The E3 ligase TRIM22 restricts SARS-CoV-2 replication by promoting proteasomal degradation of NSP8

The E3 ligase TRIM22 restricts SARS-CoV-2 replication by promoting proteasomal degradation of NSP8

February 2024 | Lujie Fan, Yuzheng Zhou, Xiafei Wei, Wei Feng, Huimin Guo, Yunfei Li, Xiang Gao, Jian Zhou, Yanling Wen, Yezi Wu, Xiaotong Shen, Lei Liu, Gang Xu, Zheng Zhang
The E3 ligase TRIM22 restricts SARS-CoV-2 replication by promoting proteasomal degradation of NSP8. This study reveals that TRIM22, an interferon-stimulated gene, interacts with NSP8 and ubiquitinates it at Lys97 via K48-type ubiquitination, leading to its degradation. TRIM22 overexpression significantly reduces viral RNA and protein levels, while its knockdown enhances viral replication. NSP8, a key component of the RNA-dependent RNA polymerase complex, is found to be unstable and degraded by the proteasome. TRIM22's E3 ubiquitin ligase activity plays a crucial role in inhibiting SARS-CoV-2 replication by targeting NSP8 for degradation. The study also shows that TRIM22-mediated degradation of NSP8 is conserved across various coronaviruses, suggesting its potential as a broad-spectrum antiviral target. These findings provide new insights into the role of host factors in viral replication and highlight TRIM22 as a promising therapeutic target for developing antiviral drugs against SARS-CoV-2 and related coronaviruses. The results emphasize the importance of understanding host-virus interactions in the context of viral infections and offer a novel approach for combating viral diseases.The E3 ligase TRIM22 restricts SARS-CoV-2 replication by promoting proteasomal degradation of NSP8. This study reveals that TRIM22, an interferon-stimulated gene, interacts with NSP8 and ubiquitinates it at Lys97 via K48-type ubiquitination, leading to its degradation. TRIM22 overexpression significantly reduces viral RNA and protein levels, while its knockdown enhances viral replication. NSP8, a key component of the RNA-dependent RNA polymerase complex, is found to be unstable and degraded by the proteasome. TRIM22's E3 ubiquitin ligase activity plays a crucial role in inhibiting SARS-CoV-2 replication by targeting NSP8 for degradation. The study also shows that TRIM22-mediated degradation of NSP8 is conserved across various coronaviruses, suggesting its potential as a broad-spectrum antiviral target. These findings provide new insights into the role of host factors in viral replication and highlight TRIM22 as a promising therapeutic target for developing antiviral drugs against SARS-CoV-2 and related coronaviruses. The results emphasize the importance of understanding host-virus interactions in the context of viral infections and offer a novel approach for combating viral diseases.
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