{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T20:01:37Z","timestamp":1791144097763,"version":"4.1.0"},"reference-count":62,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2014,10,15]],"date-time":"2014-10-15T00:00:00Z","timestamp":1413331200000},"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":[[2014,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>Viral infectivity factor (Vif) is required for lentivirus fitness and pathogenicity, except in equine infectious anemia virus (EIAV). Vif enhances viral infectivity by a Cullin5-Elongin B\/C E3 complex to inactivate the host restriction factor APOBEC3. Core-binding factor subunit beta (CBF-\u03b2) is a cell factor that was recently shown to be important for the primate lentiviral Vif function. Non-primate lentiviral Vif also degrades APOBEC3 through the proteasome pathway. However, it is unclear whether CBF-\u03b2 is required for the non-primate lentiviral Vif function. In this study, we demonstrated that the Vifs of non-primate lentiviruses, including feline immunodeficiency virus (FIV), bovine immunodeficiency virus (BIV), caprine arthritis encephalitis virus (CAEV), and maedi-visna virus (MVV), do not interact with CBF-\u03b2. In addition, CBF-\u03b2 did not promote the stability of FIV, BIV, CAEV, and MVV Vifs. Furthermore, CBF-\u03b2 silencing or overexpression did not affect non-primate lentiviral Vif-mediated APOBEC3 degradation. Our results suggest that non-primate lentiviral Vif induces APOBEC3 degradation through a different mechanism than primate lentiviral Vif.<\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            The APOBEC3 protein family members are host restriction factors that block retrovirus replication. Vif, an accessory protein of lentivirus, degrades APOBEC3 to rescue viral infectivity by forming Cullin5-Elongin B\/C-based E3 complex. CBF-\u03b2 was proved to be a novel regulator of primate lentiviral Vif function. In this study, we found that CBF-\u03b2 knockdown or overexpression did not affect FIV Vif's function, which induced polyubiquitination and degradation of APOBEC3 by recruiting the E3 complex in a manner similar to that of HIV-1 Vif. We also showed that other non-primate lentiviral Vifs did not require CBF-\u03b2 to degrade APOBEC3. CBF-\u03b2 did not interact with non-primate lentiviral Vifs or promote their stability. These results suggest that a different mechanism exists for the Vif-APOBEC interaction and that non-primates are not suitable animal models for exploring pharmacological interventions that disrupt Vif\u2013CBF-\u03b2 interaction.\n          <\/jats:p>","DOI":"10.1128\/jvi.01924-14","type":"journal-article","created":{"date-parts":[[2014,8,14]],"date-time":"2014-08-14T07:06:05Z","timestamp":1407999965000},"page":"12112-12122","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":25,"title":["Core-Binding Factor Subunit Beta Is Not Required for Non-Primate Lentiviral Vif-Mediated APOBEC3 Degradation"],"prefix":"10.1128","volume":"88","author":[{"given":"Youwei","family":"Ai","sequence":"first","affiliation":[{"name":"State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Harbin, China"},{"name":"College of Wildlife Resources, Northeast Forestry 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