Efficient Vpu-Mediated Tetherin Antagonism by an HIV-1 Group O Strain
Identifieur interne : 000617 ( Main/Exploration ); précédent : 000616; suivant : 000618Efficient Vpu-Mediated Tetherin Antagonism by an HIV-1 Group O Strain
Auteurs : Katharina Mack [Allemagne] ; Kathrin Starz [Allemagne] ; Daniel Sauter [Allemagne] ; Simon Langer [Allemagne] ; Frederic Bibollet-Ruche [États-Unis] ; Gerald Learn [États-Unis] ; Christina Stürzel [Allemagne] ; Marie Leoz [France] ; Jean-Christophe Plantier [France] ; Matthias Geyer ; Beatrice Hahn [États-Unis] ; Frank Kirchhoff [Allemagne]Source :
- Journal of Virology [ 0022-538X ] ; 2017-02-28.
English descriptors
- mix :
Abstract
Simian immunodeficiency viruses (SIVs) use their Nef proteins to counteract the restriction factor tetherin. However, a deletion in human tetherin prevents antagonism by the Nef proteins of SIVcpz and SIVgor, which represent the ape precursors of human immunodeficiency virus type 1 (HIV-1). To promote virus release from infected cells, pandemic HIV-1 group M strains evolved Vpu as a tetherin antagonist, while the Nef protein of less widespread HIV-1 group O strains acquired the ability to target a region adjacent to this deletion. In this study, we identified an unusual HIV-1 group O strain (RBF206) that evolved Vpu as an effective antagonist of human tetherin. While both RBF206 Vpu and Nef exert anti-tetherin activity in transient-transfection assays, mainly Vpu promotes RBF206 release in infected CD4+ T cells. Although mutations distinct from the adaptive changes observed in group M Vpus (M-Vpus) were critical for the acquisition of its anti-tetherin activity, RBF206 O-Vpu potently suppresses NF-κB activation and reduces CD4 cell surface expression. Interestingly, RBF206 Vpu counteracts tetherin in a largely species-independent manner, degrading both the long and short isoforms of human tetherin. Downmodulation of CD4, but not counteraction of tetherin, by RBF206 Vpu was dependent on the cellular ubiquitin ligase machinery. Our data present the first example of an HIV-1 group O Vpu that efficiently antagonizes human tetherin and suggest that counteraction by O-Nefs may be suboptimal.
Url:
DOI: 10.1128/JVI.02177-16
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream Hal, to step Corpus: 000183
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Le document en format XML
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<author><name sortKey="Sturzel, Christina" sort="Sturzel, Christina" uniqKey="Sturzel C" first="Christina" last="Stürzel">Christina Stürzel</name>
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<author><name sortKey="Leoz, Marie" sort="Leoz, Marie" uniqKey="Leoz M" first="Marie" last="Leoz">Marie Leoz</name>
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<author><name sortKey="Geyer, Matthias" sort="Geyer, Matthias" uniqKey="Geyer M" first="Matthias" last="Geyer">Matthias Geyer</name>
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<author><name sortKey="Hahn, Beatrice" sort="Hahn, Beatrice" uniqKey="Hahn B" first="Beatrice" last="Hahn">Beatrice Hahn</name>
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</address>
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<country>États-Unis</country>
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<author><name sortKey="Kirchhoff, Frank" sort="Kirchhoff, Frank" uniqKey="Kirchhoff F" first="Frank" last="Kirchhoff">Frank Kirchhoff</name>
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<idno type="DOI">10.1128/JVI.02177-16</idno>
<series><title level="j">Journal of Virology</title>
<idno type="ISSN">0022-538X</idno>
<imprint><date type="datePub">2017-02-28</date>
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<profileDesc><textClass><keywords scheme="mix" xml:lang="en"><term>HIV-1 group O</term>
<term>Vpu</term>
<term>antagonism</term>
<term>tetherin</term>
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<front><div type="abstract" xml:lang="en"> <p>Simian immunodeficiency viruses (SIVs) use their Nef proteins to counteract the restriction factor tetherin. However, a deletion in human tetherin prevents antagonism by the Nef proteins of SIVcpz and SIVgor, which represent the ape precursors of human immunodeficiency virus type 1 (HIV-1). To promote virus release from infected cells, pandemic HIV-1 group M strains evolved Vpu as a tetherin antagonist, while the Nef protein of less widespread HIV-1 group O strains acquired the ability to target a region adjacent to this deletion. In this study, we identified an unusual HIV-1 group O strain (RBF206) that evolved Vpu as an effective antagonist of human tetherin. While both RBF206 Vpu and Nef exert anti-tetherin activity in transient-transfection assays, mainly Vpu promotes RBF206 release in infected CD4+ T cells. Although mutations distinct from the adaptive changes observed in group M Vpus (M-Vpus) were critical for the acquisition of its anti-tetherin activity, RBF206 O-Vpu potently suppresses NF-κB activation and reduces CD4 cell surface expression. Interestingly, RBF206 Vpu counteracts tetherin in a largely species-independent manner, degrading both the long and short isoforms of human tetherin. Downmodulation of CD4, but not counteraction of tetherin, by RBF206 Vpu was dependent on the cellular ubiquitin ligase machinery. Our data present the first example of an HIV-1 group O Vpu that efficiently antagonizes human tetherin and suggest that counteraction by O-Nefs may be suboptimal.</p>
</div>
</front>
</TEI>
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<name sortKey="Sauter, Daniel" sort="Sauter, Daniel" uniqKey="Sauter D" first="Daniel" last="Sauter">Daniel Sauter</name>
<name sortKey="Starz, Kathrin" sort="Starz, Kathrin" uniqKey="Starz K" first="Kathrin" last="Starz">Kathrin Starz</name>
<name sortKey="Sturzel, Christina" sort="Sturzel, Christina" uniqKey="Sturzel C" first="Christina" last="Stürzel">Christina Stürzel</name>
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<country name="États-Unis"><noRegion><name sortKey="Bibollet Ruche, Frederic" sort="Bibollet Ruche, Frederic" uniqKey="Bibollet Ruche F" first="Frederic" last="Bibollet-Ruche">Frederic Bibollet-Ruche</name>
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<name sortKey="Plantier, Jean Christophe" sort="Plantier, Jean Christophe" uniqKey="Plantier J" first="Jean-Christophe" last="Plantier">Jean-Christophe Plantier</name>
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