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Journal of Virology, December 1998, p. 10066-10072, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

The Herpes Simplex Virus Triplex Protein, VP23, Exists as a Molten Globule

Marina D. Kirkitadze,1 Paul N. Barlow,1 Nicholas C. Price,2 Sharon M. Kelly,2 Christopher J. Boutell,3 Frazer J. Rixon,3 and David A. McClelland3,*

Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, Edinburgh EH9 3JJ,1 Department of Biological and Molecular Sciences, University of Stirling, Stirling FK9 4LA,2 and Medical Research Council Virology Unit, Glasgow G11 5JR,3 United Kingdom

Received 28 May 1998/Accepted 2 September 1998

Two proteins, VP19C (50,260 Da) and VP23 (34,268 Da), make up the triplexes which connect adjacent hexons and pentons in the herpes simplex virus type 1 capsid. VP23 was expressed in Escherichia coli and purified to homogeneity by Ni-agarose affinity chromatography. In vitro capsid assembly experiments demonstrated that the purified protein was functionally active. Its physical status was examined by differential scanning calorimetry, ultracentrifugation, size exclusion chromatography, circular dichroism, fluorescence spectroscopy, and 8-anilino-1-naphthalene sulfonate binding studies. These studies established that the bacterially expressed VP23 exhibits properties consistent with its being in a partially folded, molten globule state. We propose that the molten globule represents a functionally relevant intermediate which is necessary to allow VP23 to undergo interaction with VP19C in the process of capsid assembly.

* Corresponding author. Mailing address: MRC Virology Unit, Church St., Glasgow G11 5JR, United Kingdom. Phone: 44 141 330 4025. Fax: 44 141 337 2236. E-mail: d.mcclelland{at}bio.gla.ac.uk.

Journal of Virology, December 1998, p. 10066-10072, Vol. 72, No. 12
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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