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HIV-1 Vpu protein forms stable oligomers in aqueous solution via its transmembrane domain self-association.
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Involvement of a C-terminal motif in the interference of primate lentiviral Vpu proteins with CD1d-mediated antigen presentation.
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HIV-1 Nef and Vpu Interfere with L-Selectin (CD62L) Cell Surface Expression To Inhibit Adhesion and Signaling in Infected CD4+ T Lymphocytes.
J Virol. 2015 May;89(10):5687-700. doi: 10.1128/JVI.00611-15. Epub 2015 Mar 11.
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Membrane Anchoring by a C-terminal Tryptophan Enables HIV-1 Vpu to Displace Bone Marrow Stromal Antigen 2 (BST2) from Sites of Viral Assembly.
J Biol Chem. 2015 Apr 24;290(17):10919-33. doi: 10.1074/jbc.M114.630095. Epub 2015 Mar 10.
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Vpu is the main determinant for tetraspanin downregulation in HIV-1-infected cells.
J Virol. 2015 Mar;89(6):3247-55. doi: 10.1128/JVI.03719-14. Epub 2015 Jan 7.
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Nef proteins of epidemic HIV-1 group O strains antagonize human tetherin.
Cell Host Microbe. 2014 Nov 12;16(5):639-50. doi: 10.1016/j.chom.2014.10.002.
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HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors, including tetraspanins.
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Bacteria-based analysis of HIV-1 Vpu channel activity.
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HIV-1 Vpu mediated downregulation of CD155 requires alanine residues 10, 14 and 18 of the transmembrane domain.
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Genistein as antiviral drug against HIV ion channel.
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Downmodulation of CCR7 by HIV-1 Vpu results in impaired migration and chemotactic signaling within CD4⁺ T cells.
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