Ubiquitin and Ubiquitin-Like Pathways in Viral Infection

Dear Colleagues,

The Ubiquitin (Ub) system is a major conserved post-translational process critical in many cellular functions, including regulation of immunity, virus replication, and modulation of virus–host intercations. The function of ubiquitinated proteins depends on the linkage type of the polyubiquitin chain, the length of the chain, and the the presence of ubiquitin-binding domains (UBDs) on specific proteins. Ub conjugation requires an E1-activating enzyme, an E2-conjugase, and an E3-ligase, which transfers Ub to the target protein. Each of these factors can be exploited by viruses to enhance their replication. Since the Ub system is also critical for the activation of antiviral immune signaling, this raises the question regarding the importance of Ub in promoting virus replication versus its role in inducing antiviral responses. To develop antiviral strategies, we need a better understanding  of which factors of the Ub system can be targeted to reduce virus replication and at the same time decrease immune pathology. Extensive research has been done on mechanisms used by viruses that promote the degradation of antiviral host factors through Ub-dependent mechanisms or inhibit innate immune signaling pathways by blocking ubiquitination of host signaling components. Previously unrecognized mechanisms include the presence of ubiquitinated viral proteins or unanchored (not-covalently attached) Ub in infectious virions, which help virus entry and replication. In this Special Issue, we will explore novel aspects of virus antagonism of the immune reponse by targeting the host ubiquitin machinery and how viruses hijack ubiquitin factors to enhance their replication, a mechanism that ultimetely can be targeted to design antiviral strategies.

Dr. Ricardo Rajsbaum
Guest Editor

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