The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
Abstract The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acid...
Gespeichert in:
| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2008-07, Vol.377 (1), p.49-53 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 53 |
|---|---|
| container_issue | 1 |
| container_start_page | 49 |
| container_title | Virology (New York, N.Y.) |
| container_volume | 377 |
| creator | Donahue, John P Vetter, Michael L Mukhtar, Nizar A D'Aquila, Richard T |
| description | Abstract The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161–164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity. |
| doi_str_mv | 10.1016/j.virol.2008.04.017 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2474554</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0042682208002560</els_id><sourcerecordid>20936634</sourcerecordid><originalsourceid>FETCH-LOGICAL-c609t-4dafe87af54e48c53ab24894d38407454d9bb2e84189b70201995672727875413</originalsourceid><addsrcrecordid>eNqFkl9v2yAUxa1p05p2-wSTJp72Zu-CsQ0Pq9RGXVspUi2t6yvC-Dohc6ADJ1K__UgT7d9LxQMgzjlc-N0s-0ChoEDrz-tiZ4MfCwYgCuAF0OZVNqMg6xxKTl9nMwDO8lowdpKdxriGtG8aeJudUMGlZJTNsvZ-heTm9iGn5MEOpG0XLdn4KS1tJA4NxqjDExl8IKvtRjty0d5dXs3La9JZ11u3JNr1pMdl0L2erHfvsjeDHiO-P85n2fevV_fzm3xxd307v1jkpgY55bzXA4pGDxVHLkxV6o5xIXlfCg4Nr3gvu46h4FTIrgEGVMqqblgaoqk4Lc-y80Pu47bbYG_QTUGP6jHYTSpYeW3VvyfOrtTS7xTjKb7iKeDTMSD4n1uMk9rYaHActUO_jaqWjHHaVC8KGciyrst9YnkQmuBjDDj8roaC2iNTa_WMTO2RKeAqIUuuj38_5I_nyCgJvhwEmL5zZzGoaCw6g70NaCbVe_vCBef_-c1onTV6_IFPGNd-G1wipaiKTIH6tu-afdOAAGBVDeUvZly62A</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>20936634</pqid></control><display><type>article</type><title>The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><creator>Donahue, John P ; Vetter, Michael L ; Mukhtar, Nizar A ; D'Aquila, Richard T</creator><creatorcontrib>Donahue, John P ; Vetter, Michael L ; Mukhtar, Nizar A ; D'Aquila, Richard T</creatorcontrib><description>Abstract The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161–164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2008.04.017</identifier><identifier>PMID: 18499212</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Motifs ; Amino Acid Sequence ; APOBEC-3G Deaminase ; APOBEC3G ; Binding Sites - genetics ; Cell Line ; Cullin Proteins - chemistry ; Cullin Proteins - metabolism ; Cytidine Deaminase - antagonists & inhibitors ; Cytidine Deaminase - metabolism ; Elongin ; Genetic Complementation Test ; HIV-1 - genetics ; HIV-1 - pathogenicity ; HIV-1 - physiology ; HIV-1 Vif ; Human immunodeficiency virus 1 ; Humans ; Infectious Disease ; Multiprotein Complexes ; Mutation ; Proteasome Endopeptidase Complex - metabolism ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; vif Gene Products, Human Immunodeficiency Virus - chemistry ; vif Gene Products, Human Immunodeficiency Virus - genetics ; vif Gene Products, Human Immunodeficiency Virus - metabolism ; Vif multimerization ; Vif PPLP motif ; Virulence ; Virus Replication</subject><ispartof>Virology (New York, N.Y.), 2008-07, Vol.377 (1), p.49-53</ispartof><rights>Elsevier Inc.</rights><rights>2008 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c609t-4dafe87af54e48c53ab24894d38407454d9bb2e84189b70201995672727875413</citedby><cites>FETCH-LOGICAL-c609t-4dafe87af54e48c53ab24894d38407454d9bb2e84189b70201995672727875413</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.virol.2008.04.017$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,777,781,882,3537,27905,27906,45976</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18499212$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Donahue, John P</creatorcontrib><creatorcontrib>Vetter, Michael L</creatorcontrib><creatorcontrib>Mukhtar, Nizar A</creatorcontrib><creatorcontrib>D'Aquila, Richard T</creatorcontrib><title>The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>Abstract The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161–164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.