Localization of the herpes simplex virus type 1 major capsid protein VP5 to the cell nucleus requires the abundant scaffolding protein VP22a

J Gen Virol. 1994 May;75 ( Pt 5):1091-9. doi: 10.1099/0022-1317-75-5-1091.


The intracellular distributions of three herpes simplex virus type 1 (HSV-1) capsid proteins, VP23, VP5 and VP22a, were examined using vaccinia virus and plasmid expression systems. During infection of cells with HSV-1 wild-type virus, all three proteins were predominantly located in the nucleus, which is the site of capsid assembly. However, when expressed in the absence of any other HSV-1 proteins, although VP22a was found exclusively in the nucleus as expected, VP5 and VP23 were distributed throughout the cell. Thus nuclear localization is not an intrinsic property of these proteins but must be mediated by one or more HSV-1-induced proteins. Co-expression experiments demonstrated that VP5 was efficiently transported to the nucleus in the presence of VP22a, but the distribution of VP23 was unaffected by the presence of either or both of the other two proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biological Transport
  • Capsid / genetics
  • Capsid / isolation & purification
  • Capsid / metabolism*
  • Capsid Proteins
  • Cell Compartmentation*
  • Cell Nucleus / metabolism
  • Endopeptidases / metabolism*
  • Fluorescent Antibody Technique
  • Herpesvirus 1, Human / genetics
  • Herpesvirus 1, Human / growth & development*
  • Recombinant Proteins / biosynthesis
  • Vaccinia virus / genetics
  • Viral Proteins*


  • Capsid Proteins
  • Recombinant Proteins
  • VP23 protein, Human herpesvirus 1
  • VP5 protein, Herpes simplex virus type 1
  • Viral Proteins
  • scaffold protein, Herpes simplex virus-1
  • Endopeptidases