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Article Abstract
African swine fever virus (ASFV) encodes multiple proteins to achieve immune escape, thereby disrupting the host's antiviral defense. This study demonstrates that the ASFV-encoded pE248R protein disrupted the Retinoic Acid-Inducible Gene I (RIG-I) mediated antiviral signaling cascade through dual regulatory mechanisms. Mechanistically, pE248R interacted with the caspase activation and recruitment domains (CARD) of RIG-I, effectively blocking its interaction with the mitochondrial adaptor MAVS. Secondly, pE248R interacted with the coiled-coil domain (CCD) of TRIM25, which impaired TRIM25's multimerization capacity and consequently abolished its ability to catalyze K63-linked ubiquitination of RIG-I. Our research elucidates a novel mechanism by which the ASFV modulates the host innate immune signaling pathway and provides new insights into understanding the immune evasion strategies of ASFV.
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