Vif hijacks CBF-b to degrade APOBEC3G and promote HIV-1 infection英文学习资料.PDFVIP

LETTER doi:10.1038/nature10693 Vif hijacks CBF-b to degrade APOBEC3G and promote HIV-1 infection ¨ 1,2 3 4 4 4 3 4 Stefanie Jager *, Dong Young Kim *, Judd F. Hultquist *, Keisuke Shindo , Rebecca S. LaRue , Eunju Kwon , Ming Li , 4 3 3 1,2,3 1,2 1,2 2,5 Brett D. Anderson , Linda Yen , David Stanley , Cathal Mahon , Joshua Kane , Kathy Franks-Skiba , Peter Cimermancic , 2,3 2,3,5,6 2,3 4 2,3,6 1,2,6,7 Alma Burlingame , Andrej Sali , Charles S. Craik , Reuben S. Harris , John D. Gross Nevan J. Krogan Restriction factors, such as the retroviral complementary DNA (ELOBC) has been reported13, the architecture of the full-length Vif in deaminase APOBEC3G, are cellular proteins that dominantly block complex with host factors has remained elusive, in part because Vif virus replication1–3. The AIDS virus, human immunodeficiency virus complexes have poor solubility and activity. We therefore reasoned type 1 (HIV-1), produces the accessory factor Vif, which counteracts that Vif may bind an additional host factor and that such a factor may the host’s antiviral defence by hijacking a ubiquitin ligase complex, render it more tractable in vitro. containing CUL5, ELOC, ELOB and a RING-box protein, and