ArticleThe Journal of general virology2011
Analysis of the human immunodeficiency virus type 1 M group Vpu domains involved in antagonizing tetherin.
Article in The Journal of general virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- Efficient Vpu-Mediated Tetherin Antagonism by an HIV-1 Group O Strain.Journal of virology · 2017Article
- Identification of BST-2/tetherin-induced hepatitis B virus restriction and hepatocyte-specific BST-2 inactivation.Scientific reports · 2015Article
- Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly.The Journal of biological chemistry · 2015Article
- Nef proteins of epidemic HIV-1 group O strains antagonize human tetherin.Cell host & microbe · 2014Article
- Counteraction of the multifunctional restriction factor tetherin.Frontiers in microbiology · 2014Review
- Tetherin restricts herpes simplex virus 1 and is antagonized by glycoprotein M.Journal of virology · 2013Article
- Article
- The transmembrane domain of HIV-1 Vpu is sufficient to confer anti-tetherin activity to SIVcpz and SIVgor Vpu proteins: cytoplasmic determinants of Vpu function.Retrovirology · 2013Article
- Article
- Human tetherin exerts strong selection pressure on the HIV-1 group N Vpu protein.PLoS pathogens · 2012Article
- Construction of a high titer infectious HIV-1 subtype C proviral clone from South Africa.Viruses · 2012Article
- HIV-1 Group P is unable to antagonize human tetherin by Vpu, Env or Nef.Retrovirology · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Zoonosis of chimpanzee simian immunodeficiency virus cpz to humans has given rise to both pandemic (M) and non-pandemic (O, N and P) groups of human immunodeficiency virus type-1 (HIV). These lentiviruses encode accessory proteins, including Vpu, which has been shown to reduce CD4 levels on the cell surface, as well as increase virion release from the cell by antagonizing tetherin (CD317, BST2). Here, we confirm that O group Vpus (Ca9 and BCF06) are unable to counteract tetherin or downregulate the protein from the cell surface, although they are still able to reduce cell-surface CD4 levels. We hypothesize that this inability to antagonize tetherin may have contributed to O group viruses failing to achieve pandemic levels of human-to-human transmission. Characterization of chimeric O/M group Vpus and Vpu mutants demonstrate that the Vpu-tetherin interaction is complex, involving several domains. We identify specific residues within the transmembrane proximal region that, along with the transmembrane domain, are crucial for tetherin counteraction and enhanced virion release. We have also shown that the critical domains are responsible for the localization of M group Vpu to the trans-Golgi network, where it relocalizes tetherin to counteract its function. This work sheds light on the acquisition of anti-tetherin activity and the molecular details of pandemic HIV infection in humans.
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Registered trials
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