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

MD Kirkitadze, PN Barlow, NC Price, SM Kelly, CJ Boutell, FJ Rixon, DA McClelland

Research output: Contribution to journalArticlepeer-review

Abstract

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 inEscherichia 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.
Original languageEnglish
Pages (from-to)10066-10072
Number of pages7
JournalJournal of Virology
Volume72
Issue number12
Publication statusPublished - 1998

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