{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,27]],"date-time":"2026-10-27T19:38:08Z","timestamp":1793129888098,"version":"4.5.0"},"reference-count":71,"publisher":"American Society for Microbiology","issue":"10","license":[{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,10,20]],"date-time":"2026-10-20T00:00:00Z","timestamp":1792454400000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/501100012166","name":"National Key Research and Development Program of China","doi-asserted-by":"publisher","award":["2025YFD1800903"],"award-info":[{"award-number":["2025YFD1800903"]}],"id":[{"id":"10.13039\/501100012166","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2026,10,20]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:sec>\n                    <jats:title\/>\n                    <jats:p>\n                      The global outbreak of SARS-CoV-2 has resulted in a renewed focus on coronaviruses with the potential for cross-species transmission and mutation risks. In particular, swine acute diarrhea syndrome coronavirus (SADS-CoV), potentially originating from the intermediate horseshoe bat (\n                      <jats:italic toggle=\"yes\">Rhinolophus affinis<\/jats:italic>\n                      ), is a novel coronavirus that causes acute diarrhea, vomiting, and high mortality in suckling piglets. Innate immunity plays a crucial role in defending the host against invading pathogens. Previous studies have identified several host factors that inhibit SADS-CoV replication through innate immunity; however, research on SADS-CoV remains insufficient compared to that on other coronaviruses. This study demonstrates that Moloney leukemia virus 10 protein (MOV10) exerts anti-SADS-CoV activity via its N-terminal domain in a helicase activity-independent manner. Mechanistic analysis reveals that MOV10 induces translocation of tripartite motif-containing 24 (TRIM24) from the nucleus to the cytoplasm. The cytoplasmically localized TRIM24 binds to MOV10 and TNF receptor-associated factor 3 (TRAF3) to form a ternary complex. Functional studies demonstrate that MOV10 strengthens the interaction between TRIM24 and TRAF3 in a dose-dependent manner and facilitates TRIM24-mediated K63-linked ubiquitination of TRAF3, thereby activating interferon immune responses. Furthermore, we identify the strategies by which SADS-CoV evades innate immunity. The viral N protein inhibits the antiviral effect of MOV10 by disrupting the interaction between MOV10 and TRAF3 and by promoting K48-linked polyubiquitination of TRAF3, leading to TRAF3 degradation via the ubiquitin-proteasome pathway. Collectively, our findings reveal the role of MOV10 in antiviral immunity and how SADS-CoV evades host immune defense.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>IMPORTANCE<\/jats:title>\n                    <jats:p>Moloney leukemia virus 10 protein (MOV10), a DExD-box RNA helicase, is a known component of cytoplasmic RNA processing centers known as P bodies. As an interferon-stimulated gene (ISG), MOV10 exhibits broad-spectrum antiviral activity against multiple viruses, including SARS-CoV-2, HIV, HSV-1, IAV, and PRRSV. Here, we identify a novel helicase-independent antiviral mechanism of MOV10 against SADS-CoV. In this study, we show that MOV10 bridges TRIM24 and TRAF3 and facilitates K63-linked ubiquitination of TRAF3 independent of its helicase activity. This process strongly amplifies downstream interferon antiviral responses and suppresses viral replication. Furthermore, the SADS-CoV N protein efficiently antagonizes MOV10-mediated immune defense by disrupting the MOV10-TRAF3 interaction and inducing K48-linked ubiquitination and proteasomal degradation of TRAF3. Collectively, this study establishes a previously uncharacterized MOV10-TRIM24-TRAF3 antiviral regulatory axis, which offers new mechanistic insights into how coronaviruses evade host immune defenses.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1128\/jvi.01215-26","type":"journal-article","created":{"date-parts":[[2026,9,29]],"date-time":"2026-09-29T13:01:54Z","timestamp":1790686914000},"update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":0,"title":["MOV10 inhibits SADS-CoV replication by enhancing TRIM24-mediated K63-linked TRAF3 ubiquitination, and this inhibition is antagonized by viral N protein"],"prefix":"10.1128","volume":"100","author":[{"given":"Miaomiao","family":"Zeng","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0313jb750","id-type":"ROR","asserted-by":"publisher"}],"name":"State Key Laboratory of Harbin Veterinary Research Institute, Chinese Academy of Agricultural 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