Self-assembly of purified polyomavirus capsid protein VP1

Salunke, Dinakar M. ; Caspar, Donald L.D. ; Garcea, Robert L. (1986) Self-assembly of purified polyomavirus capsid protein VP1 Cell, 46 (6). pp. 895-904. ISSN 0092-8674

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The polyomavirus major capsid protein VP1, purified after expression of the recombinant gene in E. coli, was isolated as oligomers resembling the dissociated capsomeres derived from viral capsids. Image analysis of low-dose electron micrographs demonstrates that these VP1 oligomers are exclusively pentamers. The purified VP1 pentamers associated to form capsid-like assemblies and polymorphic aggregates at high ionic strength. The capsid-like assemblies were stabilized at low ionic strength by the addition of calcium. Self-assembly of the unmodified, recombinant DNA-generated VP1 implies that the posttranslational charge modifications of VP1 and the minor virion protein components, VP2 and VP3, are not essential for capsid formation. The nonequivalently related subunits of the penta- and hexavalent capsomeres therefore must spontaneously switch their bonding specificity during assembly.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
ID Code:52429
Deposited On:04 Aug 2011 07:48
Last Modified:04 Aug 2011 07:48

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