Depletion of intracellular zinc inhibits the ubiquitin ligase activity of viral regulatory protein ICP0 and restricts herpes simplex virus 1 replication in cell culture

Kyle Grant, Louise Grant, Lily Tong, Chris Boutell

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13 Citations (Scopus)


The viral ubiquitin ligase ICP0 stimulates the onset of HSV-1 lytic infection and productive reactivation of viral genomes from latency. In order to mediate these processes, it requires its C3HC4 RING finger domain, a tertiary structural fold that is coordinated by the binding of two zinc (Zn2+) atoms. Here we formally demonstrate that Zn2+ binding and intracellular Zn2+ levels are critical for ICP0's biochemical activity and that depletion of intracellular Zn2+ severely attenuates HSV-1 replication.

Original languageEnglish
Pages (from-to)4029-4033
Number of pages5
JournalJournal of Virology
Issue number7
Early online date25 Jan 2012
Publication statusPublished - Apr 2012


  • ring finger domain
  • binding domain
  • type-1 mutant
  • in-vitro
  • PML
  • infection
  • VMW110
  • gene
  • degradation
  • expression

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