Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection
Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication. The AIDS virus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host's antiviral defence by hija...
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| Published in | Nature (London) Vol. 481; no. 7381; pp. 371 - 375 |
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| Main Authors | , , , , , , , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing Group
19.01.2012
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| Subjects | |
| Online Access | Get full text |
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| Abstract | Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication. The AIDS virus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host's antiviral defence by hijacking a ubiquitin ligase complex, containing CUL5, ELOC, ELOB and a RING-box protein, and targeting APOBEC3G for degradation. Here we reveal, using an affinity tag/purification mass spectrometry approach, that Vif additionally recruits the transcription cofactor CBF-β to this ubiquitin ligase complex. CBF-β, which normally functions in concert with RUNX DNA binding proteins, allows the reconstitution of a recombinant six-protein assembly that elicits specific polyubiquitination activity with APOBEC3G, but not the related deaminase APOBEC3A. Using RNA knockdown and genetic complementation studies, we also demonstrate that CBF-β is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity. Finally, simian immunodeficiency virus (SIV) Vif also binds to and requires CBF-β to degrade rhesus macaque APOBEC3G, indicating functional conservation. Methods of disrupting the CBF-β-Vif interaction might enable HIV-1 restriction and provide a supplement to current antiviral therapies that primarily target viral proteins. |
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| AbstractList | Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication
1
-
3
. The AIDS virus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host’s antiviral defence by hijacking a ubiquitin ligase complex, containing CUL5, ELOC, ELOB and a RING-box protein, and targeting APOBEC3G for degradation
4
-
10
. Here we reveal, using an affinity tag/purification mass spectrometry approach, that Vif additionally recruits the transcription cofactor CBF-β to this ubiquitin ligase complex. CBF-β, which normally functions in concert with RUNX DNA binding proteins, allows the reconstitution of a recombinant six-protein assembly that elicits specific polyubiquitination activity with APOBEC3G, but not the related deaminase APOBEC3A. Using RNA knockdown and genetic complementation studies, we also demonstrate that CBF-β is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity. Finally, simian immunodeficiency virus (SIV) Vif also binds to and requires CBF-β to degrade rhesus macaque APOBEC3G, indicating functional conservation. Methods of disrupting the CBF-β–Vif interaction might enable HIV-1 restriction and provide a supplement to current antiviral therapies that primarily target viral proteins. Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication (1-3). The AIDS virus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host's antiviral defence by hijacking a ubiquitin ligase complex, containing CUL5, ELOC, ELOB and a RING-box protein, and targeting APOBEC3G for degradation (4-10). Here we reveal, using an affinity tag/purification mass spectrometry approach, that Vif additionally recruits the transcription cofactor CBF-β to this ubiquitin ligase complex. CBF-β, which normally functions in concert with RUNX DNA binding proteins, allows the reconstitution of a recombinant six-protein assembly that elicits specific polyubiquitination activity with APOBEC3G, but not the related deaminase APOBEC3A. Using RNA knockdown and genetic complementation studies, we also demonstrate that CBF-b is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity. Finally, simian immunodeficiency virus (SIV) Vif also binds to and requires CBF-β to degrade rhesus macaque APOBEC3G, indicating functional conservation. Methods of disrupting the CBF-β-Vif interaction might enable HIV-1 restriction and provide a supplement to current antiviral therapies that primarily target viral proteins. Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication. The AIDS virus, human immunodeficiency virus type 1 (HIV-1), produces the accessory factor Vif, which counteracts the host's antiviral defence by hijacking a ubiquitin ligase complex, containing CUL5, ELOC, ELOB and a RING-box protein, and targeting APOBEC3G for degradation. Here we reveal, using an affinity tag/purification mass spectrometry approach, that Vif additionally recruits the transcription cofactor CBF-β to this ubiquitin ligase complex. CBF-β, which normally functions in concert with RUNX DNA binding proteins, allows the reconstitution of a recombinant six-protein assembly that elicits specific polyubiquitination activity with APOBEC3G, but not the related deaminase APOBEC3A. Using RNA knockdown and genetic complementation studies, we also demonstrate that CBF-β is required for Vif-mediated degradation of APOBEC3G and therefore for preserving HIV-1 infectivity. Finally, simian immunodeficiency virus (SIV) Vif also binds to and requires CBF-β to degrade rhesus macaque APOBEC3G, indicating functional conservation. Methods of disrupting the CBF-β-Vif interaction might enable HIV-1 restriction and provide a supplement to current antiviral therapies that primarily target viral proteins. |
