“…UL3 and UL30 have little sequence similarity and vary considerably in their contribution to CMV infection in fibroblasts; UL3 is classified a non-essential gene, while deletion of UL30 caused a severe defect in viral replication [46]. The Meq protein from the avian herpesvirus MDV has been reported to associate with Cajal bodies [7], however, to our knowledge, CMV UL3 and UL30 are the first human herpesvirus proteins reported to associate with or disrupt these structures. Although the functions of Cajal bodies are not completely clear, they are strongly associated with transcription and the maturation of ribonuclear particles and only form when these processes are active [49].…”
Herpesviruses are large, ubiquitous DNA viruses with complex host interactions, yet many of the proteins encoded by these viruses have not been functionally characterized. As a first step in functional characterization, we determined the subcellular localization of 234 epitope-tagged proteins from herpes simplex virus, cytomegalovirus, and Epstein–Barr virus. Twenty-four of the 93 proteins with nuclear localization formed subnuclear structures. Twelve of these localized to the nucleolus, and five at least partially localized with promyelocytic leukemia (PML) bodies, which are known to suppress viral lytic infection. In addition, two proteins disrupted Cajal bodies, and 19 of the nuclear proteins significantly decreased the number of PML bodies per cell, including six that were shown to be SUMO-modified. These results have provided the first functional insights into over 120 previously unstudied proteins and suggest that herpesviruses employ multiple strategies for manipulating nuclear bodies that control key cellular processes.
“…UL3 and UL30 have little sequence similarity and vary considerably in their contribution to CMV infection in fibroblasts; UL3 is classified a non-essential gene, while deletion of UL30 caused a severe defect in viral replication [46]. The Meq protein from the avian herpesvirus MDV has been reported to associate with Cajal bodies [7], however, to our knowledge, CMV UL3 and UL30 are the first human herpesvirus proteins reported to associate with or disrupt these structures. Although the functions of Cajal bodies are not completely clear, they are strongly associated with transcription and the maturation of ribonuclear particles and only form when these processes are active [49].…”
Herpesviruses are large, ubiquitous DNA viruses with complex host interactions, yet many of the proteins encoded by these viruses have not been functionally characterized. As a first step in functional characterization, we determined the subcellular localization of 234 epitope-tagged proteins from herpes simplex virus, cytomegalovirus, and Epstein–Barr virus. Twenty-four of the 93 proteins with nuclear localization formed subnuclear structures. Twelve of these localized to the nucleolus, and five at least partially localized with promyelocytic leukemia (PML) bodies, which are known to suppress viral lytic infection. In addition, two proteins disrupted Cajal bodies, and 19 of the nuclear proteins significantly decreased the number of PML bodies per cell, including six that were shown to be SUMO-modified. These results have provided the first functional insights into over 120 previously unstudied proteins and suggest that herpesviruses employ multiple strategies for manipulating nuclear bodies that control key cellular processes.
“…This suggests that vIL-8 affects virus replication rather than tumorigenesis. The possibility of immunomodulatory functions for vIL-8 cannot be eliminated, but the discovery that it can also be expressed as a fusion protein with the MDV oncoprotein Meq presents the likelihood of a more complicated situation [192].…”
Section: Immunoevasion Mechanism Of the Avian Herpesvirusesmentioning
“…This suggests that vIL-8 affects virus replication rather than tumorigenesis. The possibility of immunomodulatory functions for vIL-8 cannot be eliminated but the discovery that it can also be expressed as a fusion protein with the MDV oncoprotein Meq presents the likelihood of a more complicated situation (Anobile et al, 2006).…”
Section: Immunoevasion Mechanism Of the Avian Herpesvirusesmentioning
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