Abstract
ABSTRACTThe human adenovirus genome is transported into the nucleus, where viral gene transcription, viral DNA replication, and virion assembly take place. Posttranslational modifications by small ubiquitin-like modifiers (SUMOs) are implicated in the regulation of diverse cellular processes, particularly nuclear events. It is not surprising, therefore, that adenovirus modulates and utilizes the host sumoylation system. Adenovirus early proteins play an important role in establishing optimal host environments for virus replication within infected cells by stimulating the cell cycle and counteracting host antiviral defenses. Here, we review findings on the mechanisms and functional consequences of the interplay between human adenovirus early proteins and the host sumoylation system.
Highlights
The human adenovirus genome is transported into the nucleus, where viral gene transcription, viral DNA replication, and virion assembly take place
In 1996, the first evidence for association between Ad and host sumoylation was obtained by screening of adenovirus 5 (Ad5) E1A protein binding partners using the yeast two-hybrid system [19]. These results identified mouse Ubc9 as an E1A-interacting protein and further showed that CR2 of either Ad5 or Ad12 E1A is required for binding murine Ubc9 in yeast [19]
When CRM1-dependent nuclear export is blocked by leptomycin B (LMB) treatment, wild-type E1B 55-kDa protein (E1B-55K) is localized in the nucleus and overlaid with small ubiquitin-like modifiers (SUMOs) proteins in promyelocytic leukemia (PML)-NBs, while the K104R mutant remains in the cytoplasm and fails to show any colocalization with SUMO proteins [34, 43]
Summary
The human adenovirus genome is transported into the nucleus, where viral gene transcription, viral DNA replication, and virion assembly take place. The E4-ORF3 protein induces sumoylation of multiple cellular proteins involved in a DNA damage response and functions as a SUMO E3 ligase and a SUMO E4 elongase (Fig. 1). Multiple viral oncoproteins have been shown to regulate sumoylation of cellular pocket proteins, such as pRb, p107, and p130 [22, 23], and it will be interesting to study the role of SUMO modification on pocket protein activities.
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