</description><subject>Amino Acid Motifs</subject><subject>Amino Acid Sequence</subject><subject>APOBEC-3G Deaminase</subject><subject>APOBEC3G</subject><subject>Binding Sites - genetics</subject><subject>Cell Line</subject><subject>Cullin Proteins - chemistry</subject><subject>Cullin Proteins - metabolism</subject><subject>Cytidine Deaminase - antagonists & inhibitors</subject><subject>Cytidine Deaminase - metabolism</subject><subject>Elongin</subject><subject>Genetic Complementation Test</subject><subject>HIV-1 - genetics</subject><subject>HIV-1 - pathogenicity</subject><subject>HIV-1 - physiology</subject><subject>HIV-1 Vif</subject><subject>Human immunodeficiency virus 1</subject><subject>Humans</subject><subject>Infectious Disease</subject><subject>Multiprotein Complexes</subject><subject>Mutation</subject><subject>Proteasome Endopeptidase Complex - metabolism</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>vif Gene Products, Human Immunodeficiency Virus - chemistry</subject><subject>vif Gene Products, Human Immunodeficiency Virus - genetics</subject><subject>vif Gene Products, Human Immunodeficiency Virus - metabolism</subject><subject>Vif multimerization</subject><subject>Vif PPLP motif</subject><subject>Virulence</subject><subject>Virus Replication</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkl9v2yAUxa1p05p2-wSTJp72Zu-CsQ0Pq9RGXVspUi2t6yvC-Dohc6ADJ1K__UgT7d9LxQMgzjlc-N0s-0ChoEDrz-tiZ4MfCwYgCuAF0OZVNqMg6xxKTl9nMwDO8lowdpKdxriGtG8aeJudUMGlZJTNsvZ-heTm9iGn5MEOpG0XLdn4KS1tJA4NxqjDExl8IKvtRjty0d5dXs3La9JZ11u3JNr1pMdl0L2erHfvsjeDHiO-P85n2fevV_fzm3xxd307v1jkpgY55bzXA4pGDxVHLkxV6o5xIXlfCg4Nr3gvu46h4FTIrgEGVMqqblgaoqk4Lc-y80Pu47bbYG_QTUGP6jHYTSpYeW3VvyfOrtTS7xTjKb7iKeDTMSD4n1uMk9rYaHActUO_jaqWjHHaVC8KGciyrst9YnkQmuBjDDj8roaC2iNTa_WMTO2RKeAqIUuuj38_5I_nyCgJvhwEmL5zZzGoaCw6g70NaCbVe_vCBef_-c1onTV6_IFPGNd-G1wipaiKTIH6tu-afdOAAGBVDeUvZly62A</recordid><startdate>20080720</startdate><enddate>20080720</enddate><creator>Donahue, John P</creator><creator>Vetter, Michael L</creator><creator>Mukhtar, Nizar A</creator><creator>D'Aquila, Richard T</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20080720</creationdate><title>The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation</title><author>Donahue, John P ; Vetter, Michael L ; Mukhtar, Nizar A ; D'Aquila, Richard T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c609t-4dafe87af54e48c53ab24894d38407454d9bb2e84189b70201995672727875413</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Motifs</topic><topic>Amino Acid Sequence</topic><topic>APOBEC-3G Deaminase</topic><topic>APOBEC3G</topic><topic>Binding Sites - genetics</topic><topic>Cell Line</topic><topic>Cullin Proteins - chemistry</topic><topic>Cullin Proteins - metabolism</topic><topic>Cytidine Deaminase - antagonists & inhibitors</topic><topic>Cytidine Deaminase - metabolism</topic><topic>Elongin</topic><topic>Genetic Complementation Test</topic><topic>HIV-1 - genetics</topic><topic>HIV-1 - pathogenicity</topic><topic>HIV-1 - physiology</topic><topic>HIV-1 Vif</topic><topic>Human immunodeficiency virus 1</topic><topic>Humans</topic><topic>Infectious Disease</topic><topic>Multiprotein Complexes</topic><topic>Mutation</topic><topic>Proteasome Endopeptidase Complex - metabolism</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><topic>vif Gene