| Audience | Academic |
| Author | SALI, Andrej JÄGER, Stefanie FRANKS-SKIBA, Kathy KANE, Joshua KWON, Eunju BURLINGAME, Alma ANDERSON, Brett D CIMERMANCIC, Peter SHINDO, Keisuke LARUE, Rebecca S MAHON, Cathal DONG YOUNG KIM MING LI HARRIS, Reuben S GROSS, John D HULTQUIST, Judd F CRAIK, Charles S KROGAN, Nevan J YEN, Linda STANLEY, David |
| AuthorAffiliation | 5 Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158, USA 7 J. David Gladstone Institutes, San Francisco, California 94158, USA 1 Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, USA 3 Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA 2 California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, USA 4 Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, USA 6 HPC (Host Pathogen Circuitry) Group, University of California-San Francisco, San Francisco, California 94158, USA |
| AuthorAffiliation_xml | – name: 5 Department of Bioengineering and Therapeutic Sciences, University of California, San Francisco, California 94158, USA – name: 2 California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, USA – name: 3 Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, USA – name: 7 J. David Gladstone Institutes, San Francisco, California 94158, USA – name: 4 Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, USA – name: 6 HPC (Host Pathogen Circuitry) Group, University of California-San Francisco, San Francisco, California 94158, USA – name: 1 Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, USA |
| Author_xml | – sequence: 1 givenname: Stefanie surname: JÄGER fullname: JÄGER, Stefanie organization: Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, United States – sequence: 2 surname: DONG YOUNG KIM fullname: DONG YOUNG KIM organization: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States – sequence: 3 givenname: Cathal surname: MAHON fullname: MAHON, Cathal organization: Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, United States – sequence: 4 givenname: Joshua surname: KANE fullname: KANE, Joshua organization: Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, United States – sequence: 5 givenname: Kathy surname: FRANKS-SKIBA fullname: FRANKS-SKIBA, Kathy organization: Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, United States – sequence: 6 givenname: Peter surname: CIMERMANCIC fullname: CIMERMANCIC, Peter organization: California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, United States – sequence: 7 givenname: Alma surname: BURLINGAME fullname: BURLINGAME, Alma organization: California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, United States – sequence: 8 givenname: Andrej surname: SALI fullname: SALI, Andrej organization: California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, United States – sequence: 9 givenname: Charles S surname: CRAIK fullname: CRAIK, Charles S organization: California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, United States – sequence: 10 givenname: Reuben S surname: HARRIS fullname: HARRIS, Reuben S organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 11 givenname: John D surname: GROSS fullname: GROSS, John D organization: California Institute for Quantitative Biosciences, QB3, San Francisco, California, California 94158, United States – sequence: 12 givenname: Nevan J surname: KROGAN fullname: KROGAN, Nevan J organization: Department of Cellular and Molecular Pharmacology, University of California-San Francisco, San Francisco, California 94158, United States – sequence: 13 givenname: Judd F surname: HULTQUIST fullname: HULTQUIST, Judd F organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 14 givenname: Keisuke surname: SHINDO fullname: SHINDO, Keisuke organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 15 givenname: Rebecca S surname: LARUE fullname: LARUE, Rebecca S organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 16 givenname: Eunju surname: KWON fullname: KWON, Eunju organization: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States – sequence: 17 surname: MING LI fullname: MING LI organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 18 givenname: Brett D surname: ANDERSON fullname: ANDERSON, Brett D organization: Department of Biochemistry, Molecular Biology and Biophysics, Institute for Molecular Virology, Center for Genome Engineering, University of Minnesota, Minneapolis, Minnesota 55455, United States – sequence: 19 givenname: Linda surname: YEN fullname: YEN, Linda organization: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States – sequence: 20 givenname: David surname: