhm

Institut für Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, D-06120 Halle (Saale), Germany

Received 6 July 1999/Accepted 9 November 1999

VP1 is the major viral coat protein of murine polyomavirus and can be used for the generation of virus-like particles in vitro. Here, we demonstrate that capsid assembly is an equilibrium reaction followed by oxidation of intracapsomere disulfide bonds, which are not essential for the formation of virus-like particles but enable complete particle assembly and prevent capsid dissembly.

* Corresponding author. Mailing address: Institut für Biotechnologie, Martin-Luther-Universität Halle-Wittenberg, Kurt-Mothes-Strasse 3, D-06120 Halle (Saale), Germany. Phone: 49 345 55 24948 or 49 345 55 24940. Fax: 345 55 27013. E-mail: uli.schmidt{at}biochemtech.uni-halle.de.

Journal of Virology, February 2000, p. 1658-1662, Vol. 74, No. 4
0022-538X/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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