{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:19:24Z","timestamp":1791292764768,"version":"4.1.0"},"reference-count":52,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2007,1,15]],"date-time":"2007-01-15T00:00:00Z","timestamp":1168819200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2007,1,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Understanding the mechanisms of hepatitis C virus (HCV) pathogenesis and persistence has been hampered by the lack of small, convenient animal models. GB virus B (GBV-B) is phylogenetically the closest related virus to HCV. It causes generally acute and occasionally chronic hepatitis in small primates and is used as a surrogate model for HCV. It is not known, however, whether GBV-B has evolved strategies to circumvent host innate defenses similar to those of HCV, a property that may contribute to HCV persistence in vivo. We show here in cultured tamarin hepatocytes that GBV-B NS3\/4A protease, but not a related catalytically inactive mutant, effectively blocks innate intracellular antiviral responses signaled through the RNA helicase, retinoic acid-inducible gene I (RIG-I), an essential sensor molecule that initiates host defenses against many RNA viruses, including HCV. GBV-B NS3\/4A protease specifically cleaves mitochondrial antiviral signaling protein (MAVS; also known as IPS-1\/Cardif\/VISA) and dislodges it from mitochondria, thereby disrupting its function as a RIG-I adaptor and blocking downstream activation of both interferon regulatory factor 3 and nuclear factor kappa B. MAVS cleavage and abrogation of virus-induced interferon responses were also observed in Huh7 cells supporting autonomous replication of subgenomic GBV-B RNAs. Our data indicate that, as in the case of HCV, GBV-B has evolved to utilize its major protease to disrupt RIG-I signaling and impede innate antiviral defenses. These data provide further support for the use of GBV-B infection in small primates as an accurate surrogate model for deciphering virus-host interactions in hepacivirus pathogenesis.<\/jats:p>","DOI":"10.1128\/jvi.02076-06","type":"journal-article","created":{"date-parts":[[2006,11,9]],"date-time":"2006-11-09T01:54:45Z","timestamp":1163037285000},"page":"964-976","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":118,"title":["GB Virus B Disrupts RIG-I Signaling by NS3\/4A-Mediated Cleavage of the Adaptor Protein MAVS"],"prefix":"10.1128","volume":"81","author":[{"given":"Zihong","family":"Chen","sequence":"first","affiliation":[{"name":"Departments of Microbiology &amp; Immunology"},{"name":"Center for Hepatitis Research, Institute for Human Infections &amp; Immunity, University of Texas Medical Branch, Galveston, Texas"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yann","family":"Benureau","sequence":"additional","affiliation":[{"name":"Unite\u0301 de Ge\u0301ne\u0301tique Mole\u0301culaire des Virus Respiratoires, CNRS URA 1966, Institut Pasteur, Paris, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rene","family":"Rijnbrand","sequence":"additional","affiliation":[{"name":"Departments of Microbiology &amp; 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