查看文章

Understanding interactions between the host and SARS-CoV-2 is essential for developing effective vaccines and therapeutics. Here, we report that SARS-CoV-2 usurps the host ubiquitin system to polyubiquitinate accessory protein ORF7a at Lys119. The ORF7a polyubiquitination is primarily formed by K63-linked ubiquitin chains. Such ubiquitination enhances ORF7a to inhibit type-I interferon (IFN-I) signaling via STAT2 phosphorylation. Protein ubiquitination is a posttranslational modification that regulates many aspects of eukaryotic biology, including viral infection. 1 This modification plays a key role in modulating the immune response, 2 and viruses have evolved to evade immune responses by subverting the host ubiquitin system. 3, 4 To date, little is known about whether SARS-CoV-2 utilizes the ubiquitin system to antagonize the innate antiviral response. Coronavirus accessory proteins are well documented …