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By using immunoprecipitation coupled with mass spectroscopy, we observed that the E3 ubiquitin ligase TRIM21 interacted with the SARS\u2010CoV\u20102 nucleocapsid (N) protein and ubiquitinated it at Lys\n                    <jats:sup>375<\/jats:sup>\n                    . Upon determining the topology of the TRIM21\u2010mediated polyubiquitination chain on N protein, we then found that polyubiquitination led to tagging of the N protein for degradation by the host cell proteasome. Furthermore, TRIM21 also ubiquitinated the N proteins of SARS\u2010CoV\u20102 variants of concern, including\n                    <jats:italic>Alpha, Beta, Gamma, Delta<\/jats:italic>\n                    , and\n                    <jats:italic>Omicron<\/jats:italic>\n                    together with SARS\u2010CoV and MERS\u2010CoV variants. Herein, we propose that ubiquitylation and degradation of the SARS\u2010CoV\u20102 N protein inhibited SARS\u2010CoV\u20102 viral particle assembly, by which it probably involved in preventing cytokine storm. Eventually, our study has fully revealed the association between the host innate immune system and SARS\u2010CoV\u20102 N protein, which may aid in developing novel SARS\u2010CoV\u20102 treatment strategies.\n                  <\/jats:p>","DOI":"10.1002\/jmv.28719","type":"journal-article","created":{"date-parts":[[2023,4,13]],"date-time":"2023-04-13T22:50:31Z","timestamp":1681426231000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":26,"title":["TRIM21 promotes ubiquitination of SARS\u2010CoV\u20102 nucleocapsid protein to regulate innate immunity"],"prefix":"10.1002","volume":"95","author":[{"given":"Shenglan","family":"Mao","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine Chongqing Medical University Chongqing China"},{"name":"The Key Laboratory of Molecular Biology of Infectious Diseases designated by the Chinese Ministry of Education Chongqing Medical University  Chongqing 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