Products, Human Immunodeficiency Virus - chemistry</topic><topic>vif Gene Products, Human Immunodeficiency Virus - genetics</topic><topic>vif Gene Products, Human Immunodeficiency Virus - metabolism</topic><topic>Vif multimerization</topic><topic>Vif PPLP motif</topic><topic>Virulence</topic><topic>Virus Replication</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Donahue, John P</creatorcontrib><creatorcontrib>Vetter, Michael L</creatorcontrib><creatorcontrib>Mukhtar, Nizar A</creatorcontrib><creatorcontrib>D'Aquila, Richard T</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Virology (New York, N.Y.)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Donahue, John P</au><au>Vetter, Michael L</au><au>Mukhtar, Nizar A</au><au>D'Aquila, Richard T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation</atitle><jtitle>Virology (New York, N.Y.)</jtitle><addtitle>Virology</addtitle><date>2008-07-20</date><risdate>2008</risdate><volume>377</volume><issue>1</issue><spage>49</spage><epage>53</epage><pages>49-53</pages><issn>0042-6822</issn><eissn>1096-0341</eissn><abstract>Abstract The HIV-1 virion infectivity factor (Vif) is required during viral replication to inactivate the host cell anti-viral factor, APOBEC3G (A3G). Vif binds A3G and a Cullin5-ElonginBC E3 ubiquitin ligase complex which results in the proteasomal degradation of A3G. The Vif PPLP motif (amino acids 161–164) is essential for normal Vif function because mutations in this motif reduce the infectivity of virions produced in T-cells. In this report, we demonstrate that mutation of the Vif PPLP motif reduces Vif binding to A3G without affecting its interaction with ElonginC and Cullin5. We demonstrate that the failure of the Vif mutant to bind A3G resulted in A3G incorporation into assembling virions with loss of viral infectivity.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>18499212</pmid><doi>10.1016/j.virol.2008.04.017</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0042-6822 |
| ispartof | Virology (New York, N.Y.), 2008-07, Vol.377 (1), p.49-53 |
| issn | 0042-6822 1096-0341 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_2474554 |
| source | MEDLINE; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Amino Acid Motifs Amino Acid Sequence APOBEC-3G Deaminase APOBEC3G Binding Sites - genetics Cell Line Cullin Proteins - chemistry Cullin Proteins - metabolism Cytidine Deaminase - antagonists & inhibitors Cytidine Deaminase - metabolism Elongin Genetic Complementation Test HIV-1 - genetics HIV-1 - pathogenicity HIV-1 - physiology HIV-1 Vif Human immunodeficiency virus 1 Humans Infectious Disease Multiprotein Complexes Mutation Proteasome Endopeptidase Complex - metabolism Transcription Factors - chemistry Transcription Factors - metabolism vif Gene Products, Human Immunodeficiency Virus - chemistry vif Gene Products, Human Immunodeficiency Virus - genetics vif Gene Products, Human Immunodeficiency Virus - metabolism Vif multimerization Vif PPLP motif Virulence Virus Replication |
| title | The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T09%3A32%3A47IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20HIV-1%20Vif%20PPLP%20motif%20is%20necessary%20for%20human%20APOBEC3G%20binding%20and%20degradation&rft.jtitle=Virology%20(New%20York,%20N.Y.)&rft.au=Donahue,%20John%20P&rft.date=2008-07-20&rft.volume=377&rft.issue=1&rft.spage=49&rft.epage=53&rft.pages=49-53&rft.issn=0042-6822&rft.eissn=1096-0341&rft_id=info:doi/10.1016/j.virol.2008.04.017&rft_dat=%3Cproquest_pubme%3E20936634%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=20936634&rft_id=info:pmid/18499212&rft_els_id=S0042682208002560&rfr_iscdi=true |