The nuclear domain 10 (ND10) is disrupted by the human cytomegalovirus gene product IE1.

The nuclear domain 10 (ND10) is modified during the life cycle of a number of viruses. In this study we report the effect of infection with human cytomegalovirus (HCMV) on the ND10 proteins PML, Sp100, and NDP52. Immunofluorescence analyses revealed that 1-2 h after infection (p.i.) with HCMV the immediate early gene (IE) products IE1 and IE2 transiently colocalize with ND10 proteins. At 4 h p.i. the IE gene products were distributed throughout the nucleus, which was accompanied by a complete disruption of ND10, affecting all analyzed proteins. Transfection studies using different HCMV-cDNA expression plasmids revealed that the expression of IE1 alone was sufficient to induce this disruption. As reported for other ND10-modifying viral proteins, no direct interaction between IE1 and the analyzed ND10 proteins could be detected. The disruption of ND10 by HCMV IE1 is very similar to that described for HSV-1 ICP0. Although there is no sequence similarity between proteins, this observation might suggest similar functions in virus-host interactions.