Abstract
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 language | English |
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Pages (from-to) | 4029-4033 |
Number of pages | 5 |
Journal | Journal of Virology |
Volume | 86 |
Issue number | 7 |
Early online date | 25 Jan 2012 |
DOIs | |
Publication status | Published - Apr 2012 |
Keywords
- ring finger domain
- binding domain
- type-1 mutant
- in-vitro
- PML
- infection
- VMW110
- gene
- degradation
- expression