STANLEY fullname: STANLEY, David organization: Department of Pharmaceutical Chemistry, University of California, San Francisco, California 94158, United States |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=25380628$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/22190037$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1128/JVI.00767-08 10.1016/j.chom.2008.04.008 10.1038/nsmb.1744 10.1016/j.ymeth.2010.08.007 10.1016/j.cub.2003.10.034 10.1101/gad.1249904 10.1074/jbc.M313093200 10.1074/jbc.M609659200 10.1128/JVI.00377-08 10.1093/emboj/19.1.94 10.1093/nar/gkq174 10.1128/JVI.05238-11 10.1016/j.molcel.2009.01.011 10.1016/j.cell.2005.09.033 10.1016/S1097-2765(03)00353-8 10.1126/science.1089591 10.1042/bj20040198 10.1016/j.molcel.2010.02.025 10.1038/nature00939 10.1016/j.cell.2007.05.027 10.1111/j.1365-2567.2010.03381.x 10.1016/j.molcel.2004.12.001 10.1017/S1462399409001343 10.1128/JVI.01089-09 10.1038/nm945 10.1038/nature10719 10.1016/j.molcel.2008.08.021 10.1101/gad.1252404 |
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| References | 18541215 - Cell Host Microbe. 2008 Jun 12;3(6):388-98 22245926 - Nat Rev Microbiol. 2012 Feb;10(2):81 15601820 - Genes Dev. 2004 Dec 15;18(24):3055-65 22190034 - Nature. 2012 Jan 19;481(7381):365-70 19250909 - Mol Cell. 2009 Feb 27;33(4):483-95 16360039 - Cell. 2005 Dec 16;123(6):1107-20 18562529 - J Virol. 2008 Sep;82(17):8656-63 14672928 - J Biol Chem. 2004 Feb 27;279(9):7792-8 19587057 - J Virol. 2009 Sep;83(18):9474-85 14564014 - Science. 2003 Nov 7;302(5647):1056-60 15610729 - Mol Cell. 2004 Dec 22;16(6):849-59 14528300 - Nat Med. 2003 Nov;9(11):1404-7 21091910 - Immunology. 2011 Feb;132(2):157-64 17426036 - J Biol Chem. 2007 Jun 15;282(24):17375-86 12167863 - Nature. 2002 Aug 8;418(6898):646-50 20708689 - Methods. 2011 Jan;53(1):13-9 14998368 - Biochem J. 2004 May 1;379(Pt 3):513-25 20308164 - Nucleic Acids Res. 2010 Jul;38(13):4274-84 14614829 - Curr Biol. 2003 Nov 11;13(22):2009-13 20347421 - Mol Cell. 2010 Mar 26;37(6):784-96 20062055 - Nat Struct Mol Biol. 2010 Feb;17(2):222-9 18596088 - J Virol. 2008 Sep;82(18):9265-72 14527406 - Mol Cell. 2003 Sep;12(3):591-601 15574592 - Genes Dev. 2004 Dec 1;18(23):2861-6 18851830 - Mol Cell. 2008 Oct 10;32(1):21-31 21835787 - J Virol. 2011 Nov;85(21):11220-34 20096141 - Expert Rev Mol Med. 2010;12:e4 17632060 - Cell. 2007 Jul 13;130(1):127-39 10619848 - EMBO J. 2000 Jan 4;19(1):94-102 MC Rodrigo-Brenni (BFnature10693_CR24) 2007; 130 S Jäger (BFnature10693_CR14) 2011; 53 JS Albin (BFnature10693_CR3) 2010; 12 K Stopak (BFnature10693_CR10) 2003; 12 FA Koning (BFnature10693_CR26) 2009; 83 AM Sheehy (BFnature10693_CR7) 2002; 418 HT Kim (BFnature10693_CR20) 2007; 282 MD Petroski (BFnature10693_CR19) 2005; 123 AM Sheehy (BFnature10693_CR8) 2003; 9 DT Huang (BFnature10693_CR17) 2009; 33 JL DeHart (BFnature10693_CR21) 2008; 82 SG Conticello (BFnature10693_CR9) 2003; 13 BJ Stanley (BFnature10693_CR13) 2008; 82 A Saha (BFnature10693_CR28) 2008; 32 SP Goff (BFnature10693_CR1) 2004; 16 JF Hultquist (BFnature10693_CR23) 2011; 85 A Mehle (BFnature10693_CR6) 2004; 279 K Wu (BFnature10693_CR25) 2010; 37 A Mehle (BFnature10693_CR5) 2004; 18 T Kamura (BFnature10693_CR16) 2004; 18 MD Stenglein (BFnature10693_CR22) 2010; 17 EW Refsland (BFnature10693_CR27) 2010; 38 WF Wong (BFnature10693_CR18) 2011; 132 BFnature10693_CR15 LA Passmore (BFnature10693_CR11) 2004; 379 X Yu (BFnature10693_CR4) 2003; 302 JS Thrower (BFnature10693_CR12) 2000; 19 MH Malim (BFnature10693_CR2) 2008; 3 |
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| Snippet | Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication. The AIDS... Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication (1-3). The AIDS... Restriction factors, such as the retroviral complementary DNA deaminase APOBEC3G, are cellular proteins that dominantly block virus replication 1 - 3 . The... |
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| SubjectTerms | Affinity Labels Animals APOBEC-3G Deaminase Biological and medical sciences Core Binding Factor beta Subunit - metabolism Cullin Proteins - metabolism Cytidine Deaminase - metabolism DNA binding proteins Fundamental and applied biological sciences. Psychology Gene Knockdown Techniques Gene Products, vif - metabolism Genetic aspects Genetic Complementation Test Health aspects HEK293 Cells HIV infection HIV Infections - metabolism HIV Infections - virology HIV-1 - physiology Host-Pathogen Interactions Humans Jurkat Cells Macaca mulatta - metabolism Macaca mulatta - virology Mass Spectrometry Microbiology Models, Biological Physiological aspects Protein Binding Proteolysis Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains Risk factors Simian Immunodeficiency Virus - metabolism Ubiquitin-proteasome system Ubiquitin-Protein Ligases - chemistry Ubiquitin-Protein Ligases - metabolism Ubiquitination vif Gene Products, Human Immunodeficiency Virus - metabolism Virology Virus Replication |
| Title | Vif hijacks CBF-β to degrade APOBEC3G and promote HIV-1 infection |
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