Table 2.

Properties of ICP0 proteins expressed by viruses used in this studya

Virus EGFP versionICP0 structureComments
17+vEG-1101–775Wild type
dl1403vEG-dl1101–105Null mutant
FXEvEG-FXE1–105::150–775RING finger deletion
D22NAb 1–161::189–775RING finger distal region deletion
E32NA4-aac insertion at 222Insertion in RING finger distal region
K144ENAaa 144 point mutationSubstitution in RING finger helix
Q148ENAaa 148 point mutationSubstitution in RING finger helix
N151DNAaa 151 point mutationSubstitution in RING finger helix
M1vEG-M1R623L, K624IUSP7 binding negative substitution
D12vEG-D121–593::634–775USP7 binding region deletion
E52XvEG-E52X1–593C-terminal truncation.
  • a Data were assembled from references9, 21, 33, 37, and 52. The EGFP version viruses have ICP0 containing the cognate mutation linked to the C-terminal end of EGFP, except in the case of EG-dl110, which expresses EGFP in place of ICP0.

  • b NA, not applicable.

  • c aa, amino acid.