The insulin degrading enzyme binding domain of varicella-zoster virus (VZV) glycoprotein E is important for cell-to-cell spread and VZV infectivity, while a glycoprotein I binding domain is essential for infection

Virology. 2009 Apr 10;386(2):270-9. doi: 10.1016/j.virol.2009.01.023. Epub 2009 Feb 23.

Abstract

Varicella-zoster virus (VZV) glycoprotein E (gE) interacts with glycoprotein I and with insulin degrading enzyme (IDE), which is a receptor for the virus. We found that a VZV gE deletion mutant could only be grown in cells expressing gE. Expression of VZV gE on the surface of cells did not interfere with VZV infection. HSV deleted for gE is impaired for cell-to-cell spread; VZV gE could not complement this activity in an HSV gE null mutant. VZV lacking the IDE binding domain of gE grew to peak titers nearly equivalent to parental virus; however, it was impaired for cell-to-cell spread and for infectivity with cell-free virus. VZV deleted for a region of gE that binds glycoprotein I could not replicate in cell culture unless grown in cells expressing gE. We conclude that the IDE binding domain is important for efficient cell-to-cell spread and infectivity of cell-free virus.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Animals
  • Binding Sites
  • Cell Line, Tumor
  • Cosmids
  • Herpesvirus 3, Human / genetics
  • Herpesvirus 3, Human / metabolism
  • Herpesvirus 3, Human / pathogenicity*
  • Herpesvirus 3, Human / physiology
  • Humans
  • Insulysin / metabolism*
  • Receptors, Virus / metabolism
  • Sequence Deletion
  • Viral Envelope Proteins / genetics
  • Viral Envelope Proteins / metabolism*
  • Virus Replication

Substances

  • Receptors, Virus
  • Viral Envelope Proteins
  • glycoprotein E, varicella-zoster virus
  • Insulysin