The UL24 protein of herpes simplex virus 1 affects the sub-cellular distribution of viral glycoproteins involved in fusion

Virology. 2013 Sep;444(1-2):263-73. doi: 10.1016/j.virol.2013.06.021. Epub 2013 Jul 20.

Abstract

Mutations in UL24 of herpes simplex virus type 1 can lead to a syncytial phenotype. We hypothesized that UL24 affects the sub-cellular distribution of viral glycoproteins involved in fusion. In non-immortalized human foreskin fibroblasts (HFFs) we detected viral glycoproteins B (gB), gD, gH and gL present in extended blotches throughout the cytoplasm with limited nuclear membrane staining; however, in HFFs infected with a UL24-deficient virus (UL24X), staining for the viral glycoproteins appeared as long, thin streaks running across the cell. Interestingly, there was a decrease in co-localized staining of gB and gD with F-actin at late times in UL24X-infected HFFs. Treatment with chemical agents that perturbed the actin cytoskeleton hindered the formation of UL24X-induced syncytia in these cells. These data support a model whereby the UL24 syncytial phenotype results from a mislocalization of viral glycoproteins late in infection.

Keywords: F-actin; Herpes simplex virus 1; Syncytia; UL24; gB; gD.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Fusion*
  • Cells, Cultured
  • Fibroblasts / virology
  • Giant Cells / cytology
  • Giant Cells / virology
  • Glycoproteins / metabolism*
  • Herpesvirus 1, Human / genetics
  • Herpesvirus 1, Human / physiology
  • Humans
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Viral Proteins / genetics
  • Viral Proteins / metabolism

Substances

  • Glycoproteins
  • Mutant Proteins
  • UL24 protein, Human herpesvirus 1
  • Viral Proteins