Abstract
Ubiquitination is a prominent posttranslational modification, in which the ubiquitin moiety is covalently attached to a target protein to influence protein stability, interaction partner and biological function. All seven lysine residues of ubiquitin, along with the N-terminal methionine, can each serve as a substrate for further ubiquitination, which effectuates a diverse combination of mono- or poly-ubiquitinated proteins with linear or branched ubiquitin chains. The intricately composed ubiquitin codes are then recognized by a large variety of ubiquitin binding domain (UBD)-containing proteins to participate in the regulation of various pathways to modulate the cell behavior. Viruses, as obligate parasites, involve many aspects of the cell pathways to overcome host defenses and subjugate cellular machineries. In the virus-host interactions, both the virus and the host tap into the rich source of versatile ubiquitination code in order to compete, combat, and co-evolve. Here, we review the recent literature to discuss the role of ubiquitin system as the infection progresses in virus life cycle and the importance of ubiquitin specificity in the regulation of virus-host relation.
Highlights
Ubiquitination is a reversible post-translational modification (PTM) that regulates protein functions in almost every aspect of a cell’s life
T cell immunoglobulin and mucin (TIM)-1 serves as a Dengue virus receptor to facilitate the entry via endocytosis, and ubiquitination at K338 and K346 of TIM-1 is required for an effective virus uptake [47]
It has been reported that an E2 conjugating enzyme CIN85 associated with Cbl interacts with an HSV-1 immediate early protein ICP0 [54], which is a viral really interesting new gene (RING)-type E3 ubiquitin ligase by itself [55], it is not yet clear whether Cbl activity is controlled by ICP0 for a selective viral enhancement
Summary
Ubiquitination is a reversible post-translational modification (PTM) that regulates protein functions in almost every aspect of a cell’s life. Viruses are obligate parasites that closely interact with the host to subjugate many cellular machineries to achieve viral replication. They have evolved to manipulate and take advantage of the ubiquitin system so as to redirect the cellular pathways in their own favor. Host cells adopt special code of ubiquitination to mount immune responses against viral infection. It is fascinating to witness the unveiling of ubiquitin regulation in cell anti-viral defenses as well as viral counteractions in recent years. Through delineating the complex ubiquitin code on both the virus and host factors, we hope to understand the significance of ubiquitination specificity in virus-host interaction and to search for potential targets useful for prophylactic and therapeutic treatment of viral diseases
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