{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,14]],"date-time":"2026-09-14T23:23:46Z","timestamp":1789428226745,"version":"build-2803163510"},"reference-count":48,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2025,12,24]],"date-time":"2025-12-24T00:00:00Z","timestamp":1766534400000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"},{"start":{"date-parts":[[2025,12,24]],"date-time":"2025-12-24T00:00:00Z","timestamp":1766534400000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"publisher","award":["32300144"],"award-info":[{"award-number":["32300144"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Medical Virology"],"published-print":{"date-parts":[[2026,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n                  <jats:p>\n                    Severe fever with thrombocytopenia syndrome virus (SFTSV) is an emerging pathogenic\n                    <jats:italic>Bunyavirus<\/jats:italic>\n                    with a fatality rate of up to 30%. SFTSV nonstructural protein (NSs) forms viroplasm\u2010like structures in the cytoplasm of infected cells, sequestering antiviral proteins and inhibiting interferon signaling. Nuclear scaffold attachment factor A (SAFA), a novel RNA sensor, can be retained in the cytoplasm by SFTSV nucleoprotein (NP) and facilitates antiviral immune response. Intriguingly, we discovered that SFTSV NSs triggered the nucleocytoplasmic translocation of SAFA. Nevertheless, it remains unclear about the roles of NSs and NP in the recognition of SAFA and downstream signaling molecules. Herein, we demonstrate that after SFTSV infection, both of NP and NSs can interact with SPRY, AAA+ and RGG domains of SAFA in the cytoplasm. NSs can not only capture SAFA for degradation, but also sequester NP\u2010SAFA complex into inclusion bodies (IBs), isolating and degrading SAFA with downstream signaling proteins. With the result that the nuclear translocation of p\u2010IRF3 is prevented and the production of IFN\u03b2 is suppressed. In conclusion, our study reveals a novel immune evasion strategy for SFTSV by sequestering NP\u2010SAFA complex to suppress IFN\u03b2 secretion.\n                  <\/jats:p>","DOI":"10.1002\/jmv.70774","type":"journal-article","created":{"date-parts":[[2025,12,24]],"date-time":"2025-12-24T13:35:52Z","timestamp":1766583352000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["SFTSV NSs Sequesters the Complex of SFTSV NP\u2010SAFA to Suppress SAFA Mediated Immune Response"],"prefix":"10.1002","volume":"98","author":[{"given":"Xin\u2010bo","family":"Huang","sequence":"first","affiliation":[{"name":"Center for Environment and Health in Water Source Area of South\u2010to\u2010North Water Diversion, School of Public Health Hubei University of Medicine  Shiyan Hubei Province P.R. 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