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Review
. 2016 Sep 20;7(5):e01154-16.
doi: 10.1128/mBio.01154-16.

Adenovirus Early Proteins and Host Sumoylation

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Free PMC article
Review

Adenovirus Early Proteins and Host Sumoylation

Sook-Young Sohn et al. mBio. .
Free PMC article

Abstract

The 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.

Figures

FIG 1
FIG 1
Schematic overview of the interplay between Ad early proteins and the host sumoylation system. (A) E1A directly binds to SUMO E2 enzyme Ubc9 and inhibits SUMO-1 conjugation to pRb. (B) E1B-55K is a SUMO substrate and an E3 ligase for p53 and Sp100A. (C) E4-ORF3 functions as a SUMO E3 ligase and an E4 elongase. E4-ORF3 triggers sumoylation of multiple host proteins and subsequent proteasomal degradation of some of the target proteins. S, SUMO.

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