Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids

Michelle A. Bucks, Kevin J. O'Regan, Michael A. Murphy, John Wills, Richard J. Courtney

Research output: Contribution to journalArticle

55 Citations (Scopus)

Abstract

The assembly of the tegument of herpes simplex virus type 1 (HSV-1) is a complex process that involves a number of events at various sites within virus-infected cells. Our studies focused on determining whether tegument proteins, VP1/2 and UL37, are added to capsids located within the nucleus. Capsids were isolated from the nuclear fraction of HSV-1-infected cells and purified by rate-zonal centrifugation to separate B capsids (containing the scaffold proteins and no viral DNA) and C capsids (containing DNA and no scaffold proteins). Western blot analyses of these capsids indicated that VP1/2 associated primarily with C capsids and UL37 associated with B and C capsids. The results demonstrate that at least two of the tegument proteins of HSV-1 are associated with capsids isolated from the nuclear fraction, and these capsid-tegument protein interactions may represent initial events of the tegumentation process.

Original languageEnglish (US)
Pages (from-to)316-324
Number of pages9
JournalVirology
Volume361
Issue number2
DOIs
StatePublished - May 10 2007

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Capsid
Human Herpesvirus 1
Proteins
Zonal Centrifugation
Viral DNA
Capsid Proteins
Western Blotting
Viruses
DNA

All Science Journal Classification (ASJC) codes

  • Virology
  • Infectious Diseases

Cite this

Bucks, Michelle A. ; O'Regan, Kevin J. ; Murphy, Michael A. ; Wills, John ; Courtney, Richard J. / Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. In: Virology. 2007 ; Vol. 361, No. 2. pp. 316-324.
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Herpes simplex virus type 1 tegument proteins VP1/2 and UL37 are associated with intranuclear capsids. / Bucks, Michelle A.; O'Regan, Kevin J.; Murphy, Michael A.; Wills, John; Courtney, Richard J.

In: Virology, Vol. 361, No. 2, 10.05.2007, p. 316-324.

Research output: Contribution to journalArticle

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