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Background  The HCMV  UL76  gene is a member of  UL24  family in herpes virus and encodes a highly conserved herpes virus protein. Inherited from common ancestor, members of Herpes _ UL24 family encode proteins with a conserved N terminal and varied in C terminal region. To define which region (conserved N terminal or unconserved C terminal) of UL76 was responsible for its ability to induce DNA damage and aggresome formation, the wild-type  UL76  gene and two deletion mutants were transfected to cells and analyzed by immunofluorescent staining, Western blotting and comet assay.    Results  We report that the EGFP-fusion proteins present as globular aggresomes and colocalize with γ-H2AX in cells transfected with either pEGFP-UL76 or pEGFP-UL76C. The relative expression level of γ-H2AX and percentage of cells with comet tails were elevated in pEGFP-UL76 or pEGFP-UL76C transfection groups compared to the control.    Conclusion  Our findings suggest that the unconserved C terminal (not the conserved N terminal) of pUL76 was sufficient to induce DNA damage and aggresome formation in transfected cells.

Unconserved C terminal of human cytomegalovirus tegument protein pUL76 elicits nuclear aggresome formation and induces DNA damage in transfected cells