Ubiquitination: A Double-Edged Mechanism in Coronavirus Infections.

The emergence of SARS-CoV-2 in late 2019 had a profound impact on public health, leading to the global COVID-19 pandemic. This viral outbreak has significantly heightened interest in coronaviruses, accelerating research into their pathogenesis. Ubiquitination, a common Posttranslational protein modification, plays a crucial role in processes such as protein localization, metabolism, and degradation. During coronavirus invasion and disease progression, complex interactions involving ubiquitination are at play. On one hand, the host utilizes ubiquitination to activate innate immune signaling pathway or degrade crucial viral proteins via the ubiquitin-proteasome pathway, thereby inhibiting viral replication. On the other hand, coronaviruses manipulate ubiquitination to suppress the activation of key antiviral molecules or promote their degradation. Thus, both the host and virus leverage ubiquitination to their advantage. Thus, investigating the role of ubiquitination in coronavirus infection provides crucial insights into viral infection mechanisms and pathogenesis, potentially facilitating the development of novel antiviral drugs, particularly those targeting ubiquitination regulation, such as PROTAC. This paper offers a comprehensive examination of the regulatory function of ubiquitination in coronavirus infection, with the potential to advance research in the field and open new avenues for the effective control of coronaviruses, especially SARS-CoV-2.